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Information on EC 2.5.1.47 - cysteine synthase
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EC Tree
2.5.1.47 cysteine synthaseIUBMB Comments
A pyridoxal-phosphate protein. Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. Not identical with EC 2.5.1.51 (beta-pyrazolylalanine synthase), EC 2.5.1.52 (L-mimosine synthase) and EC 2.5.1.53 (uracilylalanine synthase).
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Word Map
- 2.5.1.47
- h2s
- sulfur
- l-cysteine
- gsh
-
gamma-glutamyl
- acetyltransferase
- pyridoxal
-
slow-releasing
- typhimurium
- 5'-phosphate
-
gasotransmitter
-
o-acetylserinethiollyase
- nahs
- sulfite
-
gaseous
-
schiff
-
buthionine
- sulfoximine
- phytochelatins
-
assimilatory
-
plp-dependent
- desulfhydrase
-
h2s-releasing
- alpha-aminoacrylate
- thiosulfate
- oxygenase-1
- gamma-gcs
- sulphide
- dl-propargylglycine
-
transsulfuration
-
bienzyme
- 3-mercaptopyruvate
-
5'-phosphate-dependent
- beta-synthase
-
h2s-producing
-
sulfurylase
-
aldimine
-
beta-replacement
-
gamma-lyase
- sulfurtransferase
- cysb
- hydrosulfide
- biotechnology
- agriculture
- synthesis
- pharmacology
- medicine
- environmental protection
- drug development
- analysis
The enzyme appears in viruses and cellular organisms
Synonyms
gyy4137, cysteine synthase, cysteine synthetase, o-acetylserine sulfhydrylase, oastl, oas-tl, o-acetylserine(thiol)lyase, csase, o-acetylserine (thiol) lyase, oass-a, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylserine sulfhydrylase
-
-
-
-
BAbS19_I09950
CS1
CS26
CSase
CSase A
CSase B
Cys synthase complex
-
serine acetyltransferase (EC 2.3.1.30) and O-acetylserine thiol lyase reversibly form the heterooligomeric Cys synthase complex
cysK
CysK1
CysK2
CysM
Cysteine synthase
cysteine synthase A
cysteine synthase B
cysteine synthetase
-
-
-
-
DcsD
EC 4.2.99.8
-
-
formerly
-
Fn1220
lanthionine synthase
LbrCS
O -acetylserine (thiol)-lyase
O-acetyl-L-serine acetate-lyase (adding hydrogen sulfide)
-
-
-
-
O-acetyl-L-serine sulfhydrylase
O-acetyl-L-serine sulfhydrylase B
O-acetyl-L-serine sulfohydrolase
-
-
-
-
O-acetyl-L-serine(thiol)lyase
-
-
-
-
O-acetylserine (thiol) lyase
O-acetylserine (Thiol)-lyase
-
-
-
-
O-acetylserine (thiol)-lyase A
-
O-acetylserine (thiol)-lyase B
-
O-acetylserine (thiol)lyase
-
-
-
-
O-acetylserine sulfhydrylase
O-acetylserine sulfhydrylase A
O-acetylserine sulfhydrylase B
-
O-acetylserine sulfhydrylase-A
O-acetylserine sulfhydrylase-B
O-acetylserine(thiol)lyase
O-acetylserine-O-acetylhomoserine sulfhydro-lyase
-
-
-
-
O3-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase
-
OAS Shase
-
-
-
-
OAS-TL
OAS-TL A
OAS-TL B
OASS
OASS-A
OASS-B
OASTL
OASTL-A
OASTL-A1
S-sulfocysteine synthase
-
-
-
-
SSC synthase
synthase, cysteine
-
-
-
-
CSase
-
-
-
-
cysK
-
O-acetyl-L-serine sulfhydrylase
-
-
-
-
O-acetylserine sulfhydrylase
-
-
-
-
O-acetylserine sulfhydrylase
-
cysteine synthase is a multiprotein assembly formed by the pyridoxal 5'-phosphate-dependent enzyme O-acetylserine sulfhydrylase and serine acetyltransferase
O-acetylserine sulfhydrylase
-
-
O-acetylserine sulfhydrylase
-
O-acetylserine sulfhydrylase
-
O-acetylserine sulfhydrylase
-
-
O-acetylserine sulfhydrylase A
-
-
-
-
O-acetylserine sulfhydrylase A
-
O-acetylserine sulfhydrylase-A
-
O-acetylserine sulfhydrylase-B
-
O-acetylserine(thiol)lyase
-
-
-
-
OAS-TL
-
-
-
-
OASS
-
-
-
-
OASS-B
-
produced under unaerobic grwoth conditions in contrast to OASS-A
OASTL
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
mechanism
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
ping-pong bi-bi mechanism
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
mechanism interpreted in structural context, conformational changes during catalysis
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
mechanism similar to those of other pyridoxal enzymes
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
identification and spectral characterization of the external aldimine of the reaction, mechanism
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
mechanism of reverse reaction
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
model of reaction mechanism
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
geometric model of reaction, comparison isoenzyme CysK
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
ping-pong bi-bi mechanism
Escherichia coli W3110 / ATCC 27325
-
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
model of reaction mechanism
-
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-O bond cleavage
-
-
-
-
elimination
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
O3-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase
A pyridoxal-phosphate protein. Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. Not identical with EC 2.5.1.51 (beta-pyrazolylalanine synthase), EC 2.5.1.52 (L-mimosine synthase) and EC 2.5.1.53 (uracilylalanine synthase).
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CAS REGISTRY NUMBER
COMMENTARY
37290-89-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 L-cysteine
(2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid) + H2S
-
-
-
?
3-chloro-L-alanine + NaHS
L-cysteine + ?
-
beta-replacement reaction, enzyme can be induced by 3-chloro-L-alanine
-
?
5-thio-2-nitrobenzoate + O-acetyl-L-serine
acetate + ?
-
-
-
-
?
L-Cys + acetate
?
-
involved in mobilization of sulfide from cysteine for Fe-S cluster formation, significance in vivo unclear
-
-
?
L-homoserine + sulfide
?
-
1.6% of the activity with O-acetyl-L-serine
-
-
?
monofluoralanine + H2S
?
-
-
-
?
O-acetyl-L-Ser + 5-mercapto-2-nitrobenzoate
S-(3-carboxy-4-nitrophenyl)-L-cysteine + ?
-
-
-
?
O-acetyl-L-serine + H2O
pyruvate + acetate + NH3
-
-
-
?
O-acetyl-L-serine + sulfide
L-Cys + acetate
-
-
-
?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate + H+
-
-
-
-
?
O-acetyl-Ser + selenide
selenocysteine + acetate
-
maximal 40% rate of cysteine synthesis
-
?
O3-acetyl-L-serine
alpha-aminoacrylate
-
-
in absence of S2- and at 50°C, not below
-
?
O3-acetyl-L-serine + benzylmercaptan
S-benzyl-L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + cyanide
beta-cyano-L-alanine + acetate
-
-
-
?
O3-acetyl-L-serine + ethylmercaptan
S-ethyl-L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + methylmercaptan
S-methyl-L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + phenol
O-phenyl-L-serine + acetate
-
-
-
?
O3-acetyl-L-serine + phenylmercaptan
S-phenyl-L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + propylmercaptan
S-propyl-L-cysteine + acetate
-
-
-
?
chloroalanine + sulfide
cysteine + chloride
-
3-6% of the activity of the cysteine synthase reaction
-
r
chloroalanine + sulfide
cysteine + chloride
-
beta-chloroalanine, 6% of the activity with O-acetyl-L-Ser
-
-
r
chloroalanine + sulfide
cysteine + chloride
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
beta-chloroalanine, 6% of the activity with O-acetyl-L-Ser
-
-
r
cysteine + CN-
cyanoalanine + H2S
Xanthium pennsylvanicum
-
involved in cyanide metabolism during seed germination
-
-
?
L-Cys + acetate
O-acetyl-L-Ser + H2S
-
-
-
r
L-Cys + acetate
O-acetyl-L-Ser + H2S
-
equilibrium constant
-
r
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
-
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
-
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
the side reaction of the enzyme seems to contribute massively to the total H2S release of higher plants at least at higher pH values
-
-
?
L-cysteine + L-cysteine
L-lanthionine + H2S
-
preferred reaction
-
-
?
L-cysteine + L-cysteine
L-lanthionine + H2S
-
preferred reaction
-
-
?
L-cysteine + L-homocysteine
L-cystathionine + H2S
-
-
-
?
NaN3 + O-acetyl-Ser
beta-azidoalanine + sodium acetate
-
-
mutagenic
?
NaN3 + O-acetyl-Ser
beta-azidoalanine + sodium acetate
-
-
mutagenic in Salmonella typhimurium
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
-
18% of activity with sulfide
-
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
-
6.2% of the activity with sulfide, isoenzyme 2
-
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
-
2.6% and 6.8% of the activity with sulfide, isoenzyme 1 and 2, respectively
-
-
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
-
18% of activity with sulfide
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
enzyme that catalyzes the final step in cysteine biosynthesis. Cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
Entamoeba histolytica, the causative agent of human amoebiasis, is essentially anaerobic, requiring a small amount of oxygen for growth. It cannot tolerate the higher concentration of oxygen present in human tissues or blood. However, during tissue invasion it is exposed to a higher level of oxygen, leading to oxygen stress. Cysteine, which is a vital thiol in Entamoeba histolytica, plays an essential role in its oxygen-defence mechanisms. The major route of cysteine biosynthesis in this parasite is the condensation of O-acetylserine with sulfide by the de novo cysteine-biosynthetic pathway, which involves cysteine synthase (EhCS) as a key enzyme
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
yeast two-hybrid system for screening of a cDNA library of Nicotiana plumbaginifolia for clones encoding plant proteins interacting with two proteins of Escherichia coli: serine acetyltransferase (SAT, the product of cysE gene) and O-acetylserine (thiol) lyase A, also termed cysteine synthase (OASTL-A, the product of cysK gene). Two plant cDNA clones are identified when using the cysE gene as a bait
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
r
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
equilibrium constant
-
r
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
the second half of the OASS-A reaction is limited by the conformational change needed to open the active site and release the amino acid product. No quinonoid or geminal-diamine intermediates are detected. The amino acid external Schiff base of the enzyme is found to be very stable when the reaction is run in D2O
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
OASTL activity regulates not only Cys de novo synthesis but also its homeostasis
-
-
?
O-acetyl-L-Ser + isoxazolin-5-one
?
-
synthesis of precursor of neurotoxin beta-N-oxalyl-L-alpha,beta-diaminopropionic acid
-
-
?
O-acetyl-L-Ser + isoxazolin-5-one
?
-
synthesis of precursor of neurotoxin beta-N-oxalyl-L-alpha,beta-diaminopropionic acid
-
-
?
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
-
6.1% of activity with sulfide
-
?
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
-
2.2% of activity with sulfide, isoenzyme 1 and 2
-
?
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
-
2.3% and 1.6% of activity with sulfide, isoenzymes 1 and 2, respectively
-
?
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
-
2.5% of activity with sulfide
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
21.5% and 77% of activity with sulfide, isoenzymes 1 and 2, respectively
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
-
-
ir
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
4% and 1% of activity with sulfide, isoenzymes 1 and 2, respectively
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
-
-
ir
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
-
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
-
product identification uncertain
ir
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
32% of activity with sulfide
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
-
6.84% and 7.64% of activity with sulfide, isoenzymes 1 and 2, respectively
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
-
12.3% of activity with sulfide
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
-
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
the cysteine synthase complex functions as a molecular sensor system that monitors the sulfur status of the cell and controls sulfate assimilation and cysteine synthesis according to the availability of sulfate
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in synthesis of antioxidants such as glutathione during fruit development
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in glutathione formation
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
controlled by feedback inhibition, adaptively significant as sulfide removal mechanism
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
repressed during growth with sulfide or thiosulfide as sulfur source
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
key role in metabolism of S-containing amino acids
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
functions as a Cys synthase rather than as a homocysteine synthase in vivo
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
enzyme transcription repressed by L-cystine, derepressed by limiting sulfide concentrations
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in thiosulfate assimilation
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
activity varies between sulfur sources, enzyme formation regulated by L-Cys concentration
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + thiosulfate
S-sulfocysteine + sodium acetate
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
ir
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
-
-
-
-
?
O-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
residue Arg210 near the entrance of the active site and is important for O-acetyl-L-serine substrate recognition
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
Escherichia coli W3110 / ATCC 27325
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
Escherichia coli W3110 / ATCC 27325
-
residue Arg210 near the entrance of the active site and is important for O-acetyl-L-serine substrate recognition
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate. The enzyme catalyzes the reaction with O-acetyl-L-serine and hydroxyurea with 80fold lower catalytic efficiency
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate. The enzyme catalyzes the reaction with O-acetyl-L-serine and hydroxyurea with 80fold lower catalytic efficiency
-
-
?
O-acetyl-L-serine + L-homocysteine
cystathionine + acetate
-
-
-
?
O-acetyl-L-serine + L-homocysteine
cystathionine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
O-acetyl-L-serine + L-homocysteine
cystathionine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
O-acetylhomoserine + H2S
homocysteine + ?
-
not, low molecular weight enzyme
-
-
?
O-acetylhomoserine + H2S
homocysteine + ?
-
2.4% of the activity with O-acetyl-L-Ser
-
-
?
O-acetylhomoserine + H2S
homocysteine + ?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
2.4% of the activity with O-acetyl-L-Ser
-
-
?
O-diazoacetyl-L-serine + sulfide
?
-
44% of the activity with O-acetyl-Ser
-
-
?
O-diazoacetyl-L-serine + sulfide
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
44% of the activity with O-acetyl-Ser
-
-
?
O-succinyl-L-homoserine + sulfide
?
-
3.6% of the activity with O-acetyl-L-serine
-
-
?
O-succinyl-L-homoserine + sulfide
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
3.6% of the activity with O-acetyl-L-serine
-
-
?
O3-acetyl-L-serine + 2-nitro-5-thiobenzoate
?
-
-
-
-
?
O3-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
-
-
-
-
?
O3-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
in the absence of sulfide O3-acetyl-L-serine reacts with the cofactor pyridoxal 5'-phosphate to alpha-aminoacrylate intermediate
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
970% of the activity with cyanide
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.5.1.65, O-phosphoserine hydrolase
-
-
?
additional information
?
-
-
isoenzyme 1 and 2 have different substrate specificities towards various beta-substituted L-Cys
-
-
?
additional information
?
-
-
enzyme is induced in leaves exposed to salt stress. The results suggest that the plant enzyme is responding to the salt stress by inducing cysteine biosynthesis as a protection against high ion concentrations
-
-
?
additional information
?
-
-
model of a dynamic cysteine synthesis system with regulatory function
-
-
?
additional information
?
-
-
preferred state of sulfide is hydrogen sulfide
-
-
?
additional information
?
-
the mitochondrial isozyme OAS-TL C accounts for less than 5% of total OAS-TL activity
-
-
?
additional information
?
-
-
the mitochondrial isozyme OAS-TL C accounts for less than 5% of total OAS-TL activity
-
-
?
additional information
?
-
-
cysteine synthase CysB is the only isoform of physiological importance in Aspergillus nidulans. Starvation-induced cysteine synthase activity is under control of cross-pathway regulation
-
-
?
additional information
?
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
the enzyme shows H2S synthesizing activity, cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9
-
-
?
additional information
?
-
-
the enzyme shows H2S synthesizing activity, cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9
-
-
?
additional information
?
-
-
beta-substituted alanines, low activity
-
-
?
additional information
?
-
-
several nucleophiles may stimulate sulfide formation
-
-
?
additional information
?
-
-
activity of the enzyme bound to serine acetyltransferase is lower than that of the free enzyme
-
-
?
additional information
?
-
no substrate: L-serine, L-homoserine, O-acetyl-L-homoserine, L-alanine, L-homocysteine
-
-
?
additional information
?
-
-
no substrate: L-serine, O-propionyl-L-serine, L-alanine, glycine
-
-
?
additional information
?
-
-
stopped-flow fluorescence spectroscopy is used to characterize the interaction of serine acetyltransferase with OASS and in the presence of the physiological regulators cysteine and bisulfide. Cysteine synthase assembly occurs via a two-step mechanism involving rapid formation of an encounter complex between the two enzymes, followed by a slow conformational change. The conformational change likely results from the closure of the active site of OASS upon binding of the serine acetyltransferase C-terminal peptide. Bisulfide stabilizes the cysteine synthase complex mainly by decreasing the back rate of the isomerization step. Cysteine, the product of the OASS reaction and a SAT inhibitor, slightly affects the kinetics of cysteine synthase formation leading to destabilization of the complex
-
-
?
additional information
?
-
-
the binding free energy of 400 pentapeptides, MNXXI, interacting with the HiOASS-A active site using a combined docking-scoring procedure based on GOLD and HINTare examined. The free energy prediction is verified by the experimental determination of the binding affinity of 14 of these pentapeptides, selected for spanning a large range of predicted binding affinity and presenting charged, polar, or apolar residues at mutation sites
-
-
?
additional information
?
-
the binding free energy of 400 pentapeptides, MNXXI, interacting with the HiOASS-A active site using a combined docking-scoring procedure based on GOLD and HINTare examined. The free energy prediction is verified by the experimental determination of the binding affinity of 14 of these pentapeptides, selected for spanning a large range of predicted binding affinity and presenting charged, polar, or apolar residues at mutation sites
-
-
?
additional information
?
-
no substrates: serine, phosphoserine, O-succinylhomoserine, thiosulfate
-
-
?
additional information
?
-
-
no substrates: serine, phosphoserine, O-succinylhomoserine, thiosulfate
-
-
?
additional information
?
-
no synthesis of mimosine. The enzyme is specific for cysteine synthesis. The recombinant enzyme is active with or without the leader peptide
-
-
?
additional information
?
-
-
no synthesis of mimosine. The enzyme is specific for cysteine synthesis. The recombinant enzyme is active with or without the leader peptide
-
-
?
additional information
?
