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Information on EC 1.1.1.269 - 2-(S)-hydroxypropyl-CoM dehydrogenase
for references in articles please use BRENDA:EC1.1.1.269
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.269 2-(S)-hydroxypropyl-CoM dehydrogenase
IUBMB Comments
The enzyme is highly specific for (2S)-2-hydroxyalkyl thioethers of CoM, in contrast to EC 1.1.1.268, 2-(R)-hydroxypropyl-CoM dehydrogenase, which is highly specific for the (R)-enantiomer. This enzyme forms component IV of a four-component enzyme system EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC 1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II], EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV].html">click here that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.
The enzyme appears in viruses and cellular organisms
- 1.1.1.269
- epoxide
-
stereoselectivity
- autotrophicus
-
xanthobacter
-
achiral
-
s-enantiomers
- ketones
-
enantioselectivity
-
product-bound
- propylene
- epoxypropane
- acetoacetate
- 2-butanone
showSynonyms
s-hpcdh, (s)-hydroxypropyl-coenzyme m dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(S)-hydroxypropyl-coenzyme M dehydrogenase
(S)-hydroxypropylthioethanesulfonate dehydrogenase
2-(2-(S)-hydroxypropylthio)ethanesulfonate dehydrogenase
-
-
-
-
HPCDH3
S-HPCDH
xecE
xecE1
xecE3
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2S)-2-hydroxypropyl-CoM + NAD+ = 2-oxopropyl-CoM + NADH + H+
highly specific
-
-
-
(2S)-2-hydroxypropyl-CoM + NAD+ = 2-oxopropyl-CoM + NADH + H+
The enzyme is highly specific for (S)-2-hydroxyalkyl thioethers of CoM, in contrast to EC 1.1.1.268, 2-(R)-hydroxypropyl-CoM dehydrogenase, which is highly specific of the (R)-enantiomer. This enzyme forms component IV of four-component enzyme system. Comprising EC 4.2.99.19, 2-hydroxypropyl-CoM lyase, component I, EC 1.8.1.5, 2-oxopropyl-CoM reductase, carboxylating, component II, EC 1.1.1.268, 2-(R)-hydroxypropyl-CoM dehydrogenase, component III, and EC 1.1.1.269, 2-(S)-hydroxypropyl-CoM dehydrogenase, component IV, that is involved in epoxylalkane carboxylation in Xanthobacter sp. strain Py2
-
-
-
(2S)-2-hydroxypropyl-CoM + NAD+ = 2-oxopropyl-CoM + NADH + H+
active site structure modeling and stereochemistry of reaction mechanism, overview
(2S)-2-hydroxypropyl-CoM + NAD+ = 2-oxopropyl-CoM + NADH + H+
active site structure modeling and stereochemistry of reaction mechanism, overview
-
-
(2S)-2-hydroxypropyl-CoM + NAD+ = 2-oxopropyl-CoM + NADH + H+
active site structure modeling and stereochemistry of reaction mechanism, overview
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
propene degradation
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SYSTEMATIC NAME
IUBMB Comments
2-[2-(S)-hydroxypropylthio]ethanesulfonate:NAD+ oxidoreductase
The enzyme is highly specific for (2S)-2-hydroxyalkyl thioethers of CoM, in contrast to EC 1.1.1.268, 2-(R)-hydroxypropyl-CoM dehydrogenase, which is highly specific for the (R)-enantiomer. This enzyme forms component IV of a four-component enzyme system {comprising EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC 1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II], EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV]} that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.