-
-
enzyme additionally catalyzes synthesis of mimosine, reaction of EC 2.5.1.52. The apparent kcat for Cys production is over sixfold higher than mimosine synthesis and the apparent Km is 3.7 times lower
-
-
-
additional information
?
-
enzyme additionally catalyzes synthesis of mimosine, reaction of EC 2.5.1.52. The apparent kcat for Cys production is over sixfold higher than mimosine synthesis and the apparent Km is 3.7 times lower
-
-
-
additional information
?
-
-
enzyme is unable to synthesize mimosine, reaction of EC 2.5.1.52
-
-
-
additional information
?
-
enzyme is unable to synthesize mimosine, reaction of EC 2.5.1.52
-
-
-
additional information
?
-
enzyme is specific for synthesis of cysteine, no synthesis of mimosine
-
-
-
additional information
?
-
-
enzyme is specific for synthesis of cysteine, no synthesis of mimosine
-
-
-
additional information
?
-
-
the enzyme is induced by Al3+. Cysteine synthase may be a key player during Al response/adaptation in rice
-
-
?
additional information
?
-
protein predominately catalyzes the synthesis but not the degradation of cysteine. The L-cysteine desulfhydrase reaction may be a side reaction
-
-
-
additional information
?
-
enzyme additionally catalyzes the formation of O-ureido-L-serine from O-acetyl-L-serine and hydroxyurea, reaction of EC 2.6.99.3. The kcat/Km value of DcsD for L-cysteine synthesis is 80fold higher than that for O-ureido-L-serine synthesis
-
-
?
additional information
?
-
-
enzyme additionally catalyzes the formation of O-ureido-L-serine from O-acetyl-L-serine and hydroxyurea, reaction of EC 2.6.99.3. The kcat/Km value of DcsD for L-cysteine synthesis is 80fold higher than that for O-ureido-L-serine synthesis
-
-
?
additional information
?
-
enzyme additionally catalyzes the formation of O-ureido-L-serine from O-acetyl-L-serine and hydroxyurea, reaction of EC 2.6.99.3. The kcat/Km value of DcsD for L-cysteine synthesis is 80fold higher than that for O-ureido-L-serine synthesis
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cysteine + CN-
cyanoalanine + H2S
Xanthium pennsylvanicum
-
involved in cyanide metabolism during seed germination
-
-
?
L-Cys + acetate
?
-
involved in mobilization of sulfide from cysteine for Fe-S cluster formation, significance in vivo unclear
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
the side reaction of the enzyme seems to contribute massively to the total H2S release of higher plants at least at higher pH values
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
enzyme that catalyzes the final step in cysteine biosynthesis. Cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
Entamoeba histolytica, the causative agent of human amoebiasis, is essentially anaerobic, requiring a small amount of oxygen for growth. It cannot tolerate the higher concentration of oxygen present in human tissues or blood. However, during tissue invasion it is exposed to a higher level of oxygen, leading to oxygen stress. Cysteine, which is a vital thiol in Entamoeba histolytica, plays an essential role in its oxygen-defence mechanisms. The major route of cysteine biosynthesis in this parasite is the condensation of O-acetylserine with sulfide by the de novo cysteine-biosynthetic pathway, which involves cysteine synthase (EhCS) as a key enzyme
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
OASTL activity regulates not only Cys de novo synthesis but also its homeostasis
-
-
?
O-acetyl-L-Ser + isoxazolin-5-one
?
-
synthesis of precursor of neurotoxin beta-N-oxalyl-L-alpha,beta-diaminopropionic acid
-
-
?
O-acetyl-L-Ser + isoxazolin-5-one
?
-
synthesis of precursor of neurotoxin beta-N-oxalyl-L-alpha,beta-diaminopropionic acid
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
the cysteine synthase complex functions as a molecular sensor system that monitors the sulfur status of the cell and controls sulfate assimilation and cysteine synthesis according to the availability of sulfate
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in synthesis of antioxidants such as glutathione during fruit development
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in glutathione formation
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
controlled by feedback inhibition, adaptively significant as sulfide removal mechanism
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
repressed during growth with sulfide or thiosulfide as sulfur source
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
key role in metabolism of S-containing amino acids
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
functions as a Cys synthase rather than as a homocysteine synthase in vivo
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
enzyme transcription repressed by L-cystine, derepressed by limiting sulfide concentrations
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in thiosulfate assimilation
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
activity varies between sulfur sources, enzyme formation regulated by L-Cys concentration
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
Escherichia coli W3110 / ATCC 27325
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
in the absence of sulfide O3-acetyl-L-serine reacts with the cofactor pyridoxal 5'-phosphate to alpha-aminoacrylate intermediate
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
additional information
?
-
-
enzyme is induced in leaves exposed to salt stress. The results suggest that the plant enzyme is responding to the salt stress by inducing cysteine biosynthesis as a protection against high ion concentrations
-
-
?
additional information
?
-
-
model of a dynamic cysteine synthesis system with regulatory function
-
-
?
additional information
?
-
the mitochondrial isozyme OAS-TL C accounts for less than 5% of total OAS-TL activity
-
-
?
additional information
?
-
-
the mitochondrial isozyme OAS-TL C accounts for less than 5% of total OAS-TL activity
-
-
?
additional information
?
-
-
cysteine synthase CysB is the only isoform of physiological importance in Aspergillus nidulans. Starvation-induced cysteine synthase activity is under control of cross-pathway regulation
-
-
?
additional information
?
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
the enzyme shows H2S synthesizing activity, cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9
-
-
?
additional information
?
-
-
the enzyme shows H2S synthesizing activity, cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9
-
-
?
additional information
?
-
-
stopped-flow fluorescence spectroscopy is used to characterize the interaction of serine acetyltransferase with OASS and in the presence of the physiological regulators cysteine and bisulfide. Cysteine synthase assembly occurs via a two-step mechanism involving rapid formation of an encounter complex between the two enzymes, followed by a slow conformational change. The conformational change likely results from the closure of the active site of OASS upon binding of the serine acetyltransferase C-terminal peptide. Bisulfide stabilizes the cysteine synthase complex mainly by decreasing the back rate of the isomerization step. Cysteine, the product of the OASS reaction and a SAT inhibitor, slightly affects the kinetics of cysteine synthase formation leading to destabilization of the complex
-
-
?
additional information
?
-
-
the enzyme is induced by Al3+. Cysteine synthase may be a key player during Al response/adaptation in rice
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
-
enzyme contains pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate containing catalytic sites are not equivalent
pyridoxal 5'-phosphate
-
2.1 mol per mol of dimeric enzyme
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate-binding site covalently bound, buried deeply within protein
pyridoxal 5'-phosphate
-
stoichiometry, binds to Lys, protects against inactivation by heat, urea, and trypsin, four binding sites per mol apoenzyme, association constant
pyridoxal 5'-phosphate
-
enzyme contains 1.2 pyridoxal phosphate per subunit
pyridoxal 5'-phosphate
-
1 per subunit of free enzyme, 4 per of cysteine synthase complex
pyridoxal 5'-phosphate
-
sequence alignment and site-directed mutation of the enzyme reveal that the cofactor PLP is covalently bound in Schiff base linkage with K30, as well as the two residues H150 and H168 are the crucial residues for PLP binding and stabilization
pyridoxal 5'-phosphate
-
the 31P chemical shift of the internal and external Schiff bases of pyridoxal 5'-phosphate in OASS-B are further downfield compared to OASS-A, suggesting a tighter binding of the cofactor in the B-isozyme. The chemical shift of the internal Schiff base (ISB) of OASS-B is 6.2 ppm, the highest value reported for the ISB of a PLP-dependent enzyme. Considering the similarity in the binding sites of the pyridoxal 5'-phosphate cofactor for both isozymes, torsional strain of the C5-C5' bond (O4'-C5'-C5-C4) of the Schiff base is proposed to contribute to the further downfield shift
pyridoxal 5'-phosphate
-
enzyme sites K30, H150, and H168 are crucial for cofactor binding and stabilization
pyridoxal 5'-phosphate
gives the crystals a yellow color, covalently linked to Lys58, interaction with Gly236, Ser280, Pro307, cofactor orientation at the active site and absorbance maximum change upon binding of cysteine or methionine
pyridoxal 5'-phosphate
-
R186 interacts with the cofactor
pyridoxal 5'-phosphate
-
the 5'-phosphate is tightly bound to the enzyme via a hydrogen bond to His152, one to the residues responsible for positioning of the cofactor
pyridoxal 5'-phosphate
-
tighter binding than in OASS-A, treatment with 1 mM hydroxylamine in 500 mM phosphate, pH 7.6, with 0.2 mM dithiothreitol, followed by dialysis against 100 mM phosphate, pH 7.0, with 0.2 mM dithiothreitol gerates apo-enzyme without the cofactor
pyridoxal 5'-phosphate
-
residue K51 forms a Schiff base with pyridoxal 5'-phosphate, with conserved residues N82 and S274 forming hydrogen bonds to the cofactor. Further residues predicted to orient and hold the pyridoxal 5'-phosphate in position are G186, T182, G183 and T185
pyridoxal 5'-phosphate
-
cofactor pyridoxal 5'-phosphate is linked covalently to Lys58, which is conserved in all OASS structures and is positioned in between these two domains, and highly conserved residues, such as Gly236, Ser280 and Pro307, interact with the aromatic ring of pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
dependent on, binding site structure analysis in a cleft between the N- and C-terminal domains, the phosphate group of PLP interacts with the highly conserved Gly/Thr-rich loop (G181TGGT185) and a water molecule, overview
pyridoxal 5'-phosphate
A0A1J9VES8
cofactor is highly flexible due to the active site being wide open
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2R)-1-(4-chlorobenzyl)-2-phenylcyclopropanecarboxylic acid
-
(1R,2R)-1-(4-methylbenzyl)-2-phenylcyclopropanecarboxylic acid
-
(1R,2R)-1-benzyl-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-ethyl-2-phenylcyclopropanecarboxylic acid
-
(1S,2R)-1-ethyl-2-phenylcyclopropanecarboxylic acid
-
(1S,2S)-1-(4-chlorobenzyl)-2-phenylcyclopropanecarboxylic acid
-
(1S,2S)-1-(4-methylbenzyl)-2-phenylcyclopropanecarboxylic acid
-
(1S,2S)-1-benzyl-2-phenylcyclopropanecarboxylic acid
-
(2E)-3-chloropent-2-enedioic acid
-
1,1'-(1,3-propanediyl)bis(5-benzyl-6-methylsulfanyl-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-4-one)
-
-
1,1'-(1,3-propanediyl)bis(5-ethyl-6-methylthio-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-4-one)
-
-
1,1'-(1,3-propanediyl)bis(5-methyl-6-methylthio-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-4-one)
-
-
1,3-bis(4-ethoxy-6-methyl-sulfanyl-1H-pyrazolo[3,4-d]pyrimidin-1-yl)propane
-
-
1-(2-naphthylsulfonyl)-3-phenyl-1H-pyrazolo[3,4-d]pyrimidin-4-amine
-
-
1-(4,6-dimethylsulfanyl-1H-pyrazolo[3,4-d]pyrimidin-1-yl)-3-(5-methyl-6-methylsulfanyl-4-oxo-1,5-dihydropyrazolo[3,4-d]pyrimidin-1-yl)propane
-
-
1-(4-chlorophenyl)-1H-pyrazole-5-carboxylic acid
9% inhibition at 1 microM, 56% inhibition at 1 mM
1-(4-fluorophenyl)-1H-pyrazole-5-carboxylic acid
8% inhibition at 1 microM, 95% inhibition at 1 mM; 8% inhibition at 1 microM, 95% inhibition at 1 mM
1-ethyl-4-nitro-1H-pyrazole-5-carboxylic acid
-
1-N,4-N-bis[3-(1Hbenzimidazol-2-yl) phenyl]benzene-1,4-dicarboxamide
determined as potential inhibitor via computational inhibitor screening, molecular dynamics simulation and homology modeling
1-phenyl-1H-pyrazole-5-carboxylic acid
11% inhibition at 1 microM, 65% inhibition at 1 mM
-
1-[(2,5-dichlorophenyl)sulfonyl]-3-phenyl-1Hpyrazolo[3,4-d]pyrimidine-4-amine
-
-
1-[(4-chlorophenyl)sulfonyl]-3-phenyl-1H-pyrazolo[3,4-d]pyrimidine-4-amine
-
-
1-[(4-nitrophenyl)sulfonyl]-3-phenyl-1H-pyrazolo[3,4-d]pyrimidine-4-amine
-
-
1H-pyrazole-5-carboxylic acid
9% inhibition at 1 microM, 94% inhibition at 1 mM
2,2'-(1,2,4-thiadiazole-3,5-diyldisulfanediyl)diacetic acid
-
2,2'-(5-ethyl-5-nitrodihydropyrimidine-1,3(2H,4H)-diyl)diacetic acid
-
2-phenylbutanedioic acid
-
2-[(1-methyl-1H-tetrazol-5-yl)sulfanyl]pyridine-3-carboxylic acid
-
2-[(5-methyl-1,3,4-thiadiazol-2-yl)carbamoyl]-3-nitrobenzoic acid
-
3,3'-[(phenylsulfonyl)imino]dipropanoic acid (non-preferred name)
-
3-(morpholin-4-ylmethyl)furan-2-carboxylic acid
-
3-[[(3,4-dichlorophenyl)carbamoyl]amino]benzoic acid
inhibits both isoforms CysK1 and CysK2 and O-phosphoserine sulfhydrylase CysM
3-[[([1,1'-biphenyl]-3-yl)carbamoyl]amino]benzoic acid
inhibits both isoforms CysK1 and CysK2 and O-phosphoserine sulfhydrylase CysM
4,6-bis(methylsulfanyl)-1-phthalimidopropyl-1H-pyrazolo[3,4-d]-pyrimidine
-
-
4-(2-methylphenyl)-8-nitro-2-thioxo-2,3,4,4a-tetrahydro-5H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidin-5-one
minimum inhibitory concentration against Mycobacterium tuberculosis 0.0335 mM, cytotoxicity against HEK 293T cell 3.6% at 0.025 mM
4-(4-methoxyphenyl)-8-nitro-2-thioxo-2,3,4,4a-tetrahydro-5H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidin-5-one
minimum inhibitory concentration against Mycobacterium tuberculosis 0.0321 mM, cytotoxicity against HEK 293T cell 0.2% at 0.025 mM
4-(methylsulfinyl)-2-[(phenylsulfonyl)amino]butanoic acid
-
4-hydroxy-2-[2-(1H-indol-3-yl)-2-oxoethyl]sulfanyl-1H-pyrimidin-6-one
inhibitor identified by molecular docking. Conserved residues involved in hydrogen bonding interaction include T85, S86, Q159, G87, R116, and G236. The compound displays a binding affinity of 8.05 microM and inhibits about 73% activity at 0.1 mM
4-[[(3,4-dichlorophenyl)carbamoyl]amino]-2-hydroxybenzoic acid
selective for isoform CysK1, IC50 value for isoform CysK2 above 300 microM
4-[[([1,1'-biphenyl]-3-yl)carbamoyl]amino]-2-hydroxybenzoic acid
inhibits both isoforms CysK1 and CysK2 and O-phosphoserine sulfhydrylase CysM
5-[[(3,4-dichlorophenyl)carbamoyl]amino]-2-hydroxybenzoic acid
inhibits both isoforms CysK1 and CysK2
5-[[([1,1'-biphenyl]-3-yl)carbamoyl]amino]-2-hydroxybenzoic acid
inhibits both isoforms CysK1 and CysK2 and O-phosphoserine sulfhydrylase CysM
6-(1,3,4-thiadiazol-2-ylcarbamoyl)cyclohex-3-ene-1-carboxylic acid
-
6-methyl-4,5,6,7-tetrahydro-1,2-benzoxazole-5,6-dicarboxylic acid
-
6-methyl-7-oxo-6-azabicyclo[3.2.1]oct-2-ene-2,8-dicarboxylic acid
-
6-methylsulfanyl-1-(3-phenylpropyl)-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-4-one
-
-
6-methylsulfanyl-1-phthalimidopropyl-4(pyrrolidin-1-yl)-1H-pyrazolo[3,4-d]pyrimidine
-
-
6-[(pyridin-4-ylmethyl)carbamoyl]cyclohex-3-ene-1-carboxylic acid
-
8-nitro-4-(2-nitrophenyl)-2-thioxo-2,3,4,4a-tetrahydro-5H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidin-5-one
minimum inhibitory concentration against Mycobacterium tuberculosis 0.0309 mM, cytotoxicity against HEK 293T cell 1% at 0.025 mM
8-nitro-4-[2-(trifluoromethyl)phenyl]-4,4a-dihydro-2H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidine-2,5(3H)-dione
minimum inhibitory concentration against Mycobacterium tuberculosis 0.0076 mM, cytotoxicity against HEK 293T cell 5.7% at 0.025 mM
cystine
competitive versus O-acetyl-L-serine, the cystine-binding residues are highly conserved in all OASS proteins; competitive versus O-acetyl-L-serine, the cystine-binding residues are highly conserved in all OASS proteins. Active site of CysK2cystine binding structure, overview. Cystine occupies the substrate/product binding site of the enzyme
D-cycloserine
-
82% loss of activity at 5 mM
DYVI
-
a peptide based on the C-terminus of the partner serine acetyltransferase with which the enzyme forms a complex, competitive inhibition
exophillic acid
from Exophiala sp.FKI-7082 , specific for isozyme CS1
MNDGI
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNEGI
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNENI
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNETI
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNKGI
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNKVI
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNLGI
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNLNI
pentapeptide inhibitor; wild type pentapeptide of serine acetyltransferase
MNPHI
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNVPI
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNWNI
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNYFI
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNYSI
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
N-(furan-2-ylcarbonyl)leucine
-
N-(furan-2-ylcarbonyl)phenylalanine
-
N-(thiophen-2-ylsulfonyl)valine
-
N-[(2,2-dimethyl-4,6-dioxo-1,3-dioxan-5-ylidene)methyl]glutamic acid
-
N-[(2,2-dimethyl-4,6-dioxo-1,3-dioxan-5-ylidene)methyl]leucine
-
N-[(3-carboxybicyclo[2.2.1]hept-5-en-2-yl)carbonyl]glycylglycine
-
N-{4-[(4-amino-3-phenyl-1H-pyrazolo[3,4-d]pyrimidin-1-yl)sulfonyl]phenyl}acetamide
-
-
NH2OH
-
97% loss of activity at 10 mM
pencolide
shows cysteine deprivation-dependent antiamebic activity,with 7.6 times lower IC50 in the absence of cysteine than that in the presence of cysteine; shows cysteine deprivation-dependent antiamebic activity,with 7.6 times lower IC50 in the absence of cysteine than that in the presence of cysteine
peroxynitrite
-
nitrating conditions after exposure to peroxynitrite strongly inhibit enzyme activity. Among the isoforms, cytosolic OASA1 is markedly sensitive to nitration. Nitration assays on purified recombinant OASA1 protein lead to 90% reduction of the activity due to inhibition of the enzyme. Inhibition of OASA1 activity upon nitration correlates with the identification of a modified OASA1 protein containing a 3-nitroTyr302 residue. Inhibition caused by Tyr302 nitration on OASA1 activity seems to be due to a drastically reduced O-acetylserine substrate binding to the nitrated protein, and also to reduced stabilization of the pyridoxal-5-phosphate cofactor through hydrogen bonds
serine acetyltransferase
-
serine acetyltransferase (EC 2.3.1.30) can inhibit O-acetylserine sulfhydrylase catalytic activity with a double mechanism, the competition with O-acetylserine for binding to the enzyme active site and the stabilization of a closed conformation that is less accessible to the natural substrate
-
trans-1-(4-chlorobenzyl)-2-phenylcyclopropanecarboxylic acid
-
trans-1-(4-methylbenzyl)-2-phenylcyclopropanecarboxylic acid
-
trans-1-benzyl-2-phenylcyclopropanecarboxylic acid
-
trans-1-ethyl-2-phenylcyclopropanecarboxylic acid
-
trans-1-phenethyl-2-phenylcyclopropanecarboxylic acid
-
trans-2-phenylcyclopropanecarboxylic acid
-
trichloroacetic acid
inactivation at 16.6% v/v; inactivation at 16.6% v/v
trifluoroalanine
irreversible but weak inhibitor; irreversible but weak inhibitor
xanthofulvin
from Penicillium sp. if08054; from Penicillium sp. if08054 , inhibits isozymes CS1 and CS3
[2-[3-acetyl-1-(2,2-dihydroxyethyl)-4-hydroxy-5-oxo-2,5-dihydro-1H-pyrrol-2-yl]phenyl](hydroxy)oxoammonium
-
[3-[(2-carboxy-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-en-7-yl)carbamoyl]-1-methyl-1H-pyrazol-4-yl](hydroxy)oxoammonium
-
[3-[(2-carboxypiperidin-1-yl)sulfonyl]phenyl](hydroxy)oxoammonium
-
Aminooxyacetate
-
57% and 64% inhibition at 1 mM, isoenzymes 1 and 2, respectively
cadmium chloride
-
plants grown in the presence of 0.0178 mM cadmium chloride show 141% increase in activity in leaves, and 189% increase in activity in root, respectively
cadmium chloride
-