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CAS REGISTRY NUMBER
COMMENTARY
369364-40-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-2-butanol + NAD+
2-butanone + NADH + H+
Substrates: -
Products: -
Products: -
r
2-(2-hydroxyethylthio)ethanesulfonate + NAD+
2-(formylmethylthio)ethanesulfonate + NADH + H+
Substrates: achiral mimic of both R-hydroxypropyl-CoM and S-hydroxypropyl-CoM, substrate for both the R- and S-HPCDH enzymes with identical Km values
Products: -
Products: -
r
2-propanol + NAD+
acetone + NADH + H+
Substrates: -
Products: -
Products: -
r
(2S)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: -
Products: -
Products: -
r
(2S)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: substrate binding structure, overview
Products: -
Products: -
r
(2S)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: -
Products: -
Products: -
r
(2S)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: substrate binding structure, overview
Products: -
Products: -
r
(2S)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: -
Products: -
Products: -
r
(2S)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: substrate binding structure, overview
Products: -
Products: -
r
(S)-2-butanol + NAD+
2-butanone + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-2-butanol + NAD+
2-butanone + NADH + H+
Substrates: -
Products: -
Products: -
r
2-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: -
Products: -
Products: -
r
2-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: poor substrate. S-HPCDH3 cannot bind hydroxypropyl-CoM with CoM oriented properly in the sulfonate-binding pocket that consists of residues R211 and K214. R-hydroxypropyl-CoM binds to S-HPCDH3 with a 290-fold lower affinity but in an orientation where the hydroxyl and hydrogen on C2 can be more properly aligned with tyrosine 156 and NAD+, such that kcat decreases by 4.5-fold relative to the natural substrate S-hydroxypropyl-CoM
Products: -
Products: -
r
2-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: -
Products: -
Products: -
r
2-(R)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: poor substrate. S-HPCDH3 cannot bind hydroxypropyl-CoM with CoM oriented properly in the sulfonate-binding pocket that consists of residues R211 and K214. R-hydroxypropyl-CoM binds to S-HPCDH3 with a 290-fold lower affinity but in an orientation where the hydroxyl and hydrogen on C2 can be more properly aligned with tyrosine 156 and NAD+, such that kcat decreases by 4.5-fold relative to the natural substrate S-hydroxypropyl-CoM
Products: -
Products: -
r
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
-
Substrates: -
Products: -
Products: -
?
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: oxidation of S-hydroxypropyl-CoM with a kcat that is 402 times less than that for R-hydroxypropyl-CoM
Products: -
Products: -
r
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: -
Products: -
Products: -
r
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: -
Products: -
Products: -
?
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: substrate binding structures, overview
Products: -
Products: -
?
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
-
Substrates: -
Products: -
Products: -
?
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: oxidation of S-hydroxypropyl-CoM with a kcat that is 402 times less than that for R-hydroxypropyl-CoM
Products: -
Products: -
r
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: -
Products: -
Products: -
r
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: -
Products: -
Products: -
?
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: substrate binding structures, overview
Products: -
Products: -
?
2-(S)hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH
-
Substrates: involved in propylene metabolism in bacteria
Products: -
Products: -
?
2-(S)hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH
-
Substrates: involved in propylene metabolism in bacteria
Products: -
Products: -
?
2-butanone + NADH + H+
(S)-2-butanol + (R)-2-butanol + NAD+
Substrates: -
Products: -
Products: -
r
2-butanone + NADH + H+
(S)-2-butanol + (R)-2-butanol + NAD+
Substrates: -
Products: without additions, 99.2% (S)-enantiomer + 0.8% (R)-enantiomer, in presence of 1 mM ethansulfonate 99.0% (S)-enantiomer + 2% (R)-enantiomer. Mutant K214A, without additions, 91.6% (S)-enantiomer + 8.4% (R)-enantiomer, in presence of 1 mM ethansulfonate 90.9% (S)-enantiomer + 9.1% (R)-enantiomer
Products: without additions, 99.2% (S)-enantiomer + 0.8% (R)-enantiomer, in presence of 1 mM ethansulfonate 99.0% (S)-enantiomer + 2% (R)-enantiomer. Mutant K214A, without additions, 91.6% (S)-enantiomer + 8.4% (R)-enantiomer, in presence of 1 mM ethansulfonate 90.9% (S)-enantiomer + 9.1% (R)-enantiomer
r
2-butanone + NADH + H+
(S)-2-butanol + (R)-2-butanol + NAD+
Substrates: -
Products: -
Products: -
r
2-butanone + NADH + H+
(S)-2-butanol + (R)-2-butanol + NAD+
Substrates: -
Products: without additions, 99.2% (S)-enantiomer + 0.8% (R)-enantiomer, in presence of 1 mM ethansulfonate 99.0% (S)-enantiomer + 2% (R)-enantiomer. Mutant K214A, without additions, 91.6% (S)-enantiomer + 8.4% (R)-enantiomer, in presence of 1 mM ethansulfonate 90.9% (S)-enantiomer + 9.1% (R)-enantiomer
Products: without additions, 99.2% (S)-enantiomer + 0.8% (R)-enantiomer, in presence of 1 mM ethansulfonate 99.0% (S)-enantiomer + 2% (R)-enantiomer. Mutant K214A, without additions, 91.6% (S)-enantiomer + 8.4% (R)-enantiomer, in presence of 1 mM ethansulfonate 90.9% (S)-enantiomer + 9.1% (R)-enantiomer
r
2-oxopropyl-CoM + NADH + H+
2-(R)-hydroxypropyl-CoM + NAD+
Substrates: -
Products: -
Products: -
r
2-oxopropyl-CoM + NADH + H+
2-(R)-hydroxypropyl-CoM + NAD+
Substrates: -
Products: -
Products: -
r
additional information
?