plants grown in the presence of 0.0178 mM cadmium chloride show 150% increase in activity in leaves; plants grown in the presence of 0.0178 mM cadmium chloride show 260% increase in activity in leaves, and 222% increase in activity in root, respectively
copper sulfate
-
plants grown in the presence of 0.78 mM copper sulfate show 102% increase in activity in leaves, and 98% increase in activity in root, respectively
copper sulfate
-
plants grown in the presence of 0.78 mM copper sulfate show 20% increase in activity in leaves, and 110% increase in activity in root, respectively; plants grown in the presence of 0.78 mM copper sulfate show 56% increase in activity in leaves
hydroxylamine
-
35% and 48% inhibition at 5 mM, isoenzymes 1 and 2, respectively
hydroxylamine
-
complete inhibition at 10 mM, isoenzymes 1 and 2, 90% inhibition at 10 mM, isoenzyme 3
L-cysteine
-
not inhibitory up to 3.7 mM
lead nitrate
-
plants grown in the presence of 2.4 mM lead nitrate plus 5 mM EDTA show 197% increase in activity in leaves, and 201% increase in activity in root, respectively
lead nitrate
-
plants grown in the presence of 2.4 mM lead nitrate plus 5 mM EDTA show 176% increase in activity in leaves; plants grown in the presence of 2.4 mM lead nitrate plus 5 mM EDTA show 302% increase in activity in leaves, and 300% increase in activity in root, respectively
methionine
-
46% and 37% inhibition at 1 mM, isoenzymes 1 and 2, respectively
MNYDI
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNYDI
interaction of the inhibitory pentapeptide MNYDI with CysK OASS isozyme from Salmonella typhimurium, the MNYDI peptide interacts with the HiCysK active site mainly through H-bonds involving its C-terminal carboxylate and hydrophobic interactions involving the side chains of Ile5 and Tyr3, saturation transfer-difference NMR spectroscopy and docking study, docking simulations and molecular modelling, overview
MNYDI
interaction of the inhibitory pentapeptide MNYDI with CysK OASS isozyme from Salmonella typhimurium, the MNYDI peptide interacts with the HiCysK active site mainly through H-bonds involving its C-terminal carboxylate and hydrophobic interactions involving the side chains of Ile5 and Tyr3, saturation transfer-difference NMR spectroscopy and docking study, docking simulations and molecular modelling, overview; interaction of the inhibitory pentapeptide MNYDI with CysM OASS isozyme from Salmonella typhimurium, saturation transfer-difference NMR spectroscopy and docking study, docking simulations and molecular modelling, overview. In isozyme CysM multiple H-bond interactions are made by Asn2 side chain with S205 side chain and I206 and I209 backbone carbonyl groups
p-chloromercuribenzoate
-
14% and 4% inhibition at 1 mM, isoenzymes 1 and 2, respectively
S-sulfocysteine
-
26% loss of activity at 5 mM
Semicarbazide
-
60% loss of activity at 1 mM
sodium arsenite
-
plants grown in the presence of 0.0267 mM sodium arsenite show 109% increase in activity in leaves, and 238% increase in activity in root, respectively
sodium arsenite
-
plants grown in the presence of 0.0267 mM sodium arsenite show 108% increase in activity in leaves, and 250% increase in activity in root, respectively; plants grown in the presence of 0.0267 mM sodium arsenite show 120% increase in activity in leaves
additional information
direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis, several polypeptides based on OAS-TL C amino-acid sequence found at SAT-OASTL interaction sites are designed as probable competitors for SAT binding. After verification of the binding in a yeast two-hybrid assay, the most strongly interacting polypeptide is introduced to different cellular compartments of Arabidopsis thaliana cell via genetic transformation
-
additional information
-
direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis, several polypeptides based on OAS-TL C amino-acid sequence found at SAT-OASTL interaction sites are designed as probable competitors for SAT binding. After verification of the binding in a yeast two-hybrid assay, the most strongly interacting polypeptide is introduced to different cellular compartments of Arabidopsis thaliana cell via genetic transformation
-
additional information
identification and evaluation of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolites, high-throughput screening. Terreinol and citromycetin are poor inhibitors; identification and evaluation of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolites, high-throughput screening. Terreinol and citromycetin are poor inhibitors, no inhibition of isozyme CS3 by exophillic acid from Exophiala sp.FKI-7082, which is specific for isozyme CS1
-
additional information
identification and evaluation of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolites, high-throughput screening. Terreinol and citromycetin are poor inhibitors; identification and evaluation of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolites, high-throughput screening. Terreinol and citromycetin are poor inhibitors, no inhibition of isozyme CS3 by exophillic acid from Exophiala sp.FKI-7082, which is specific for isozyme CS1
-
additional information
-
identification and evaluation of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolites, high-throughput screening. Terreinol and citromycetin are poor inhibitors; identification and evaluation of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolites, high-throughput screening. Terreinol and citromycetin are poor inhibitors, no inhibition of isozyme CS3 by exophillic acid from Exophiala sp.FKI-7082, which is specific for isozyme CS1
-
additional information
-
enzyme inhibitor development, in silico molecular docking simulations, using the three-dimensional crystal structure of O-acetyl-L-serine sulfhydrylase enzyme complexed with cysteine and pyridoxal 5'-phosphate ligands, PDB ID 3BM5, on nine pyrazolo[3,4-d]pyrimidine molecules without linkers and nine pyrazolo[3,4-d]pyrimidine molecules with a trimethylene linker along with the reference drug metronidazole, binding structures, ligand docking and interaction analysis, detiled overview
-
additional information
CysK is competitively inhibited within the cysteine synthase complex
-
additional information
-
partial inhibition of enzyme upon complex formation with serine acetyltransferase
-
additional information
activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction
-
additional information
-
activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction
-
additional information
presence of 4% NaCl is not inhibitory
-
additional information
rational structure-guided design of nanomolar thiazolidine inhibitors of Mycobacterium tuberculosis CysK1 O-acetyl serine sulfhydrylase, discovered using the crystal structure of a CysK1-peptide inhibitor complex as template, pharmacophore modeling and in vitro screening, overview. Chemical synthesis leads to improved thiazolidine inhibitors with an IC50 value of 19 nM for the best compound, a 150fold higher potency than the natural peptide inhibitor with IC50 of 0.0029 mM
-
additional information
-
rational structure-guided design of nanomolar thiazolidine inhibitors of Mycobacterium tuberculosis CysK1 O-acetyl serine sulfhydrylase, discovered using the crystal structure of a CysK1-peptide inhibitor complex as template, pharmacophore modeling and in vitro screening, overview. Chemical synthesis leads to improved thiazolidine inhibitors with an IC50 value of 19 nM for the best compound, a 150fold higher potency than the natural peptide inhibitor with IC50 of 0.0029 mM
-
additional information
activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction
-
additional information
anions, like sulfate, significantly reduce the affinity of peptides for CysK
-
additional information
anions, like sulfate, significantly reduce the affinity of peptides for CysK
-
additional information
-
anions, like sulfate, significantly reduce the affinity of peptides for CysK
-
additional information
computational and spectroscopic approaches to rationally design, synthesize, and test a series of substituted 2-phenylcyclopropane carboxylic acids that bind to the two Salmonella typhymurium OASS isoforms at nanomolar concentrations, Kd values and binding structures, molecular modeling and docking study, overview; computational and spectroscopic approaches to rationally design, synthesize, and test a series of substituted 2-phenylcyclopropane carboxylic acids that bind to the two Salmonella typhymurium OASS isoforms at nanomolar concentrations, Kd values and binding structures, molecular modeling and docking study, overview
-
additional information
computational and spectroscopic approaches to rationally design, synthesize, and test a series of substituted 2-phenylcyclopropane carboxylic acids that bind to the two Salmonella typhymurium OASS isoforms at nanomolar concentrations, Kd values and binding structures, molecular modeling and docking study, overview; computational and spectroscopic approaches to rationally design, synthesize, and test a series of substituted 2-phenylcyclopropane carboxylic acids that bind to the two Salmonella typhymurium OASS isoforms at nanomolar concentrations, Kd values and binding structures, molecular modeling and docking study, overview
-
additional information
-
computational and spectroscopic approaches to rationally design, synthesize, and test a series of substituted 2-phenylcyclopropane carboxylic acids that bind to the two Salmonella typhymurium OASS isoforms at nanomolar concentrations, Kd values and binding structures, molecular modeling and docking study, overview; computational and spectroscopic approaches to rationally design, synthesize, and test a series of substituted 2-phenylcyclopropane carboxylic acids that bind to the two Salmonella typhymurium OASS isoforms at nanomolar concentrations, Kd values and binding structures, molecular modeling and docking study, overview
-
additional information
identification of potential inhibitors of the two isozymes A and B via a ligand- and structure-based in silico screening of a subset of the ZINC library using FLAP. The binding affinities of the most promising candidates are measured in vitro on purified O-acetylserine sulfhydrylase-A and O-acetylserine sulfhydrylase-B by a direct method that exploits the change in the cofactor fluorescence, ligand binding analysis, overview; identification of potential inhibitors of the two isozymes A and B via a ligand- and structure-based in silico screening of a subset of the ZINC library using FLAP. The binding affinities of the most promising candidates are measured in vitro on purified O-acetylserine sulfhydrylase-A and O-acetylserine sulfhydrylase-B by a direct method that exploits the change in the cofactor fluorescence, ligand binding analysis, overview
-
additional information
identification of potential inhibitors of the two isozymes A and B via a ligand- and structure-based in silico screening of a subset of the ZINC library using FLAP. The binding affinities of the most promising candidates are measured in vitro on purified O-acetylserine sulfhydrylase-A and O-acetylserine sulfhydrylase-B by a direct method that exploits the change in the cofactor fluorescence, ligand binding analysis, overview; identification of potential inhibitors of the two isozymes A and B via a ligand- and structure-based in silico screening of a subset of the ZINC library using FLAP. The binding affinities of the most promising candidates are measured in vitro on purified O-acetylserine sulfhydrylase-A and O-acetylserine sulfhydrylase-B by a direct method that exploits the change in the cofactor fluorescence, ligand binding analysis, overview
-
additional information
-
identification of potential inhibitors of the two isozymes A and B via a ligand- and structure-based in silico screening of a subset of the ZINC library using FLAP. The binding affinities of the most promising candidates are measured in vitro on purified O-acetylserine sulfhydrylase-A and O-acetylserine sulfhydrylase-B by a direct method that exploits the change in the cofactor fluorescence, ligand binding analysis, overview; identification of potential inhibitors of the two isozymes A and B via a ligand- and structure-based in silico screening of a subset of the ZINC library using FLAP. The binding affinities of the most promising candidates are measured in vitro on purified O-acetylserine sulfhydrylase-A and O-acetylserine sulfhydrylase-B by a direct method that exploits the change in the cofactor fluorescence, ligand binding analysis, overview
-
additional information
molecular dynamic simulation and inhibitor prediction of cysteine synthase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
serine acetyltransferase
CysE, each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. 20fold increase in catalytic efficiency upon binding of CysE to CysK as a result of both decreased KM for acetyl-CoA and increased kcat. Free CysE enzyme is less active and more susceptible to aggregation, inactivation and proteolysis
-
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site
-
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site
-
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site
-
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site
-
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site
-
additional information
-
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site
-
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site
-
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site
-
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site
-
additional information
-
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.018
5-thio-2-nitrobenzoate
-
mutant W50Y, pH 7.0, 20°C
0.049
5-thio-2-nitrobenzoate
-
wild-type, pH 7.0, 20°C
0.061
5-thio-2-nitrobenzoate
-
mutant W161Y, pH 7.0, 20°C
0.07
5-thio-2-nitrobenzoate
-
mutant H52A, pH 6.5
0.07
5-thio-2-nitrobenzoate
-
K120Q mutant with 9fold decrease compared to wild type, 100 mM MES, pH 6.5, 0.5 mM O3-acetyl-L-serine, 25°C
0.6
5-thio-2-nitrobenzoate
-
wild-type, pH 7.0
0.6
5-thio-2-nitrobenzoate
-
wild type, 100 mM HEPES, pH 7.0, 0.5 mM O3-acetyl-L-serine, 25°C
2.5
5-thio-2-nitrobenzoate
-
mutant H52A, pH 6.5
2.5
5-thio-2-nitrobenzoate
-
H152A mutant with 4.1fold increase compared to wild type, 100 mM MES, pH 6.5, 0.5 mM O3-acetyl-L-serine, 25°C
1.46
hydrogen sulfide
pH 7.5, 22°C, recombinant enzyme, Lineweaver-Burke model
1.85
hydrogen sulfide
pH 7.5, 22°C, recombinant enzymem, Michaelis-Menten model
3.2
hydrogen sulfide
-
isoform B, pH 7.5, 25°C, Hill equation, Hill coefficient 0.75
4.6
hydrogen sulfide
-
isoform C, pH 7.5, 25°C, Hill equation, Hill coefficient 1.05
4.7
hydrogen sulfide
-
isoform C, pH 7.5, 25°C, Michaelis-Menten kinetics
5.6
hydrogen sulfide
-
isoform A, pH 7.5, 25°C, Michaelis-Menten kinetics
6.4
hydrogen sulfide
-
isoform A, pH 7.5, 25°C, Hill equation, Hill coefficient 0.81
5
O-acetyl-L-Ser
-
free enzyme
5
O-acetyl-L-Ser
-
independent of sulfide concentration
20
O-acetyl-L-Ser
-
complex-bound enzyme
0.11
O-acetyl-L-serine
-
mutant H52A, pH 6.5
1
O-acetyl-L-serine
-
mutant H52A, pH 6.5
1
O-acetyl-L-serine
recombinant enzyme, pH 7.0, 25°C, with DTT
1.1
O-acetyl-L-serine
recombinant enzyme, pH 7.0, 25°C, with DTT
3.5
O-acetyl-L-serine
recombinant enzyme, pH 7.0, 25°C, with glutathione, GSSG
4.8
O-acetyl-L-serine
recombinant enzyme, pH 7.0, 25°C, with glutathione, GSSG
6.18
O-acetyl-L-serine
A0A1J9VES8
production of H2S, wild-type, pH 8.2, 37°C
9.01
O-acetyl-L-serine
A0A1J9VES8
production of H2S, mutant A72S, pH 8.2, 37°C
15
O-acetyl-L-serine
-
wild-type, pH 7.0
0.11
O3-acetyl-L-serine
-
H152A mutant with 136fold decrease compared to wild type, 100 mM MES, pH 6.5, 50 microM 5-thio-2-nitrobenzoate (TNB), 25°C
0.31
O3-acetyl-L-serine
-
isoform B, pH 7.5, 25°C, Michaelis-Menten kinetics
0.32
O3-acetyl-L-serine
-
isoform B, pH 7.5, 25°C, Hill equation, Hill coefficient 1.03
0.43
O3-acetyl-L-serine
-
isoform C, pH 7.5, 25°C, Michaelis-Menten kinetics
0.51
O3-acetyl-L-serine
-
isoform C, pH 7.5, 25°C, Hill equation, Hill coefficient 0.86
0.66
O3-acetyl-L-serine
-
isoform A, pH 7.5, 25°C, Hill equation, Hill coefficient 1.05
0.69
O3-acetyl-L-serine
-
isoform A, pH 7.5, 25°C, Michaelis-Menten kinetics
0.749
O3-acetyl-L-serine
-
wild-type, pH 7.0, 20°C
0.774
O3-acetyl-L-serine
-
mutant W50Y, pH 7.0, 20°C
1
O3-acetyl-L-serine
-
K120Q mutant with 15fold decrease compared to wild type, 100 mM MES, pH 6.5, 50 microM 5-thio-2-nitrobenzoate (TNB), 25°C
1.771
O3-acetyl-L-serine
-
mutant W161Y, pH 7.0, 20°C
15
O3-acetyl-L-serine
-
wild type, 100 mM HEPES, pH 7.0, 50 microM 5-thio-2-nitrobenzoate (TNB), 25°C
additional information
additional information
-
Hill numbers
-
additional information
additional information
-
cysteine-forming activity 245 times greater than beta-cyanoalanine-forming activity
-
additional information
additional information
-
positive kinetic cooperativity with respect to O-acetylserine in the presence of sulfide
-
additional information
additional information
-
activity varies between sulfur sources
-
additional information
additional information
-
not significantly altered by immobilization
-
additional information
additional information
-
HPLC method for product quantification
-
additional information
additional information
the B-isozyme has a an about 10fold lower Km for O-acetyl-L-serine than the A-isoenzyme
-
additional information
additional information
the B-isozyme has a an about 10fold lower Km for O-acetyl-L-serine than the A-isoenzyme
-
additional information
additional information
-
the B-isozyme has a an about 10fold lower Km for O-acetyl-L-serine than the A-isoenzyme
-
additional information
additional information
important role of the C-terminal residue Ile5 and the arylic moiety at P3 in dictating enzyme affinity, dissociation constant of MNYDI
-
additional information
additional information
important role of the C-terminal residue Ile5 and the arylic moiety at P3 in dictating enzyme affinity, dissociation constant of MNYDI
-
additional information
additional information
-
important role of the C-terminal residue Ile5 and the arylic moiety at P3 in dictating enzyme affinity, dissociation constant of MNYDI
-
additional information
additional information
important role of the C-terminal residue Ile5 and the arylic moiety at P3 in dictating enzyme affinity, dissociation constant of MNYDI
-
additional information
additional information
steady-state kinetics and modeling
-
additional information
additional information
-
steady-state kinetics and modeling
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.7
O-acetyl-L-serine
A0A1J9VES8
production of H2S, wild-type, pH 8.2, 37°C
0.9
O-acetyl-L-serine
A0A1J9VES8
production of H2S, mutant A72S, pH 8.2, 37°C
132
O-acetyl-L-serine
recombinant enzyme, pH 7.0, 25°C, with DTT
140
O-acetyl-L-serine
recombinant enzyme, pH 7.0, 25°C, with glutathione, GSSG
231
O-acetyl-L-serine
recombinant enzyme, pH 7.0, 25°C, with glutathione, GSSG
232
O-acetyl-L-serine
recombinant enzyme, pH 7.0, 25°C, with DTT
0.01
O3-acetyl-L-serine
-
turnover for mutant K120Q is decreased 56fold compared to wild type, 25°C, 100 mM HEPES, pH 7.0
0.06
O3-acetyl-L-serine
-
the turnover for H152A mutant is decreased 9fold compared to the wild type, 25°C, 100 mM MES, pH 6.5
0.56
O3-acetyl-L-serine
-
25°C, 100 mM HEPES, pH 7.0
0.56
O3-acetyl-L-serine
-
wild type, 25°C, 100 mM HEPES, pH 7.0
additional information
additional information
the B-isozyme has a turnover number 12.5fold higher than the A-isozyme
-
additional information
additional information
the B-isozyme has a turnover number 12.5fold higher than the A-isozyme
-
additional information
additional information
-
the B-isozyme has a turnover number 12.5fold higher than the A-isozyme
-
additional information
additional information
-
wild type and mutant exhibit almost identical values for sulfide as substrate, imidazole has no effect on the activity of wild type or H152A mutant enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
wild type and mutant exhibit almost identical values for sulfide as substrate
-
0.0219
5-thio-2-nitrobenzoate
-
H152A mutant with 43fold decrease compared to wild type, 100 mM MES, pH 6.5, 0.5 mM O3-acetyl-L-serine, 25°C
0.141
5-thio-2-nitrobenzoate
-
K120Q mutant with 6.7fold decrease compared to wild type value, 100 mM MES, pH 6.5, 0.5 mM O3-acetyl-L-serine, 25°C
0.95
5-thio-2-nitrobenzoate
-
wild type, 100 mM HEPES, pH 7.0, 0.5 mM O3-acetyl-L-serine, 25°C