-
Substrates: substrate specificity of the stereochemically different isozymes, R-HPCDH (EC 1.1.1.268) and S-HPCDH are 41% identical to each other, overview
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity of the stereochemically different isozymes, R-HPCDH (EC 1.1.1.268) and S-HPCDH are 41% identical to each other, overview
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity of the stereochemically different isozymes, R-HPCDH (EC 1.1.1.268) and S-HPCDH are 41% identical to each other, overview
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: -
Products: -
Products: -
r
(2S)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: -
Products: -
Products: -
r
(2S)-2-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: -
Products: -
Products: -
r
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: -
Products: -
Products: -
?
2-(S)-hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH + H+
Substrates: -
Products: -
Products: -
?
2-(S)hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH
-
Substrates: involved in propylene metabolism in bacteria
Products: -
Products: -
?
2-(S)hydroxypropyl-CoM + NAD+
2-oxopropyl-CoM + NADH
-
Substrates: involved in propylene metabolism in bacteria
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanesulfonate
-
i.e. coenzyme M: function in catabolic pathway of hydrocarbon oxidation
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(2-methyl-2-hydroxypropylthio)ethanesulfonate
competitive; competitive
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.97
2-(2-hydroxyethylthio)ethanesulfonate
wild-type, pH 7.5, 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.8
2-(2-hydroxyethylthio)ethanesulfonate
wild-type, pH 7.5, 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.29
2-(2-methyl-2-hydroxypropylthio)ethanesulfonate
pH 7.5, 30°C
0.29
2-(2-methyl-2-hydroxypropylthio)ethanesulfonate
wild-type, pH 7.5, 30°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
metabolism of propylene depends on the presence of a linear megaplasmid, that encodes enzymes of alkene oxidation, epoxide carboxylation and CoM biosynthesis
brenda
-
metabolism of propylene depends on the presence of a linear megaplasmid, that encodes enzymes of alkene oxidation, epoxide carboxylation and CoM biosynthesis
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
evolution
the enzyme belongs to the short-chain dehydrogenases/reductase (SDR) superfamily of enzymes. The C-terminal domains of SDR enzymes are responsible for imparting substrate specificity
evolution
-
the enzyme belongs to the short-chain dehydrogenases/reductase (SDR) superfamily of enzymes. The C-terminal domains of SDR enzymes are responsible for imparting substrate specificity
-
evolution
-
the enzyme belongs to the short-chain dehydrogenases/reductase (SDR) superfamily of enzymes. The C-terminal domains of SDR enzymes are responsible for imparting substrate specificity
-
metabolism
the bacterium produces R- and S-HPCDH, EC 1.1.1.268 and EC 1.1.1.269, simultaneously to facilitate transformation of R- and S-enantiomers of epoxy-propane to acommon achiral product 2-ketopropyl-CoM
metabolism
(R)- and (S)-hydroxypropyl-coenzyme M dehydrogenase (R- and S-HPCDH), are part of a bacterial pathway of short-chain alkene and epoxide metabolism. R- and S-HPCDH act on different substrate enantiomers in a common pathway
metabolism
-
the bacterium produces R- and S-HPCDH, EC 1.1.1.268 and EC 1.1.1.269, simultaneously to facilitate transformation of R- and S-enantiomers of epoxy-propane to acommon achiral product 2-ketopropyl-CoM
-
metabolism
-
(R)- and (S)-hydroxypropyl-coenzyme M dehydrogenase (R- and S-HPCDH), are part of a bacterial pathway of short-chain alkene and epoxide metabolism. R- and S-HPCDH act on different substrate enantiomers in a common pathway
-
metabolism
-
(R)- and (S)-hydroxypropyl-coenzyme M dehydrogenase (R- and S-HPCDH), are part of a bacterial pathway of short-chain alkene and epoxide metabolism. R- and S-HPCDH act on different substrate enantiomers in a common pathway
-
additional information
structural basis for stereospecificity of S-HPCDH, comparison to R-HPCDH, EC 1.1.1.268, overview. Placement of catalytic residues within the active site of each enzyme is nearly identical, structural differences in the surrounding area provide each enzyme with a distinct substrate binding pocket. The active site of S-HPCDH is located in a cleft between the N- and C-terminal domains, the catalytic tetrad comprises residues Y156, K160, S143, and N115
additional information
-