10.56
L-homocysteine
A0A1J9VES8
wild-type, production of H2S, pH 8.2, 37°C
0.1
O-acetyl-L-serine
A0A1J9VES8
production of H2S, mutant A72S, pH 8.2, 37°C
0.11
O-acetyl-L-serine
A0A1J9VES8
production of H2S, wild-type, pH 8.2, 37°C
0.14
O-acetyl-L-serine
30°C, pH 8.0, cosubstrate: hydrogen sulfide
39.8
O-acetyl-L-serine
recombinant enzyme, pH 7.0, 25°C, with glutathione, GSSG
48.1
O-acetyl-L-serine
recombinant enzyme, pH 7.0, 25°C, with glutathione, GSSG
136
O-acetyl-L-serine
recombinant enzyme, pH 7.0, 25°C, with DTT
219
O-acetyl-L-serine
recombinant enzyme, pH 7.0, 25°C, with DTT
0.01
O3-acetyl-L-serine
-
K120Q mutant with 3.7fold decrease compared to wild type value, 100 mM MES, pH 6.5, 50 microM 5-thio-2-nitrobenzoate (TNB), 25°C
0.037
O3-acetyl-L-serine
-
wild type, 100 mM HEPES, pH 7.0, 50 microM 5-thio-2-nitrobenzoate (TNB), 25°C
0.51
O3-acetyl-L-serine
-
H152A mutant with 14fold increase compared to wild type, 100 mM MES, pH 6.5, 50 microM 5-thio-2-nitrobenzoate (TNB), 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.03
MNDGI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
2.27
MNEGI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
0.0387
MNENI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
3.42
MNETI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
15.2
MNKGI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
13.3
MNKVI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
0.57
MNLGI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
0.044
MNLNI
wild type serine acetyltransferase motif, 100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
7.1
MNPHI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
3.33
MNVPI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
0.0249
MNWNI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
0.0258
MNYDI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
0.191
MNYFI
100 mM HEPES, pH 8.0, 1 microM enzyme, 20°C, steady state fluorescence titration
0.0608
MNYSI
100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration
additional information
additional information
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0101
3-[[(3,4-dichlorophenyl)carbamoyl]amino]benzoic acid
Mycobacterium tuberculosis
pH not specified in the publication, temperature not specified in the publication
0.0066
3-[[([1,1'-biphenyl]-3-yl)carbamoyl]amino]benzoic acid
Mycobacterium tuberculosis
pH not specified in the publication, temperature not specified in the publication
0.0177
4-(2-methylphenyl)-8-nitro-2-thioxo-2,3,4,4a-tetrahydro-5H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidin-5-one
Mycobacterium tuberculosis
pH not specified in the publication, temperature not specified in the publication
0.0227
4-(4-methoxyphenyl)-8-nitro-2-thioxo-2,3,4,4a-tetrahydro-5H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidin-5-one
Mycobacterium tuberculosis
pH not specified in the publication, temperature not specified in the publication
0.0269
4-[[([1,1'-biphenyl]-3-yl)carbamoyl]amino]-2-hydroxybenzoic acid
Mycobacterium tuberculosis
pH not specified in the publication, temperature not specified in the publication
0.0299
5-[[(3,4-dichlorophenyl)carbamoyl]amino]-2-hydroxybenzoic acid
Mycobacterium tuberculosis
pH not specified in the publication, temperature not specified in the publication
0.0103
5-[[([1,1'-biphenyl]-3-yl)carbamoyl]amino]-2-hydroxybenzoic acid
Mycobacterium tuberculosis
pH not specified in the publication, temperature not specified in the publication
0.0303
8-nitro-4-(2-nitrophenyl)-2-thioxo-2,3,4,4a-tetrahydro-5H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidin-5-one
Mycobacterium tuberculosis
pH not specified in the publication, temperature not specified in the publication
0.0177
8-nitro-4-[2-(trifluoromethyl)phenyl]-4,4a-dihydro-2H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidine-2,5(3H)-dione
Mycobacterium tuberculosis
pH not specified in the publication, temperature not specified in the publication
0.021
deacetylkinamycin C
Entamoeba histolytica
pH 7.5, 37°C, recombinant enzyme
0.022
deacetylkinamycin C
Entamoeba histolytica
pH 7.5, 37°C, recombinant enzyme
0.49
naphthacemycin A
Entamoeba histolytica
above, pH 7.5, 37°C, recombinant enzyme
0.217
pencolide
Entamoeba histolytica
pH not specified in the publication, temperature not specified in the publication
0.233
pencolide
Entamoeba histolytica
pH not specified in the publication, temperature not specified in the publication
additional information
deoxyfrenolicin
Entamoeba histolytica
-
IC50 value 24 microg/ml, pH not specified in the publication, temperature not specified in the publication
additional information
deoxyfrenolicin
Entamoeba histolytica
IC50 value 24 microg/ml, pH not specified in the publication, temperature not specified in the publication
additional information
deoxyfrenolicin
Entamoeba histolytica
-
IC50 value 25 microg/ml, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
149
-
purified recombinant enzyme, pH 7.5, temperature not specified in the publication
180
235
substrate O-acetyl-L-serine, purified recombinant isozyme CysK1, pH 7.0, 25°C
400
412
substrate O-acetyl-L-serine, purified recombinant isozyme CysK2, pH 7.0, 25°C
additional information
additional information
-
activity modified by protein-protein interactions within cystein synthase complex
additional information
-
cysteine and methylcysteine formation of crude leaf extracts
additional information
-
activity increased during growth on cystine, as compared to growth on sulfate
additional information
-
activity buffer-dependent, substrate unstable in Tris-HCl buffer
additional information
-
apo-enzyme reconstituted with cofactor pyridoxal 5'-phosphate exhibits 81.4% enzyme activity compared to the native enzyme, 100 mM HEPES, pH 7.0, with 0.2 mM O3-acetyl-L-serine, and 0.05 5-thio-2-nitrobenzoate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.7
7.2
7.5
7.8
7.9
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
-
pH 6: about 55% of maximal activity, pH 10.0: about 40% of maximal activity
additional information
additional information
-
pH-rate profiles for wild type and H152A mutant with O3-acetyl-L-serine and 5-thio-2-nitrobenzoate as substrates are similar, 100 mM concentrations of 2-(N-morpholino)ethanesulfonic acid (MES), pH 5.5-6.5, 3-(N-morpholino)propanesulfonic acid (MOPS), pH 7.0-7.5, N-(2-hydroxyethyl)piperazine-N'-2-ethanesulfonic acid (HEPES), pH 8.0, and 3-[[tris(hydroxymethyl)]amino]propanesulfonic acid (TAPS), pH 9.0, titrated with KOH
additional information
-
pH-rate profiles for wild type and H152A mutant with O3-acetyl-L-serine and beta-chloro-L-alanine as substrates are similar, 100 mM concentrations of 2-(N-morpholino)ethanesulfonic acid (MES), pH 5.5-6.5, 3-(N-morpholino)propanesulfonic acid (MOPS), pH 7.0-7.5, N-(2-hydroxyethyl)piperazine-N'-2-ethanesulfonic acid (HEPES), pH 8.0, and 3-[[tris(hydroxymethyl)]amino]propanesulfonic acid (TAPS), pH 9.0, titrated with KOH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
25
30
37
40
50
60
80
-
synthesis of L-cystathionine and sulfhydrylation of L-Ser. Maximal for O-acetyl-L-serine sulfhydrylation at both 70°C and at 80°C
additional information
-
assay performed at room temperature
50
-
soluble enzyme, DEAE-immobilized enzyme and silica-immobilized enzyme
60
-
vinylacetate-epoxy-immobilized enzyme and vinylacetate-hydroxy-immobilized enzyme
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two isoenzymes, one with additional S-sulfocysteine synthase activity
-
-
brenda
arginine, histidine or proline starvation leads to derepression of cysteine synthase activity. In addition to CysB, the activity is shared by homocysteine synthase CysD and at least one more enzyme, possibly CysF. Starvation-induced cysteine synthase activity is under control of cross-pathway regulation
-
-
brenda
enzyme shows activities of both EC 4.2.1.22 and 2.5.1.47
A0A1J9VES8
UniProt
brenda
bifunctional cystathionine beta-synthase EC 4.2.1.22 and O-acetyl-L-serine sulfhydrylase, EC 2.5.1.47
UniProt
brenda
Lactiplantibacillus plantarum ATCC BAA-793
bifunctional cystathionine beta-synthase EC 4.2.1.22 and O-acetyl-L-serine sulfhydrylase, EC 2.5.1.47
UniProt
brenda
two isoenzymes, one with additional S-sulfocysteine synthase activity
-
-
brenda
3 isoforms, recombinant enzymes, fast increase in enzyme product in response to sulfate deprivation
-
-
brenda
isoform CysL-2, bifunctional enzyme, cf. EC 4.4.1.9
UniProt
brenda
aerobic form of enzyme forms a tight bienzyme complex in vivo with serine acetyltransferase
-
-
brenda
low molecular weight enzyme is the same protein as serine sulfhydrylase
-
-
brenda
low molecular weight enzyme, wild type and Cys auxotroph strain
-
-
brenda
-
-
-
brenda
CysK; gene cysK
SwissProt
brenda
CysM; gene cysM
SwissProt
brenda
isoform CysK
SwissProt
brenda
isoform CysM
SwissProt
brenda
isozyme OASS-A
SwissProt
brenda
isozyme OASS-B
SwissProt
brenda
one enzyme free, one associated with serine transacetylase in cysteine synthase
-
-
brenda
S-sulfocysteine synthase is identical with cysteine synthase B
-
-
brenda
isozyme OASS-A
SwissProt
brenda
isozyme OASS-B
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
A-isozyme expressed under aerobic and the B-isozyme expressed under anaerobic conditions
brenda
A-isozyme expressed under aerobic and the B-isozyme expressed under anaerobic conditions
brenda
additional information
-
enzyme activities are increased in presence of Cu, As, Cd, or Pb
brenda
-
enzyme activities are increased in presence of Cu, As, Cd, or Pb
brenda
-
root plasma membrane SO42- transporter SULTR1,2 physically interacts with the enzyme
brenda
-
in presence of metal ions As, Cd, and Pb, OASTL transcripts are increased especially in roots, where metal accumulation is maximal, while Cu produces a decrease in the transcript levels. Enzyme activities are increased in presence of Cu, As, Cd, or Pb
brenda
-
in presence of metal ions As, Cd, and Pb, OASTL transcripts are increased especially in roots, where metal accumulation is maximal, while Cu produces a decrease in the transcript levels. Enzyme activities are increased in presence of Cu, As, Cd, or Pb
brenda
expressed in roots at the vegetative growth stage, expressed in the outer cortex and the vascular cylinder in the root mature zone
brenda
-
induction of activity under stress, 0.025-0.300 mM Cd2+, 100 mM NaCl, or 0.001 mM abscisic acid
brenda
-
induction of activity under stress, 0.025-0.300 mM Cd2+, 100 mM NaCl, or 0.001 mM abscisic acid
brenda
activity peaks in young developing seed and declines thereafter
brenda
mainly expressed in developing seeds
brenda
additional information
-
isoforms OAS-TL A and B are the most abundant isoforms in all tissues analyzed. The major isoforms present in cytosol, plastids and mitochondria show significant modifications into up to seven subspecies. Specific isoforms are found to be differentially modified in the leaves, roots, stem and cell culture. Sulfur deficiency does not alter modification of enzyme proteins purified from cell culture that shows the highest complexity of modifications. However, the pattern of enzyme modification is found to be stable within an analyzed tissue
brenda
additional information
quantitative enzyme expression analyis, overview
brenda
additional information
-
quantitative enzyme expression analyis, overview
brenda
additional information
-
quantitative enzyme expression analyis, overview
-
brenda
additional information
enzyme is constitutively expressed in all tested tissues under normal growth conditions
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
presence of an active CS26 enzyme exclusively in the thylakoid lumen
brenda
additional information
-
different from cytosolic and mitochondrial enzymes, as revealed by polyclonal antibody studies, 3-5% of total activity
brenda
-
root plasma membrane SO42- transporter SULTR1,2 physically interacts with the enzyme. The domain of SULTR1,2 important for association with enzyme is called the STAS domain, located at the C-terminus of the transporter and extending from the plasma membrane into the cytoplasm. The binding of enzyme to the STAS domain negatively impacts transporter activity. In contrast, the activity of purified enzyme measured in vitro is enhanced by co-incubation with the STAS domain of SULTR1,2 but not with the analogous domain of the SO42- transporter isoform SULTR1,1. The observations suggest a regulatory model in which interactions between SULTR1,2 and enzyme coordinate internalization of SO42- with the energetic/metabolic state of plant root cells
brenda
-
serine O-acetyltransferase SAT3 and O-acetylserine sulfhydrolase can interact in plant mitochondria to form the cysteine synthase complex. Formation of the mitochondrial cysteine synthase complex might be promoted by the stabilizing effect of sulfide, by efficient export of O-acetylserine from mitochondria, or by a combination of both
brenda
additional information
the major isoforms, OAS-TL A, OAS-TL B, and OAS-TL C, catalyze the formation of Cys by combining O-acetylserine and sulfide in the cytosol, the plastids, and the mitochondria, respectively. Subcellular localization of OAS-TL proteins is more important for efficient Cys synthesis than total cellular OAS-TL activity in leaves
-
brenda
additional information
the major isoforms, OAS-TL A, OAS-TL B, and OAS-TL C, catalyze the formation of Cys by combining O-acetylserine and sulfide in the cytosol, the plastids, and the mitochondria, respectively. Subcellular localization of OAS-TL proteins is more important for efficient Cys synthesis than total cellular OAS-TL activity in leaves
-
brenda
additional information
the major isoforms, OAS-TL A, OAS-TL B, and OAS-TL C, catalyze the formation of Cys by combining O-acetylserine and sulfide in the cytosol, the plastids, and the mitochondria, respectively. Subcellular localization of OAS-TL proteins is more important for efficient Cys synthesis than total cellular OAS-TL activity in leaves
-
brenda
additional information
-
in the unicellular green alga Chlorella sorokiniana two OASTL isoforms, chloroplastic and cytosolic, occur among which the cytosolic is induced under S-deprivation, uniquely altered amounts and activities of OASTL during S-starvation as opposed to the vascular plant systems, e.g. a 17fold increase in the specific activity of enzyme OASTL
-
brenda
additional information
-
in the unicellular green alga Chlorella sorokiniana two OASTL isoforms, chloroplastic and cytosolic, occur among which the cytosolic is induced under S-deprivation, uniquely altered amounts and activities of OASTL during S-starvation as opposed to the vascular plant systems, e.g. a 17fold increase in the specific activity of enzyme OASTL
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
O-acetylserine sulfydrylase, a highly conserved pyridoxal 5'-phosphate-dependent enzyme, present in different isoforms in bacteria, plants, and nematodes, but absent in mammals
evolution
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the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the enzyme belongs to the family of fold-type II PLP-dependent enzymes. The cyanobacterium Microcystis aeruginosa PCC 7806 encodes three putative OASSs: CAO86616, CAO86589 and CAO86970, sequence comparisons
evolution
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O-acetylserine sulfydrylase, a highly conserved pyridoxal 5'-phosphate-dependent enzyme, present in different isoforms in bacteria, plants, and nematodes, but absent in mammals
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malfunction
GmOASTL4 gene is overexpressed in tobacco. Transgenic plants show markedly increased accumulation of transcripts and higher cysteine content compared with the wild-type. Upon exposure to cadmium stress, OASTL activity and cysteine levels increase significantly in transgenic plants. Cadmium accumulation and the activity of both superoxide dismutase and catalase enzymes are enhanced in transformants
malfunction
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knockout mutants demonstrate a reduction in size and show paleness, but penetrance of the growth phenotype depend on the light regime. The cs26 mutant plants also show reductions in chlorophyll content and photosynthetic activity as well as elevated glutathione levels. cs26 mutant leaves are not able to properly detoxify reactive oxygen species, which accumulate to high levels under long-day growth conditions. The transcriptional profile of the cs26 mutant reveal that the mutation has a pleiotropic effect on many cellular and metabolic processes
malfunction
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transgenic Ipomoea aquatica plants, which simultaneously express two genes encoding serine acetyltransferase and cysteine synthase are created. Transgenic plants are shown to rapidly grow and to accumulate sulfate at a high level. Upon hydroponical cultivation in the presence of 200 mM cadmium for 7 days, two transgenic lines (SR1 and SR2) accumulate 2- to 4fold higher levels of cysteine and glutathione than the wild type control plants. When plantlets are exposed to 100 mM cadmium for 30 days, wild type and transgenic SR2 plantlets die, whereas transgenic SR1 exhibit a 1.7fold increase in total biomass in comparison with the initial weight at day-0 of cadmium treatment
malfunction
the inhibition of cysteine biosynthesis in prokaryotes and protozoa is proposed for the development of antibiotics
malfunction
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mutation of cysM causes increased sensitivity of Staphylococcus (S.) aureus to tellurite (15fold), hydrogen peroxide (45fold), acid (30fold after 4h at pH 2.0), and diamide (but not methyl viologen) and also significantly reduces the ability to recover from starvation in amino acid- or phosphate-limiting conditions. A cysM knockout mutant grows poorly in cysteine-limiting conditions
malfunction
Cys can be supplied by the mother plant for the development of female gametophytes lacking OAS-TL activity. In contrast, the presence of at least one functional OAS-TL isoform is essential in the male gametophyte. Only the absence of both isozymes OAS-TL A and OAS-TL C results in a decreased incorporation of sulfur and the carbon/nitrogen backbone into thiols, which also causes lower thiol steady-state levels. A segregation pattern can only be explained by a gamete-lethal phenotype of the oastlABC triple mutant. Phenotypes of mutants in the generative phase of the life cycle, overview
malfunction
cysl-2 mutant phenotype, overview. The cysl-2 mutant has a reduced rate of enzymatic H2S synthesis from the added substrates L-cysteine and is marked by a decline in reproductive output compared to wild-type worms. Body area and length are significantly lower in cysl-2 compared to age-matched wild type worms, and GYY4137 treatment effectively rescues this phenotype. Lifespan is reduced in cysl-2 compared to wild-type and the addition of GYY4137 reverses this effect and increases the median survival of cysl-2
malfunction
deletion of the C-terminal Ile, or substitution with Ala or Glu, in CysE consistently impairs complex formation with CysK
malfunction
direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis. OAS-TL C loss-of-function mutant shows a retarded growth phenotype, conversely to the loss-of-function mutants for OAS-TL A and OAS-TL B
malfunction
lack of a functional isozyme OASTL-A1 results in enhanced disease susceptibility against infection with virulent and non-virulent Pseudomonas syringae pv. tomato DC3000 strains. Reduction of the OASTL activity of the old3-1 protein in vitro causes autonecrosis in specific Arabidopsis accessions, association of an effector triggered-like immune response and metabolic disorder with with auto-necrosis in old3 mutants. A negative epistatic interaction with the old3-1 mutation is not linked to reduced cysteine biosynthesis. Mutations in O-acetylserine (thiol) lyase regulate innate immune responses and disease susceptibility
malfunction
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mutation of cysM causes increased sensitivity of Staphylococcus (S.) aureus to tellurite (15fold), hydrogen peroxide (45fold), acid (30fold after 4h at pH 2.0), and diamide (but not methyl viologen) and also significantly reduces the ability to recover from starvation in amino acid- or phosphate-limiting conditions. A cysM knockout mutant grows poorly in cysteine-limiting conditions
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metabolism
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catalyzes the final step of the L-cysteine biosynthesis
metabolism
biosynthesis of cysteine is one of the fundamental processes in plants providing the reduced sulfur for cell metabolism. It is accomplished by the sequential action of two enzymes, serine acetyltransferase and O-acetylserine (thiol) lyase (OAS-TL). Together they constitute the hetero-oligomeric cysteine synthase (CS) complex through specific protein-protein interactions influencing the rate of cysteine production. The enzyme activity and level of thiols are not influenced by PEP4 expression. Increased serine acetyltransferase activity, but not O-acetylserine (thiol) lyase activity is an efficient trigger for enhanced cysteine synthesis in planta
metabolism
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the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview
metabolism
the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview
metabolism
the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview
metabolism
the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview
metabolism
the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview
metabolism
the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview
metabolism
the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview
metabolism
the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview
metabolism
the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview
metabolism
the enzyme catalyzes the final reaction of cysteine biosynthesis. Biological roles of known CysK complexes in the context of cysteine metabolism, overview
metabolism
the enzyme catalyzes the last step of cysteine biosynthesis. Cysteine is a building block for several biomolecules that are crucial for living organisms
metabolism
the enzyme is part of the sulfur assimilatory de novo L-cysteine biosynthetic pathway, that is essential for various cellular activities, including the proliferation and anti-oxidative defense of Entamoeba histolytica
metabolism
the O-acetylserine sulfhydrylase catalyzes the final step of cysteine biosynthesis from O-acetylserine and inorganic sulfide, negative feedback regulation of the pathway. Autoinhibition by cystine might be a universal mechanism of cysteine biosynthesis pathway
metabolism
the O-acetylserine sulfhydrylase catalyzes the final step of cysteine biosynthesis from O-acetylserine and inorganic sulfide, negative feedback regulation of the pathway. Autoinhibition by cystine might be a universal mechanism of cysteine biosynthesis pathway, redox-dependent autoregulation
metabolism
the subcellular compartmentation of Cys precursor formation is a remarkable feature of Cys synthesis in higher plants that implies a high degree of regulation between the participating compartments. Contribution of additional OAS-TL-like proteins to Cys synthesis, overview
metabolism
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the enzyme catalyzes the last step of cysteine biosynthesis. Cysteine is a building block for several biomolecules that are crucial for living organisms
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metabolism
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catalyzes the final step of the L-cysteine biosynthesis
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physiological function
cysteine auxotrophic mutant Escherichia coli NK3 transformed with GmOAS-TL1 grow in the M9 minimal medium in the absence of cysteine
physiological function
cysteine auxotrophic mutant Escherichia coli NK3 transformed with GmOAS-TL2 does not grow in the M9 minimal medium in the absence of cysteine
physiological function
cysteine auxotrophic mutant Escherichia coli NK3 transformed with GmOAS-TL3 grow in the M9 minimal medium in the absence of cysteine
physiological function
cysteine auxotrophic mutant Escherichia coli NK3 transformed with GmOAS-TL4 grow in the M9 minimal medium in the absence of cysteine
physiological function
cysteine auxotrophic mutant Escherichia coli NK3 transformed with GmOAS-TL6 grow in the M9 minimal medium in the absence of cysteine
physiological function
cysteine auxotrophic mutant Escherichia coli NK3 transformed with GmOAS-TL7 does not grow in the M9 minimal medium in the absence of cysteine
physiological function
product cysteine plays an important role in the antioxidative defense mechanisms of the human parasite
physiological function
activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction
physiological function
activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction
physiological function
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cysteine synthase complex CSC is comprised of the two enzymes that catalyze the final steps in cysteine biosynthesis: serine O-acetyltransferase, EC 2.3.1.30, which produces O-acetyl-L-serine, and O-acetyl-L-serine sulfhydrylase, EC 2.5.1.47, which converts it to cysteine. The system exhibits a contact-induced inactivation of half of each biomolecule, and exhibits a mechanism in which serine O-acetyltransferase interacts with O-acetyl-L-serine sulfhydrylase in a nonallosteric interaction involving its C-terminus. This early docking event appears to fasten the proteins in close proximity. The complex passes through at least three stable conformations in achieving its most stable configuration. Binding of a serine O-acetyltransferase C-terminal peptide is monophasic, and binding at one O-acetyl-L-serine sulfhydrylase active site does not prevent, or otherwise influence, binding at the second. The rate constants governing the first phase of the serine O-acetyltransferase binding reaction are remarkably similar to those for the binding of peptide, suggesting that early docking of serine O-acetyltransferase occurs primarily through the its C-terminus. The inability of the peptide to either induce isomerization or close the distal site suggests that serine O-acetyltransferase structure beyond its C-terminus is required to engage in isomerization and that closure of the unoccupied O-acetyl-L-serine sulfhydrylase active site may be coupled to the one or more isomerizations
physiological function
enzyme is able to complement the cysteine auxotrophy of an Escherichia coli cysMK mutant
physiological function
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loss of CS26 function results in dramatic phenotypic changes, which are dependent on the light treatment. Under long-day growth conditions, the photosynthetic characterization, based on substomatal CO2 concentrations and CO2 concentration in the chloroplast curves, reveals significant reductions in most of the photosynthetic parameters for cs26, which are unchanged under short-day growth conditions. These parameters include net CO2 assimilation rate, mesophyll conductance, and mitochondrial respiration at darkness. Mutant cs26 under long-day growth conditions requires more absorbed quanta per driven electron flux and fixed CO2. In cs26 plants, the excess electrons that are not used in photochemical reactions may form reactive oxygen species
physiological function
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root plasma membrane SO42- transporter SULTR1,2 physically interacts with the enzyme. The domain of SULTR1,2 important for association with enzyme is called the STAS domain, located at the C-terminus of the transporter and extending from the plasma membrane into the cytoplasm. The binding of enzyme to the STAS domain negatively impacts transporter activity. In contrast, the activity of purified enzyme measured in vitro is enhanced by co-incubation with the STAS domain of SULTR1,2 but not with the analogous domain of the SO42- transporter isoform SULTR1,1. The observations suggest a regulatory model in which interactions between SULTR1,2 and enzyme coordinate internalization of SO42- with the energetic/metabolic state of plant root cells
physiological function
S-sulfocysteine activity of enzyme is essential for the proper photosynthetic performance of the chloroplast under long-day growth conditions. Results suggest that S-sulfocysteine synthase functions as a protein sensor to detect the accumulation of thiosulfate as a result of the inadequate detoxification of reactive oxygen species generated under conditions of excess light to produce the S-sulfocysteine molecule that triggers protection mechanisms of the photosynthetic apparatus
physiological function
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the enzyme's active site has two access sites. Binding of the enzyme to the C-terminal tail of serine O-acetyltransferase leads to loss of activity due to reduction in ligand accessibility of the second, unoccupied active site. The observed dynamics of the gates show allosteric closure of the unoccupied active site of the enzyme in the cysteine synthase complex, which can hinder substrate binding, abolishing its turnover to cysteine
physiological function
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the mitochondrial cysteine synthase complex CSC acts as a sensor that regulates the level of serine O-acetyltransferase activity in response to sulfur supply and cysteine demand
physiological function
beside the biosynthesis of cysteine, enzyme OASS exerts a series of moonlighting activities in bacteria, such as transcriptional regulation, contact-dependent growth inhibition, swarming motility, and induction of antibiotic resistance
physiological function
besides a role of OAST-A1 in cysteine biosynthesis, the enzyme is involved in regulation of plant immunity
physiological function
biosynthesis of cysteine is one of the fundamental processes in plants providing the reduced sulfur for cell metabolism. It is accomplished by the sequential action of two enzymes, serine acetyltransferase (SAT) and O-acetylserine (thiol) lyase (OAS-TL). Together they constitute the hetero-oligomeric cysteine synthase (CS) complex through specific proteinprotein interactions influencing the rate of cysteine production. The function of the complex formation is not metabolic channeling, but sensing the sulfur status of the cell to properly adjust the sulfur homeostasis. Whereas OAS-TL is only active outside the CS complex, SAT is strongly activated by association with OAS-TL. Mitochondrial isozyme OAS-TL C has an additional function besides cysteine synthesis, regulatory function when complexed with serine acetyltransferase. The formation of the CS complex is also important because of the inhibition of the free serine acetyltransferase by cysteine
physiological function
CysK influences transcription in Caenorhabditis elegans. The enzyme from Caenorhabditis elegans interacts with EGL-9 in regulation of O2-dependent behavioral plasticity
physiological function
enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK
physiological function
enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK
physiological function
enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK
physiological function
enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK
physiological function
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enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. CysK influences transcription in Gram-positive bacteria. The enzyme from Staphylococcus aureus interacts with CymR in transcription repression
physiological function
enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. Regulatory function of CysK/CysE interaction in plants, overview
physiological function
enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. Regulatory function of CysK/CysE interaction in plants, overview. Productive cysteine biosynthesis requires a high CysK to CysE ratio
physiological function
enzyme CysK is organized in a complex with serine acetyltransferase (CysE), which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. CysK also activates an antibacterial nuclease toxin produced by uropathogenic Escherichia coli. Role for CysK during bacterial contact-dependent growth inhibition involving the CDI system from uropathogenic Escherichi coli, overview. CysK-binding provides a mechanism to protect the bacterial CysE from cold-inactivation and proteolysis. Escherichia coli CysK acts as a so-called permissive factor to activate an antibacterial contact-dependent growth inhibition (CDI) toxin, and interacts with CdiA-CTUPEC536 in toxin activation
physiological function
enzyme CysK is organized in a complex with serine acetyltransferase (CysE), which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. CysK influences transcription in Gram-positive bacteria. In Bacillus subtilis, CysK modulates the affinity of an Rrf2-type transcription factor for its operator sequences, thereby regulating expression of the cysteine regulon. The enzyme from Bacillus subtilis interacts with CymR in transcription repression. CdiA-CT toxins are activated by CysK, also from other species
physiological function
O-acetylserine sulfhydrylase plays a key role in the adaptation of bacteria to the host environment, in the defense mechanisms to oxidative stress and in antibiotic resistance
physiological function
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occurrence of the regulatory cysteine synthase complex in microalgae. In plants and also in bacteria, enzyme OASTL is catalytically inactive in the cysteine synthase complex but becomes fully active upon dissociation from the complex realized by O-acetylserine
physiological function
the bifunctional enzyme, encoded by gene K10H10.2, or cysl-2, shows cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9. It has been described as a hypoxia inducible factor (HIF) target. The enzyme regulates the mRNA expression of aging-associated and stress-related genes in wild-type Caenorhabditis elegans. Enzyme treatment protects the wild-type nematodes against oxidative, endoplasmic reticulum stress, and thermal stressors but not cadmium-induced metallic stress. The enzyme is active in vitro and in vivo and protects against lipopolysaccharide-induced inflammation. GYY4137 induces longevity and stress resistance, mechanism of action via induction of T24B8.5 and altered transcriptional control of SKN-1
physiological function
the major isoforms, OAS-TL A, OAS-TL B, and OAS-TL C, catalyze the formation of Cys by combining O-acetylserine and sulfide in the cytosol, the plastids, and the mitochondria, respectively. Subcellular localization of OAS-TL proteins is more important for efficient Cys synthesis than total cellular OAS-TL activity in leaves
physiological function
tree legume Leucaena contains a toxic, nonprotein amino acid, mimosine, which is not formed by the enzyme O-acetylserine (thiol) lyase, OAS-TL
physiological function
upregulation of cysteine synthase and cystathionine beta-synthase contributes to Leishmania braziliensis survival under oxidative stress. Ability of Leishmania braziliensis promastigotes and amastigotes overexpressing the enzyme to resist oxidative stress, which is significantly enhanced compared to that of nontransfected cells, resulting in a phenotype far more resistant to treatment with the pentavalent form of sodium stibogluconate in vitro
physiological function
cyclophilin 20-3, 2-cysteine peroxiredoxin and cysteine synthase form a redox-sensitive module. The interference of the module is accompanied with disturbance of carbohydrate, sulfur and nitrogen metabolism, and also citric acid cycle intermediates. Serine acetyltransferase2-1 and OASB appear to play antagonistic functions in sulfur metabolism, and also in nitrogen metabolism
physiological function
knockout of OASTL-A1 leads to significantly lower levels of cysteine, glutathione, and phytochelatins in roots and increased sensitivity to arsenate stress. The knockout reduces As accumulation in the roots, but increases As accumulation in shoots. OASTL-A1 is able to complement an Escherichia coli cysteine synthase-deficient mutant
physiological function
over-expression of CS1 in Arabidopsis results in the enhanced biosynthesis of glutathione, which allows plants to tolerate cadmium stress
physiological function
overexpression of cysteine synthase in amphotericin B (Amp B) sensitive strain S1-OE modulates resistance towards oxidative stress and drug pressure. Antioxidant enzyme activities are upregulated in S1-OE parasites and these parasites alleviate intracellular reactive oxygen species efficiently by maintaining the reduced thiol pool. The Amp B sensitive strain shows higher levels of reactive oxygen species which is positively correlated with the protein carbonylation levels and negatively correlated with cell viability. Cysteine synthase overexpression also augments the ROS-primed induction of cysteine synthase-GFP as well as endogenous cysteine synthase and thiol pathway proteins in Leishmania donovani parasites. The expression of cysteine synthase is upregulated in Amp B resistant isolates and during infective stationary stages of growth. Cysteine synthase overexpression enhances the infectivity of Leishmania donovani parasites
physiological function
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overexpression of OASS does not affect the nodule number, but negatively impacts plant growth. Levels of cysteine, glutathione, and homoglutathione nearly double in OASS overexpressing nodules when compared to control nodules. Several metabolites related to serine, aspartate, glutamate, and branched-chain amino acid pathways are significantly elevated in OASS overexpressing nodules. Flavonoid levels of the OASS overexpressing nodules are mostly reduced
physiological function
parental infection by Pseudomonas vranovensis results in increased expression of the cysteine synthases CysL-1 and CysL-2 and the regulator of hypoxia inducible factor Rhy-1 in progeny, and these three genes are required for adaptation to Pseudomonas vranovensis
physiological function
serine acetyltransferase CysE is activated when bound to O-acetylserine sulfhydrylase CysK. CysE activation results from the release of substrate inhibition. Feedback inhibition of CysE by L-Cys is also relieved in the bacterial cysteine synthase complex
physiological function
the binding interaction of CdiA-CT toxin from uropathogenic Escherichia coli 536 with CysK mimics the cysteine synthase complex of CysK:CysE. The C-terminal tails of CysE and CdiA-CT each insert into the CysK active-site cleft to anchor the respective complexes. The dissociation constant for CysK:CdiA-CT is comparable to that of the Escherichia coli cysteine synthase complex, and both complexes bind through a two-step mechanism with a slow isomerization phase after the initial encounter. CdiA-CT can effectively displace CysE from pre-formed cysteine synthase complexes, enabling toxin activation even in the presence of excess competing CysE
physiological function
when expressed in tobacco plants, total O-acetylserine(thiol)lyase activity in tobacco leaves is reduced. Isoform CSaseLP binds to isoform CSaseA. The O-acetylserine(thiol)lyase activity of the copurified CSaseA is reduced compared with the activity of CSaseA that is purified on its own, CSaseLP negatively regulates cysteine biosynthesis in tobacco plants
physiological function
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upregulation of cysteine synthase and cystathionine beta-synthase contributes to Leishmania braziliensis survival under oxidative stress. Ability of Leishmania braziliensis promastigotes and amastigotes overexpressing the enzyme to resist oxidative stress, which is significantly enhanced compared to that of nontransfected cells, resulting in a phenotype far more resistant to treatment with the pentavalent form of sodium stibogluconate in vitro
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physiological function
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occurrence of the regulatory cysteine synthase complex in microalgae. In plants and also in bacteria, enzyme OASTL is catalytically inactive in the cysteine synthase complex but becomes fully active upon dissociation from the complex realized by O-acetylserine
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physiological function