structural basis for stereospecificity of S-HPCDH, comparison to R-HPCDH, EC 1.1.1.268, overview. Placement of catalytic residues within the active site of each enzyme is nearly identical, structural differences in the surrounding area provide each enzyme with a distinct substrate binding pocket. The active site of S-HPCDH is located in a cleft between the N- and C-terminal domains, the catalytic tetrad comprises residues Y156, K160, S143, and N115
additional information
structure-function relationship, active site structure modeling and stereochemistry of reaction mechanism, overview. The C-terminal domains of SDR enzymes are responsible for imparting substrate specificity
additional information
-
structural basis for stereospecificity of S-HPCDH, comparison to R-HPCDH, EC 1.1.1.268, overview. Placement of catalytic residues within the active site of each enzyme is nearly identical, structural differences in the surrounding area provide each enzyme with a distinct substrate binding pocket. The active site of S-HPCDH is located in a cleft between the N- and C-terminal domains, the catalytic tetrad comprises residues Y156, K160, S143, and N115
-
additional information
-
structure-function relationship, active site structure modeling and stereochemistry of reaction mechanism, overview. The C-terminal domains of SDR enzymes are responsible for imparting substrate specificity
-
additional information
-
structure-function relationship, active site structure modeling and stereochemistry of reaction mechanism, overview. The C-terminal domains of SDR enzymes are responsible for imparting substrate specificity
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HCDS3_XANP2
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
255
1
25473
Swiss-Prot
-
HCDS1_XANP2
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
249
3
24941
Swiss-Prot
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, X-ray diffraction structure determination and analysis
purified recombinant S-HPCDH free or bound to substrates 2-(S)-hydroxypropyl-CoM and NAD+, sitting drop vapour diffusion method, mixing of equal volumes of 13 mg/ml protein in buffer containing 25% glycerol, with or without 0.05 mM NAD+ and 0.05 mM 2-(S)-hydroxypropyl-CoM, with well solution containing of 0.1 M Bis-Tris, pH 6.5, 0.35 M ammonium acetate and 27% PEG 3350, X-ray diffraction structure determination and analysis at 1.60 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K214A
substantially reduced catalytic efficiencies with the natural substrates in both the oxidative and reductive direction
R211A
substantially reduced catalytic efficiencies with the natural substrates in both the oxidative and reductive direction
S143A
residue acts as H-bond donor to substrate and in charge stabilization of the transition state, large increase in Km value
Y156A
mutation in general acid/base, large increase in Km value
R211A
-
substantially reduced catalytic efficiencies with the natural substrates in both the oxidative and reductive direction
-
S143A
-
residue acts as H-bond donor to substrate and in charge stabilization of the transition state, large increase in Km value
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Krum, J.G.; Ensign, S.A.
Evidence that a linear megaplasmid encodes enzymes of aliphatic alkene and epoxide metabolism and coenzyme M (2-mercaptoethanesulfonate) biosynthesis in Xanthobacter strain Py2
J. Bacteriol.
183
2172-2177
2001
Xanthobacter sp., Xanthobacter sp. Py2
brenda
Krishnakumar, A.M.; Nocek, B.P.; Clark, D.D.; Ensign, S.A.; Peters, J.W.
Structural basis for stereoselectivity in the (R)- and (S)-hydroxypropylthioethanesulfonate dehydrogenases
Biochemistry
45
8831-8840
2006
Xanthobacter autotrophicus, Xanthobacter autotrophicus Py2
brenda
Sliwa, D.A.; Krishnakumar, A.M.; Peters, J.W.; Ensign, S.A.
Molecular basis for enantioselectivity in the (R)- and (S)-hydroxypropylthioethanesulfonate dehydrogenases, a unique pair of stereoselective short-chain dehydrogenases/reductases involved in aliphatic epoxide carboxylation
Biochemistry
49
3487-3498
2010
Xanthobacter autotrophicus, Xanthobacter autotrophicus (Q56841), Xanthobacter autotrophicus Py2, Xanthobacter autotrophicus Py2 (Q56841)
brenda
Bakelar, J.W.; Sliwa, D.A.; Johnson, S.J.
Crystal structures of S-HPCDH reveal determinants of stereospecificity for R- and S-hydroxypropyl-coenzyme M dehydrogenases
Arch. Biochem. Biophys.
533
62-68
2013
Xanthobacter autotrophicus (A7IQH5), Xanthobacter autotrophicus, Xanthobacter autotrophicus Py2 (A7IQH5)
brenda
Clark, D.D.
Characterization of the recombinant (R)- and (S)-hydroxypropyl-coenzyme M dehydrogenases A case study to augment the teaching of enzyme kinetics and stereoselectivity
Biochem. Mol. Biol. Educ.
47
124-132
2019
Xanthobacter autotrophicus (Q56841), Xanthobacter autotrophicus ATCC BAA-1158 (Q56841), Xanthobacter autotrophicus Py2 (Q56841)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.269)
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