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beside the biosynthesis of cysteine, enzyme OASS exerts a series of moonlighting activities in bacteria, such as transcriptional regulation, contact-dependent growth inhibition, swarming motility, and induction of antibiotic resistance
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physiological function
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serine acetyltransferase CysE is activated when bound to O-acetylserine sulfhydrylase CysK. CysE activation results from the release of substrate inhibition. Feedback inhibition of CysE by L-Cys is also relieved in the bacterial cysteine synthase complex
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physiological function
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the binding interaction of CdiA-CT toxin from uropathogenic Escherichia coli 536 with CysK mimics the cysteine synthase complex of CysK:CysE. The C-terminal tails of CysE and CdiA-CT each insert into the CysK active-site cleft to anchor the respective complexes. The dissociation constant for CysK:CdiA-CT is comparable to that of the Escherichia coli cysteine synthase complex, and both complexes bind through a two-step mechanism with a slow isomerization phase after the initial encounter. CdiA-CT can effectively displace CysE from pre-formed cysteine synthase complexes, enabling toxin activation even in the presence of excess competing CysE
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additional information
auto-necrosis depends on recognition of peronospora parasitica 1 (RPP1)-like disease resistance R gene(s) from an evolutionarily divergent R gene cluster that is present in Ler-0 but not the reference accession Col-0
additional information
computational modeling is used to build a model of the Arabidopsis thaliana mitochondrial cysteine synthase complex, overview. Direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis, several polypeptides based on OAS-TL C amino-acid sequence found at SAT-OASTL interaction sites are designed as probable competitors for SAT binding. After verification of the binding in a yeast two-hybrid assay, the most strongly interacting polypeptide is introduced to different cellular compartments of Arabidopsis thaliana cell via genetic transformation
additional information
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computational modeling is used to build a model of the Arabidopsis thaliana mitochondrial cysteine synthase complex, overview. Direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis, several polypeptides based on OAS-TL C amino-acid sequence found at SAT-OASTL interaction sites are designed as probable competitors for SAT binding. After verification of the binding in a yeast two-hybrid assay, the most strongly interacting polypeptide is introduced to different cellular compartments of Arabidopsis thaliana cell via genetic transformation
additional information
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each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific
additional information
-
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific, interaction analysis and binding structure
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific, interaction analysis and binding structure. Negative cooperativity with decapeptide binding to AtCysK
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific, the C-terminal Ile (residue P4) is fundamental for the CysE/CysK binding interaction
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific. The P4 Ile residue accounts for about 80% of total binding energy. The P2 and P3 positions account for about 10% each, and the P1 residue negatively impacts binding, interaction analysis
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific. The P4 Ile residue accounts for about 80% of total binding energy. The P2 and P3 positions account for about 10% each, and the P1 residue negatively impacts binding, interaction analysis. No negative cooperativity
additional information
enzyme structure homology modeling, three-dimensional structure, overview
additional information
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intramolecular electrostatic interaction of enzyme OASS-B, overview
additional information
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the enzyme has a CBS-ike structure and a Rhodanese homology domain in the C-terminus, structure homology modeling
additional information
three-dimensional structure comparisons of isozymes CysK1 and CysK2, overview
additional information
three-dimensional structure comparisons of isozymes CysK1 and CysK2, overview
additional information
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three-dimensional structure comparisons of isozymes CysK1 and CysK2, overview
additional information
Escherichia coli W3110 / ATCC 27325
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intramolecular electrostatic interaction of enzyme OASS-B, overview
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CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1390000
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cysteine synthetase complex, sedimentation equilibrium
26000
29000
309000
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cysteine synthetase complex, sedimentation equilibrium
32000
34000
35000
36000
40000
51000
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4 * 51000, SDS-PAGE, association does not require disulfide linkage
52000
55000
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cysteine synthase B, gel filtration
56000
58000
60000
63000
64000
65000
66000
68000
70000
96000
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wild type strain, low molecular weight enzyme, sedimentation equilibrium
68000
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free enzyme, sedimentation equilibrium
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
tetramer
additional information
?
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x * 33800, chloroplast isozyme OASTL, SDS-PAGE, x * 31900, cytosolic isozyme OASTL, SDS-PAGE
?
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x * 33800, chloroplast isozyme OASTL, SDS-PAGE, x * 31900, cytosolic isozyme OASTL, SDS-PAGE
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?
x * 40000, recombinant His-tagged enzyme, SDS-PAGE, x * 34000, about, sequence calculation of untagged enzyme
dimer
2 * ?, determined by molecular replacement of crystal structure
dimer
x * 34500, calculated from sequence, x * 38000, SDS-PAGE of His-tagged recombinant protein
tetramer
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4 * 51000, SDS-PAGE, association does not require disulfide linkage
tetramer
both in solution and in a crystalline state, crystallization data
tetramer
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both in solution and in a crystalline state, crystallization data
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additional information
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two dimeric enzyme molecules form complex with tetrameric serine acetyltransferase, complex does not dissociate during catalysis
additional information
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in the complex between serine acetyltransferase and O-acetylserine sulfhydrolase, the C-terminal C10 peptide of serine acetyltransferase binds to the O-acetylserine sulfhydrolase homodimer in a 2:1 complex. Interaction between O-acetylserine sulfhydrolase and C10 peptide is tight over a range of temperature from 10°C to 35°C and NaCl concentrations from 0.02 M to 1.3 M. Binding displays negative cooperativity at higher temperatures, and the enthalpy of interaction has a significant temperature dependence. Hydrophobic interactions drive the formation of the O-acetylserine sulfhydrolase-C10 peptide complex
additional information
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isoenzymes have different cysteine and methionine content
additional information
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OASS-B does not form a complex with Escherichia coli serine acetyltransferase (SAT, EC 2.3.1.30)
additional information
a cysteine synthase complex is formed by association of serine O-acetyltransferase (SAT) and O-acetylserine sulfhydrylase (OASS). Biophysical examination cysteine synthase complex by gel filtration and sedimentation ultracentrifugation indicates that this assembly consists of a single serine O-trimer and three OASS dimers
additional information
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a cysteine synthase complex is formed by association of serine O-acetyltransferase (SAT) and O-acetylserine sulfhydrylase (OASS). Biophysical examination cysteine synthase complex by gel filtration and sedimentation ultracentrifugation indicates that this assembly consists of a single serine O-trimer and three OASS dimers
additional information
serine O-acetyltransferase and cysteine synthase form stable complexes containing two serine O-acetyltransferase trimers and two cysteine synthase dimers
additional information
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serine O-acetyltransferase and cysteine synthase form stable complexes containing two serine O-acetyltransferase trimers and two cysteine synthase dimers
additional information
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cysteine synthase complex contains 2 mol O-acetylserine sulfhydrylase per mol serine-O-transacetylase
additional information
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serine acetyltransferase (SAT, EC 2.3.1.30) and O-acetylserine thiol lyase reversibly form the heterooligomeric Cys synthase complex. SAT from Arabidopsis thaliana expressed in tobacco interacts with endogenous tobacco OAS-TL
additional information
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amino acid analysis, one sulfhydryl group per subunit, essential for restoration of native subunit structure
additional information
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three-dimensional model of enzyme structure, catalytic sites
additional information
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amino acid analysis, N-terminal amino acid is serine
additional information
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amino acid analysis, N-terminal amino acid is serine
additional information
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at least tetramer, equilibrium between aggregated and disintegrated cysteine synthetase complex can be shifted by various effectors, has consequences for enzyme function, model of structural-functional relationships
additional information
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isoenzyme 1', N-terminal amino acid sequence differs from those of enzymes one, two, and three
additional information
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all isoforms, but particularly isoenzyme 2 can form cysteine synthetase complex with serine acetyltransferase, as revealed by polyclonal antibody studies
additional information
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monomer is composed of 15 helices and 9 beta-strands, it consists of two domains A and B and has a phosphate ligand bound to each domain
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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isoforms OAS-TL A and B are the most abundant isoforms in all tissues analyzed. The major isoforms present in cytosol, plastids and mitochondria show significant modifications into up to seven subspecies. Specific isoforms are found to be differentially modified in the leaves, roots, stem and cell culture. Sulfur deficiency does not alter modification of enzyme proteins purified from cell culture that shows the highest complexity of modifications. However, the pattern of enzyme modification is found to be stable within an analyzed tissue
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of the enzyme without acetate, the complex formed by the K127A mutant with the external Schiff base of pyridoxal 5'-phosphate with O-phosphoserine, and the complex formed by the K127A mutant with the external Schiff base of pyridoxal 5'-phosphate with O-acetylserine, to 2.1 A resolution. No significant difference is seen in the overall structure between the free and complexed forms of the enzyme. The side chains of T152, S153, and Q224 interact with the carboxylate of the substrate. The position of R297 is significantly unchanged in the complex of the K127A mutant with the external Schiff base, allowing enough space for an interaction with O-phosphoserine. The positively charged environment around the entrance of the active site including S153 and R297 is important for accepting negatively charged substrates
construction of a model of the cysteine synthase complex composed of the enzymes serine-acetyl-transferase SAT and O-acetyl-serine-(thiol)-lyase OAS-TL. Binding energy calculations suggest that, consistent with experiments, a ratio of two OAS-TL dimers to one SAT hexamer is likely
native protein and mutant K46A with pyridoxal 5-phosphate and methionine covalently linked as an external aldimine
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to elucidate the structural basis of proteinprotein interactions in the plant Cys synthase complex, the crystal structure of Arabidopsis thaliana O-acetylserine sulfhydrylase bound with a peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase (C10 peptide) is determiend at 2.9 A resolution
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native enzyme and mutant Q96A/Y125A, to 1.54 and 0.97 A resolution, respectively. OASS does not interact with its cognate serine acetyltransferase C-terminal tail. Crystal structures show that residues Gln96 and Tyr125 occupy the active-site pocket and interfere with the entry of the serine acetyltransferase C-terminal tail
analysis of the three-dimensional crystal structure of O-acetyl-L-serine sulfhydrylase enzyme complexed with cysteine and pyridoxal 5'-phosphate ligands, PDB ID 3BM5, determined by X-ray crystallography
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hanging-drop vapour-diffusion method, crystals belong to the tetragonal space group P4(1), with unit cell parameters a = 80.3, b = 80.3, c = 112.2 A, two molecules per asymmetric unit and a complete data set is collected to a resolution of 1.86 A
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native and in complex with its product L-cysteine, 50 mM Tris buffer, pH 8.0, with 150 mM NaCl, hanging drop method at 16°C, 2.3 M ammonium sulfate as precipitant for the complex with 5 mM cysteine in 100 mM Tris, pH 7.2, with increasing glycerol concentrations, diffraction data collection at -173°C
native protein at 1.86 A resolution, in complex with product cysteine at 2.4 A resolution. The dimeric interface lacks a chloride binding site. The N-terminal extension participates in dimeric interactions in a domain swapping manner. Sulfate is bound in the active site of the native structure, which is replaced by cysteine in the cysteine bound form
hanging drop vapor diffusion method, using 100 mM sodium citrate, pH 5.6, 100 mM ammonium sulfate, 20% (w/v) PEG 4000
in complex with substrate analog citrate, at 1.33 A resolution. The C1-carboxylate of citrate is bound at the carboxylate position of O-acetylserine, whereas the C6-carboxylate adopts two conformations. Modeling of the unnatural substrate 5-thio-2-nitrobenzoate into the structure
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complex with inhibitory pentapeptides MNYDI (10 mM HEPES, pH 8.0, 25 mM NaCl, 8.8 mM peptide), MNKGI (20 mM HEPES, pH 7.5, 20 mM NaCl, 12.5 mM peptide), MNWNI (10 mM HEPES, pH 7.5, 25 mM NaCl, 7.5 mM peptide), MNYFI (20 mM HEPES, pH 8.0, 20 mM NaCl, 12.7 mM peptide), MNENI (10 mM HEPES, pH 7.5, 25 mM NaCl, 9.4 mM peptide), and MNETI (20 mM HEPES, pH 7.5, 20 mM NaCl, 9.4 mM peptide), reservoir solution is 100 mM HEPES, pH 7.5, between 1.8 and 2.1 M (NH4)2SO4, and polyethylene glycol 400, except for the complex with MNWNI (100 mM CAPS, pH 10.5, 1.75 (NH4)2SO4, and 0.2 M Li2SO4), the cryoprotection solution contains glycerol, hanging drop vapor diffusion method, diffraction data are measured at -183°C
the X-ray structure of three (MNWNI, MNYDI, and MNENI) high affinity pentapeptide-OASS complexes are compared with the docked poses
to 1.8 A resolution. The biologically active unit, a dimer, constitutes the asymmetric unit. Subunit A contains residues 3-213 and 241-333, whilst subunit B comprises residues 4-214 and 241-333. A surface loop from residues 214 to 241 is disordered. The subunit contains two domains. The smaller domain I is constructed by residues 51-158, which primarily form a four-stranded beta-sheet surrounded by four alpha-helices. The larger domain II comprises residues 21-50 and 159-306. Domain II contains four alpha-helices and six beta-strands which, together with a beta-strand contributed from the partner-subunit domain I, form a seven-membered beta-sheet. In addition, residues 307-333 at the C-terminus form an extended helix-loop-helix structure that stretches across the surface of the partner subunit
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purified isozyme CysK1, hanging drop vapor diffusion technique, mixing of 10 mg/ml protein solution with an equal volume of reservoir solution containing 0.1 M MOPS, pH 6.0, 60% 2-methyl-2,4-pentanediol, 16°C, X-ray diffraction structure determination and analysis at 2.30 A resolution, molecular replacement using the coordinates of Mycobacterium tuberculosis OASS, PDB ID 2Q3B, as the search model
purified isozyme CysK2 in complex with cystine, hanging drop vapor diffusion technique, mixing of 10 mg/ml protein solution with an equal volume of reservoir solution containing 1.5 M (NH4)2SO4, 0.1M Bis-Tris-propane, pH 7.0, and 10 mM cystine, 16°C, X-ray diffraction structure determination and analysis at 1.91 A resolution, molecular replacement using the coordinates of Mycobacterium tuberculosis OASS, PDB ID 2Q3B, as the search model
identification of inhibitors by docking into crystal structure, PDB entry 2Q3C
trapping of the alpha-aminoacrylate reaction intermediate and determination of its structure by cryocrystallography, 2.2 A resolution. Determination of the crystal structure of the enzyme bound to an inhibitory four-residue peptide derived from the C-terminus of Mycobacterium tuberculosis CysE (SAT, Rv2335). The structure of this inhibited form of CysK1 may provide the basis for the design of strong binding inhibitors of this enzyme
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crystal structure of the enzyme with chloride bound at an allosteric site and sulfate bound at the active site
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hanging-drop vapor diffusion method, structure of O-acetylserine sulfhydrylase B solved to 2.3 A
structural model based on crystallographic data
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wild-type and mutant K43A, to 2.25 and 1.9 A resolution, respectively. Each monomer of DcsD takes a typical fold of type II pyridoxal 5'-phosphate enzymes with the cofactor pyridoxal 5'-phosphate covalently bound to invariant Lys residue (Lys43) at the active site. The pyridine ring of pyridoxal 5'-phoshate makes hydrogen bonds with invariant Asn73 and Ser265 residues. Its phosphate group makes hydrogen bonds with Gly177, Thr178, Thr179 and Thr181 residues
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H150A
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in contrast to the wild-type protein the mutant protein is colorless after purification, and UV-Vis scanning of the mutant proteins show that there are no absorptions between 300 and 500 nm, mutant protein does not show a comparable activity to the wild-type protein. This suggests that the mutated residue is crucial or pyridoxal 5'-phosphate binding and stabilization
H168A
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in contrast to the wild-type protein the mutant protein is colorless after purification, and UV-Vis scanning of the mutant proteins show that there are no absorptions between 300 and 500 nm, mutant protein does not show a comparable activity to the wild-type protein. This suggests that the mutated residue is crucial or pyridoxal 5'-phosphate binding and stabilization
K30A
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in contrast to the wild-type protein the mutant protein is colorless after purification, and UV-Vis scanning of the mutant proteins show that there are no absorptions between 300 and 500 nm, mutant protein does not show a comparable activity to the wild-type protein. This suggests that the mutated residue is crucial or pyridoxal 5'-phosphate binding and stabilization
K41A
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mutant protein is also colourful as the wild-type protein, mutant protein does not show the same activity as the wild-type protein
K127A
mutant is inactive for cysteine synthesis and does not form the alpha-aminoacrylate intermediate
G162E
naturally occuring mutation, the EMS-induced single nucleotide substitution in the cytosolic OASTL-A1 gene in the Ler-0 accession of Arabidopsis thaliana causes early senescence and death in plants, and is referred to as onset of leaf death3 (old3-1)
Q147A
S75A
S75T
T74S
Q96A/Y125A
F143A
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mutant retains one molecule of pyridoxal 5'-phosphate per subunit, mutant reacts with O-acetylserine but the rate is significantly smaller, kcat/KM (O-acetylserine): 950/Msec
F143D
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mutant retains one molecule of pyridoxal 5'-phosphate per subunit, mutant reacts with O-acetylserine but the rate is significantly smaller, kcat/KM (O-acetylserine): 150/Msec
F143S
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mutant retains one molecule of pyridoxal 5'-phosphate per subunit, mutant reacts with O-acetylserine but the rate is significantly smaller, kcat/KM (O-acetylserine): 380/Msec
F143Y
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mutant retains one molecule of pyridoxal 5'-phosphate per subunit, reaction with O-acetylserine is inhibited
Q142A
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ability of pyridoxal 5'-phosphate binding is not altered, mutant does not react with O-acetylserine
Q240A
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ratio kcat to Km value is 0.4% of wild-type, increase in temperature dependence factors, corresponding to an appreciable increase in the activation energy
T68A
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ratio kcat to Km value is 0.1% of wild-type, increase in temperature dependence factors, corresponding to an appreciable increase in the activation energy
A70S
residue at the substrate binding pocket, important for the H2S-generating activity
E223G
residue at the substrate binding pocket, important for the H2S-generating activity
A70S
Lactiplantibacillus plantarum ATCC BAA-793
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residue at the substrate binding pocket, important for the H2S-generating activity
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E223G
Lactiplantibacillus plantarum ATCC BAA-793
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residue at the substrate binding pocket, important for the H2S-generating activity
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DELTAE115-K118
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mutation disables the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
K118A
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mutation disables the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
K221A/P222E/G223E/P224E
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mutation disables the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
W162A
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mutation increases the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
Y188A
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mutation increases the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
DELTAE115-K118
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mutation disables the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
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K118A
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mutation disables the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
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K221A/P222E/G223E/P224E
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mutation disables the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
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W162A
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mutation increases the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
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Y188A
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mutation increases the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
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N71A
mutant exhibits formation of the alpha-aminoacrylate intermediate, but the rate constant for its formation from the external Schiff base is decreased by 1 order of magnitude compared to that of the wild type
Q142A
mutant is unable to form the alpha-aminoacrylate intermediate but produces pyruvate at a rate much greater than that of the wild-type enzyme
S69A
mutant exhibits formation of the alpha-aminoacrylate intermediate, but the rate constant for its formation from the external Schiff base is decreased by 1 order of magnitude compared to that of the wild type
T68A
mutant is unable to form the alpha-aminoacrylate intermediate but produces pyruvate at a rate much greater than that of the wild-type enzyme
H152A
K120Q
R186L
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retains one cofactor per subunit, accelerates the reaction with substrate O3-acetyl-L-serine 1.8fold, intermediates are formed faster by 1.5 and 1.3fold, respectively, with azide or thiosulfate than in the wild type
R186P
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loss of cofactor leads to enzyme inactivation
S272A
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mutant enzyme catalyzes the overall reaction, first half-reaction is decreased by factor 3, the decrease in rate of elimination is compensated by an increase in affinity for O-acetyl-L-Ser
S272D
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mutant enzyme catalyzes the overall reaction
W161Y
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2fold increase in Vmax and Km-value of O3-acetyl-L-serine
W50Y
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no effect on catalytic rate or affinity of enzyme to first substrate, Km-value for 5-thio-2-nitrobenzoate decrease by 2.7fold
H152A
K120Q
K43A
mutation in invariant Lys43 residue, inactive. Mutant forms an external aldimine adduct upon addition of L-methionine or O-ureido-L-serine
S121A
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
S121M
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
V74T
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
Y97F
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
Y97M
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
K43A
-
mutation in invariant Lys43 residue, inactive. Mutant forms an external aldimine adduct upon addition of L-methionine or O-ureido-L-serine
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S121A
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decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
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V74T
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decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
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Y97F
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decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
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Y97M
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decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
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K214A
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mutant retains high activity with O-acetylserine and sulfide (40% of the activity of the wild type enzyme), but its activity with O-phosphoserine and sulfide is reduced by more than 100fold. The ability to use thiosulfate as an alternative nucleophile in the sulfhydrylase reaction is greatly reduced, but the mutant shows no change in cysteine desulfurase activity
K43A
-
protein is yellow, indicating that it binds pyridoxal 5'-phosphate but has no detectable activity as a cysteine synthase with O-acetylserine or O-phosphoserine and no detectable cysteine desulfurase activity
additional information
Q147A
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mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase
S75A
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mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase
S75T
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mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase
T74S
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mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase
Q96A/Y125A
mutant shows relatively strong binding to serine acetyltransferase C-terminal peptides in comparison with native OASS. The mutant structure looks similar except that the active-site pocket has enough space to bind the serine acetyltransferase C-terminal end
Q96A/Y125A
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mutant shows relatively strong binding to serine acetyltransferase C-terminal peptides in comparison with native OASS. The mutant structure looks similar except that the active-site pocket has enough space to bind the serine acetyltransferase C-terminal end
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H152A
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shift in the ketoenamine to enolimine tautomeric equilibrium toward the neutral enolimineine, the internal Schiff base of the free enzyme, the amino acid external Schiff base, and the alpha-aminoacrylate intermediate. The decreased rate of the mutant likely reflects a decrease in the amount of active enzyme as a result of an increased flexibility of the cofactor , which leads to increased rates of interconversion of the open and closed forms of the enzyme and additional interactions between the cofactor and enzyme in the closed form of the enzyme. Analysis of spectral properties
H152A
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shift in the ketoeneamine to enolimine tautomeric equilibrium towards neutral enolimine in the internal Shiff base of the free enzyme, the amino acid external Schiff base, and the alpha-aminoacrylate intermediate, 2 enzyme conformers are present, decreased rate of the enzyme likely reflects a decrease in the amount of active enzyme as result of the increased cofactor flexibility which stabilizes the nonproductive binding of O3-acetyl-L-serine in the external Schiff base
K120Q
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mutation results in a shift in the tautomeric equilibrium toward the neutral enolimine and an increase in the rate of interconversion of the open and closed forms of the enzyme. A decrease in the rate of both half reactions reflects the stabilization of the external Schiff base. Role of K120 in helping to stabilize the closed conformation of the enzyme by participating in a new bond to the backbone carbonyl of A231
K120Q
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shift in the tautomeric equilibrium toward the neutral enolimine and an increase of the rate of interconversion of the open and closed forms of the enzyme, probably reflecting the stabilization of the external Schiff base
H152A
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shift in the ketoenamine to enolimine tautomeric equilibrium toward the neutral enolimineine, the internal Schiff base of the free enzyme, the amino acid external Schiff base, and the alpha-aminoacrylate intermediate. The decreased rate of the mutant likely reflects a decrease in the amount of active enzyme as a result of an increased flexibility of the cofactor , which leads to increased rates of interconversion of the open and closed forms of the enzyme and additional interactions between the cofactor and enzyme in the closed form of the enzyme. Analysis of spectral properties
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H152A
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shift in the ketoeneamine to enolimine tautomeric equilibrium towards neutral enolimine in the internal Shiff base of the free enzyme, the amino acid external Schiff base, and the alpha-aminoacrylate intermediate, 2 enzyme conformers are present, decreased rate of the enzyme likely reflects a decrease in the amount of active enzyme as result of the increased cofactor flexibility which stabilizes the nonproductive binding of O3-acetyl-L-serine in the external Schiff base
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K120Q
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mutation results in a shift in the tautomeric equilibrium toward the neutral enolimine and an increase in the rate of interconversion of the open and closed forms of the enzyme. A decrease in the rate of both half reactions reflects the stabilization of the external Schiff base. Role of K120 in helping to stabilize the closed conformation of the enzyme by participating in a new bond to the backbone carbonyl of A231
-
K120Q
-
shift in the tautomeric equilibrium toward the neutral enolimine and an increase of the rate of interconversion of the open and closed forms of the enzyme, probably reflecting the stabilization of the external Schiff base
-
additional information
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knockout of the most abundant cytosolic OAS-TL isoforms oas-a1.1 and osa-a1.2. Total intracellular Cys and glutathione concentrations are reduced, and the glutathione redox state is shifted in favor of its oxidized form. The capability of the mutants to chelate heavy metals does not differ from that of the wild type, but the mutants have an enhanced sensitivity to cadmium. The oas-a1.1 mutant plants are oxidatively stressed, H2O2 production is localized in shoots and roots, spontaneous cell death lesions occur in the leaves, and lignification and guaiacol peroxidase activity are significantly increased
additional information
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null alleles of cytosolic isoform oas-tl A or plastid isoform oas-tl B alone show that cytosolic OAS-TL A and plastid OAS-TL B are completely dispensable, although together they contribute 95% of total OAS-TL activity. An oas-tl AB double mutant, relying solely on mitochondrial OAS-TL C for Cys synthesis, shows 25% growth retardation. Although OAS-TL C alone is sufficient for full development, oas-tl C plants also show retarded growth
additional information
upon expression of the enzymes of the cysteine synthase complex, serine-acetyl-transferase SAT and O-acetyl-serine-(thiol)-lyase OAS-TL, cross-binding of Arabidopsis thaliana OAS-TL with Escherichia coli SAT may take place
additional information
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upon expression of the enzymes of the cysteine synthase complex, serine-acetyl-transferase SAT and O-acetyl-serine-(thiol)-lyase OAS-TL, cross-binding of Arabidopsis thaliana OAS-TL with Escherichia coli SAT may take place
additional information
direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis and enhance cysteine rduction. Several polypeptides based on OAS-TL C amino-acid sequence found at SAT-OASTL interaction sites are designed as probable competitors for serine acetyltransferase binding. After verification of the binding in a yeast two-hybrid assay, the most strongly interacting polypeptide is introduced to different cellular compartments of Arabidopsis thaliana cell via genetic transformation. Transgenic Arabidopsis lines with PEP4 expression show moderate changes in SAT and OAS-TL activities
additional information
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direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis and enhance cysteine rduction. Several polypeptides based on OAS-TL C amino-acid sequence found at SAT-OASTL interaction sites are designed as probable competitors for serine acetyltransferase binding. After verification of the binding in a yeast two-hybrid assay, the most strongly interacting polypeptide is introduced to different cellular compartments of Arabidopsis thaliana cell via genetic transformation. Transgenic Arabidopsis lines with PEP4 expression show moderate changes in SAT and OAS-TL activities
additional information
generation of a OAS-TL A mutant by T-DNA insertion. Generation major isozyme OAS-TL double loss-of-function mutants oastlBC A+/+, oastlAC B+/+, and oastlAB C+/+, leaving only one major OAS-TL in the cytosol, in the plastids, and in the mitochondria, respectively. Extractable OAS-TL activity is not altered in the oastlBC A+/+ mutant compared with the wild-type, while OAS-TL activities are decreased to 30% and 3% in the oastlAC B+/+ and oastlAB C+/+ mutants, respectively. Phenotypes, overview. The incorporation of sulfur into thiols but not thiol steady-state levels is decreased in mutants lacking cytosolic OAS-TL A
additional information
generation of a OAS-TL A mutant by T-DNA insertion. Generation major isozyme OAS-TL double loss-of-function mutants oastlBC A+/+, oastlAC B+/+, and oastlAB C+/+, leaving only one major OAS-TL in the cytosol, in the plastids, and in the mitochondria, respectively. Extractable OAS-TL activity is not altered in the oastlBC A+/+ mutant compared with the wild-type, while OAS-TL activities are decreased to 30% and 3% in the oastlAC B+/+ and oastlAB C+/+ mutants, respectively. Phenotypes, overview. The incorporation of sulfur into thiols but not thiol steady-state levels is decreased in mutants lacking cytosolic OAS-TL A
additional information
generation of a OAS-TL A mutant by T-DNA insertion. Generation major isozyme OAS-TL double loss-of-function mutants oastlBC A+/+, oastlAC B+/+, and oastlAB C+/+, leaving only one major OAS-TL in the cytosol, in the plastids, and in the mitochondria, respectively. Extractable OAS-TL activity is not altered in the oastlBC A+/+ mutant compared with the wild-type, while OAS-TL activities are decreased to 30% and 3% in the oastlAC B+/+ and oastlAB C+/+ mutants, respectively. Phenotypes, overview. The incorporation of sulfur into thiols but not thiol steady-state levels is decreased in mutants lacking cytosolic OAS-TL A
additional information
generation of a OAS-TL B mutant by T-DNA insertion. Generation major isozyme OAS-TL double loss-of-function mutants oastlBC A+/+, oastlAC B+/+, and oastlAB C+/+, leaving only one major OAS-TL in the cytosol, in the plastids, and in the mitochondria, respectively. Extractable OAS-TL activity is not altered in the oastlBC A+/+ mutant compared with the wild-type, while OAS-TL activities are decreased to 30% and 3% in the oastlAC B+/+ and oastlAB C+/+ mutants, respectively. Phenotypes, overview
additional information
generation of a OAS-TL B mutant by T-DNA insertion. Generation major isozyme OAS-TL double loss-of-function mutants oastlBC A+/+, oastlAC B+/+, and oastlAB C+/+, leaving only one major OAS-TL in the cytosol, in the plastids, and in the mitochondria, respectively. Extractable OAS-TL activity is not altered in the oastlBC A+/+ mutant compared with the wild-type, while OAS-TL activities are decreased to 30% and 3% in the oastlAC B+/+ and oastlAB C+/+ mutants, respectively. Phenotypes, overview
additional information
generation of a OAS-TL B mutant by T-DNA insertion. Generation major isozyme OAS-TL double loss-of-function mutants oastlBC A+/+, oastlAC B+/+, and oastlAB C+/+, leaving only one major OAS-TL in the cytosol, in the plastids, and in the mitochondria, respectively. Extractable OAS-TL activity is not altered in the oastlBC A+/+ mutant compared with the wild-type, while OAS-TL activities are decreased to 30% and 3% in the oastlAC B+/+ and oastlAB C+/+ mutants, respectively. Phenotypes, overview
additional information
generation of a OAS-TL C mutant by T-DNA insertion. Generation major isozyme OAS-TL double loss-of-function mutants oastlBC A+/+, oastlAC B+/+, and oastlAB C+/+, leaving only one major OAS-TL in the cytosol, in the plastids, and in the mitochondria, respectively. Extractable OAS-TL activity is not altered in the oastlBC A+/+ mutant compared with the wild-type, while OAS-TL activities are decreased to 30% and 3% in the oastlAC B+/+ and oastlAB C+/+ mutants, respectively. Phenotypes, overview. Lack of mitochondrial OAS-TL C diminishes the incorporation of OAS into thiols without affecting thiol steady-state levels
additional information
generation of a OAS-TL C mutant by T-DNA insertion. Generation major isozyme OAS-TL double loss-of-function mutants oastlBC A+/+, oastlAC B+/+, and oastlAB C+/+, leaving only one major OAS-TL in the cytosol, in the plastids, and in the mitochondria, respectively. Extractable OAS-TL activity is not altered in the oastlBC A+/+ mutant compared with the wild-type, while OAS-TL activities are decreased to 30% and 3% in the oastlAC B+/+ and oastlAB C+/+ mutants, respectively. Phenotypes, overview. Lack of mitochondrial OAS-TL C diminishes the incorporation of OAS into thiols without affecting thiol steady-state levels
additional information
generation of a OAS-TL C mutant by T-DNA insertion. Generation major isozyme OAS-TL double loss-of-function mutants oastlBC A+/+, oastlAC B+/+, and oastlAB C+/+, leaving only one major OAS-TL in the cytosol, in the plastids, and in the mitochondria, respectively. Extractable OAS-TL activity is not altered in the oastlBC A+/+ mutant compared with the wild-type, while OAS-TL activities are decreased to 30% and 3% in the oastlAC B+/+ and oastlAB C+/+ mutants, respectively. Phenotypes, overview. Lack of mitochondrial OAS-TL C diminishes the incorporation of OAS into thiols without affecting thiol steady-state levels
additional information
upon expression of the Arabidopsis thaliana enzymes of the cysteine synthase complex, serine-acetyl-transferase SAT and O-acetyl-serine-(thiol)-lyase OAS-TL, cross-binding of Arabidopsis thaliana OAS-TL with Escherichia coli SAT may take place
additional information
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upon expression of the Arabidopsis thaliana enzymes of the cysteine synthase complex, serine-acetyl-transferase SAT and O-acetyl-serine-(thiol)-lyase OAS-TL, cross-binding of Arabidopsis thaliana OAS-TL with Escherichia coli SAT may take place
additional information
recombinant enzyme expressed in Escherichia coli does not show catalytic activity
additional information
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recombinant enzyme expressed in Escherichia coli does not show catalytic activity
additional information
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enzyme knockout mutant, grows poorly in cysteine-limiting conditions and produces significantly less cysteine than wild-type. Mutant shows increased sensitivity to tellurite, hydrogen peroxide, acid, and diamide. Mutant cells have a significantly reduced ability to recover from starvation in amino acid- or phosphate-limiting conditions
additional information
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enzyme knockout mutant, grows poorly in cysteine-limiting conditions and produces significantly less cysteine than wild-type. Mutant shows increased sensitivity to tellurite, hydrogen peroxide, acid, and diamide. Mutant cells have a significantly reduced ability to recover from starvation in amino acid- or phosphate-limiting conditions
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21
-
pH 8.0, 50 mM dithiothreitol, 0.08 mM pyridoxal phosphate, 30 min, stable
50
57 - 60
-
purified recombinant His-tagged enzyme, 1 h, 50% activity remaining
60
65
70
77
-
5 min, complete loss of activity
80
additional information
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pyridoxal 5'-phosphate stabilizes against heat inactivation
65
-
5 min, complete loss of activity, without pyridoxal 5'-phosphate
65
-
2 min, isoenzyme 1 loses 50% loss of activity, isoenzymes 2 loses 25% of its activity, no loss of activity, isoenzyme 3
70
-
10 min, 10% loss of activity of immobilized enzyme, 65-80% loss of activity of native enzyme
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
extended dimeric interface interactions contribute to the stability of the dimer under physiological conditions
holo-O-acetylserine sulfhydrylase exhibits greater conformational stability than the apoenzyme form. Role of pyridoxal 5'-phosphate in the structural stabilization of O-acetylserine sulfhydrylase
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1,4-dioxane
Glycerol
-
5% glycerol and 5 mM 2-mercaptoethanol are essential for maintaining the long-term stability of the enzyme
mercaptoethanol
-
5% glycerol and 5 mM 2-mercaptoethanol are essential for maintaining the long-term stability of the enzyme
N,N-dimethylformamide
1,4-dioxane
-
the activity of enzyme OASS-B gradually decreases as the content of organic solvent increases
1,4-dioxane
Escherichia coli W3110 / ATCC 27325
-
the activity of enzyme OASS-B gradually decreases as the content of organic solvent increases
-
N,N-dimethylformamide
-
the activity of enzyme OASS-B gradually decreases as the content of organic solvent increases
N,N-dimethylformamide
Escherichia coli W3110 / ATCC 27325
-
the activity of enzyme OASS-B gradually decreases as the content of organic solvent increases
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15 C, potassium phosphate buffer, dithiothreitol, one week, 50% loss of activity
-
-20 C, phosphate buffer, pH 7.5, glycerol, pyridoxal-5'-phosphate, 8 days, 50% loss of activity
-
-20 C, potassium phosphate buffer, pH 6.5, 1 mM EDTA, at least several days, no loss of activity
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-20 C, Tris-HCl buffer, pH 7.6, bovine serum albumine, 8 months, 10% loss of activity
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0 C, potassium phosphate buffer, pH 8, mercaptoethanol, EDTA, three months, no loss of activity
-
0 C, potassium phosphate buffer, pH 8.0, 2-mercaptoethanol, EDTA, several months, no loss of activity
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20 C, room temperature, Tris-HCl buffer, pH 7.6, bovine serum albumine, several days, no loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cell harvesting are resuspended in 50 mM Tris buffer, pH 8.0, containing 10 mM EDTA, 15 mM beta-mercaptoethanol, 0.05 mM N-p-tosyl-L-lysine chloromethylketone, leupeptin, aprotinin, pepstatin, lysozyme and pyridoxal 5'-phosphate, centrifuged, supernatant loaded on a DE52 anion exchange column, washed with 50 mM Tris buffer, pH 8.0, with 10 mM EDTA, and 15 mM beta-mercaptoethanol, elution with NaCl gradient in buffer, active fractions are pooled, concentrated and applied to a GSTrap 4B column, washed with PBS buffer, pH 7.4, containing 140 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, and 1.8 mM KH2PO4, elution with 50 mM Tris, pH 8.0, with 20 mM reduced glutathione and thrombin, dialyzed with 15 mM potassium phosphate, pH 7.2, applied on a DE 52 column, separation of enzyme from GST-tag and thrombin with a gradient of 15-300 mM potassium phosphate buffer, pH 7.2
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cells are harvested by centrifugation, washed with sterile water, again harvested by centrifugation, suspended in 20 mM potassium phosphate buffer, pH 7.4, containing 0.5 M NaCl, lysed with lysozyme at room temperature, one-step affinity chromatography with nickel metal-affinity resin columns, dialyzed against 20 mM potassium phosphate buffer, pH 7.5, 5% glycerol, and 5 mM 2-mercaptoethanol
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ethanol precipitation, ammonium sulfate precipitation, preparative electrophoresis, phenyl sepharose
Ni-NTA affinity and Superdex 200 pg gel filtration chromatography
purified using nickel-affinity and gel filtration. Thrombin digestion is used to remove the His tag from each protein
Q-Sepharose and phenyl Sepharose column, active fractions are pooled and concentrated
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recombinant chloroplast isozyme OASTL 29fold from Chlorella sorokiniana S-sufficient and S-starved cells by affinity binding to Arabidopsis thaliana serine acetyltransferase SAT5 fused to a metal resin via its His-tag protein, elution by by O-acetylserine, to homogeneity. Successful application of SAT/OASTL interaction for purification
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recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) pLYsS by nickel affinity chhromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity chromatography and gel filtration
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity and over 95% purity
recombinant N-terminal His-tagged enzyme, cleavage and removal of the tag
recombinant N-terminally His6-tagged isozyme CysK1 from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and ultrafiltration
recombinant N-terminally His6-tagged isozyme CysK2 from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and ultrafiltration
the apoenzyme of OASS-B is prepared using hydroxylamine as the resolving reagent. Apoenzyme is reconstituted to holoenzyme by addition of pyridoxal 5'-phosphate
-
the soluble protein is purified by one-step affinity chromatography to apparent homogeneity
-
using Glutathione Sepharose 4B column
using Ni-NTA chromatography
recombinant N-terminal His-tagged enzyme, cleavage and removal of the tag
recombinant N-terminal His-tagged enzyme, cleavage and removal of the tag
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of transgenic Nicotiana tabacum carrying either spinach cytosolic cDNA, designated 3F plants, or chimeric CSAse A cDNA fused with the sequence for chloroplast-targeting transit peptide of pea Rubisco small subunit, designated 4F plants. Generation of F1 transgenic tobacco, highly tolerant to sulfur-containing pollutants, in which Csase activities are enhanced both in cytosol and in the chloroplasts by crossing 3F plants with 4F plants
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cotyledon segments of seedlings of Ipomoea aquatica are transformed with Arabidopsis serine acetyltransferase gene and Oryza sativa cysteine synthase gene under the control of the cauliflower mosaic virus 35S promoter. Strengthening of serine acetyltransferase and cysteine synthase results in increase not only in sulfate uptake, but also in total biomass
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DNA and amino acid sequence determination and analysis, sequence comparisons
-
expressed in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli as GST-fusion proteins
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli NM522 with plasmid pRSM40
-
expression in Escherichia coli
expression in with plasmid pRSM40 in Escherichia coli NM522
-
expression of the glutathione S-transferase (GST)-fusion enzyme in Escherichia coli BL21 with pGEX 4T-2 vector
-
gene CS1, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene CS3, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene Cy-OAS-TL, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3) pLYsS
gene cysK, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene cysK, recombinant expression of N-terminal His-tagged enzyme
gene cysK1, sequence comparisons, recombinant expression of N-terminally His6-tagged isozyme CysK1 in Escherichia coli strain BL21 (DE3)
gene cysK2, sequence comparisons, recombinant expression of N-terminally His6-tagged isozyme CysK2 in Escherichia coli strain BL21 (DE3)
gene cysl-2, quantitative real-time PCR enzyme expression analysis
gene cysM, recombinant expression of N-terminal His-tagged enzyme
H2S is a major environmental pollutant, highly toxic to living organisms at high concentrations. Even at low concentrations, it causes an unpleasant odor from wetlands, especially from wastewater. Plants can utilize hydrogen sulfide as a sulfur source to synthesize cysteine. It is thus feasible to use aquatic plants, which possess high potential for sulfur assimilation, to remove hydrogen sulfide from the wetland. Transgenic rice plants over-expressing cysteine synthase exhibit 3fold elevated cysteine synthase activity, and incorporate more H2S into cysteine and glutathione than their wild type counterparts upon exposure to a high level of H2S. Overexpression of cysteine synthase in aquatic plants is a viable approach to remove H2S from polluted environments
overexpression of the Atcys-3A gene of the cytosolic isoform in Saccharomyces cerevisiae can support the growth of the yeast cells at high concentrations of sodium chloride, suggesting that the plant protein is able to confer salt tolerance in yeast
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PCR-amplification, expression of His-tagged wild type and mutant enzyme in Escherichia coli BL21(DE3) with expression vector pLM1
-
recombinant expression of chloroplast isozyme OASTL in Arabidopsis thaliana transgenic plants. The cytosolic AtSAT5 isoform from Arabidopsis thaliana is N-terminaly fused with a His-tag, expressed in Escherichia coli and immobilized on a His-trap column for use as affinity anchor to purify enzyme OASTL
-
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS
-
recombinant expression of the enzyme under stress conditions in Trypanosoma rangeli, a trypanosome that does not perform cysteine biosynthesis de novo, results in rescue of the cysteine synthase activity and increased rates of survival of epimastigotes expressing the enzyme compared to those of wild-type parasites
to decrease the activity of OASTL, potato plants are transformed with the vector pBinAR harboring a cDNA encoding a sequence from either the StOASTL A or the StOASTL B gene in reverse orientation with respect to the cauliflower mosaic virus 35S promoter. THe transgenic approach is used to downregulate specifically the plastidial and cytosolic isoforms in Solanum tuberosum. This approach results in decreased RNA, protein, and enzymatic activity levels. H2S-releasing capacity is also reduced in these lines. The thiol levels in the transgenic lines are, regardless of the selected OASTL isoform, significantly elevated. Levels of metabolites such as serine, O-acetyl-L-Ser, methionine, threonine, isoleucine, and lysine also increase in the investigated transgenic lines
gene cysK, recombinant expression of N-terminal His-tagged enzyme
gene cysK, recombinant expression of N-terminal His-tagged enzyme
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is slightly increased during PEG-induced osmotic stress and significant up-regulation is observed during the combination treatment of reduced Zn2+ & increased Fe2+ (i.e., low Zn+2-high Fe+2) salt
S-starvation results in the increase of the larger chloroplastic OASTL isoform and the induction of a new and smaller cytosolic isoform
serine O-acetyltransferase and cysteine synthase proteins expression/activity is upregulated in amastigote growth stage
the enzyme is upregulated under in vitro stress conditions induced by hydrogen peroxide, S-nitroso-N-acetylpenicillamine, or antimonial compounds in a developmental stage-specific manner
S-starvation results in the increase of the larger chloroplastic OASTL isoform and the induction of a new and smaller cytosolic isoform
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S-starvation results in the increase of the larger chloroplastic OASTL isoform and the induction of a new and smaller cytosolic isoform
-
-
the enzyme is upregulated under in vitro stress conditions induced by hydrogen peroxide, S-nitroso-N-acetylpenicillamine, or antimonial compounds in a developmental stage-specific manner
the enzyme is upregulated under in vitro stress conditions induced by hydrogen peroxide, S-nitroso-N-acetylpenicillamine, or antimonial compounds in a developmental stage-specific manner
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
dehydration stress enhances the activity of enzyme OASTL, as well as Cys content by 20.0% and 25.6%, respectively. The treatment of NaHS plus dehydration stress enhances OASTL activity and Cys content by 20.7% and 22.9%, respectively, compared with the stressed plants. The inclusion of H2S scavenger hypotaurine slows down the activity of OASTL by 27.9. A similar inhibitory effect of hypotaurine is also noticed on Cys content, which exhibits a 31.9% lower value than the stressed seedlings
analysis
development of a primary cell-based phenotypic screening in both the presence and absence of L-cysteine and selection hits that show differential amebicidal effects between the two conditions
biotechnology
-
transgenic plants expressing serine acetyltransferase and cysteine synthase can mitigate detrimental effects of cadmium toxicity, perhaps by efficiently producing and accumulating sulfuric compounds
drug development
environmental protection
H2S is a major environmental pollutant, highly toxic to living organisms at high concentrations. Even at low concentrations, it causes an unpleasant odor from wetlands, especially from wastewater. Plants can utilize hydrogen sulfide as a sulfur source to synthesize cysteine. It is thus feasible to use aquatic plants, which possess high potential for sulfur assimilation, to remove hydrogen sulfide from the wetland. Transgenic rice plants over-expressing cysteine synthase exhibit 3fold elevated cysteine synthase activity, and incorporate more H2S into cysteine and glutathione than their wild type counterparts upon exposure to a high level of H2S. Overexpression of cysteine synthase in aquatic plants is a viable approach to remove H2S from polluted environments
medicine
synthesis
drug development
cysteine biosynthetic pathway is absent in humans but essential in microbial pathogens, suggesting that it provides potential targets for the development of novel antibacterial compounds
drug development
cysteine synthase is a potential drug target for trichomoniasis
drug development
-
O-acetyl-L-serine sulfhydrylase is a promising target for inhibiting the growth of Entamoeba histolytica
drug development
since mammals lack OASS, the enzyme is a potential target for antimicrobial agents
drug development
since mammals lack OASS, the enzyme is a potential target for antimicrobial agents
drug development
the enzyme is a rational drug target against amebiasis
medicine
-
humans lack cysteine synthase. Therefore, this parasite enzyme could be an exploitable drug target
medicine
target for novel peptidomimetic antibiotics based on the C-terminal pentapeptide of serine acetyltransferase
medicine
purified recombinant CysK is usefula as vaccine against Brucella in BALB/c mice, maximum protection by usage of rCysK-Al with aluminium hydroxide gel formulation followed by Freund's adjuvant formulation
synthesis
-
overexpression of enzyme in cytosol, chloroplast, or both of Nicotiana tabacum, transgenic plants show significantly more tolerance than wild-type against Cd2+, Se2+, and Ni2+. Application of transgenic plants to phyto-remediation of Cd2+ from contaminated soils
synthesis
-
enzme OASS produces novel beta-substituted L-amino acids when offered unnatural nucleophiles instead of sulfid, which is useful in producing pharmaceuticals, such as mucolytic agent L-carbocisteine and building blocks for the synthesis of pharmaceuticals and agrochemicals
synthesis
-
CysK overexpressing cells grow fast during log phase, and produce 26.5% more L-isoleucine in flask fermentation and 23.5% more L-isoleucine in fed-batch fermentation. The key genes aspC, lysC, hom, thrB, ilvA, and ilvBN involved in L-isoleucine biosynthesis are all upregulated in CysK overexpressing Corynebacterium glutamicum IWJ001. Overexpressing cells are longer and thicker than control cells, and their membrane permeability increases by 15.8% and biofilm formation ability decreases by 71.3%
synthesis
Escherichia coli W3110 / ATCC 27325
-
enzme OASS produces novel beta-substituted L-amino acids when offered unnatural nucleophiles instead of sulfid, which is useful in producing pharmaceuticals, such as mucolytic agent L-carbocisteine and building blocks for the synthesis of pharmaceuticals and agrochemicals
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synthesis
-
CysK overexpressing cells grow fast during log phase, and produce 26.5% more L-isoleucine in flask fermentation and 23.5% more L-isoleucine in fed-batch fermentation. The key genes aspC, lysC, hom, thrB, ilvA, and ilvBN involved in L-isoleucine biosynthesis are all upregulated in CysK overexpressing Corynebacterium glutamicum IWJ001. Overexpressing cells are longer and thicker than control cells, and their membrane permeability increases by 15.8% and biofilm formation ability decreases by 71.3%
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Release 2023.1 (January 2023)
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