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2 glutathione + COX2-disulfide
glutathione-disulfide + COX2-dithiol
2 glutathione + insulin disulfide
glutathione disulfide + insulin
2 glutathione + pilin FimA-disulfide
glutathione-disulfide + pilin FimA-dithiol
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
2 glutathione + SCO1-disulfide
glutathione-disulfide + SCO1-dithiol
2 glutathione + SCO2-disulfide
glutathione-disulfide + SCO2-dithiol
-
-
-
?
2,3-dimercaptopropanol + protein disulfide
2,3-dimercaptopropanol disulfide + protein-dithiol
2-mercaptoethanol + protein disulfide
2-mercaptoethanol disulfide + protein-dithiol
2-mercaptoethanol glutathione disulfide + glutathione
2-mercaptoethanol disulfide + glutathione disulfide
alpha-lipoate + protein disulfide
?
-
-
-
-
?
apocytochrome c + glutathione disulfide
apocytochrome c disulfide + 2 glutathione
cysteamine + protein disulfide
?
dihydrolipoamide + protein disulfide
?
-
-
-
-
?
dihydrolipoate + protein disulfide
?
dihydrolipoic acid + protein disulfide
?
dithiothreitol + insulin disulfide
dithiothreitol disulfide + insulin
dithiothreitol + protein disulfide
?
glutathionylated BSA + glutathione
BSA + glutathione disulfide
-
-
-
-
?
glutathionylated glyceraldehyde-3-phosphate dehydrogenase + glutathione
glutathione disulfide + glyceraldehyde-3-phosphate dehydrogenase
glutathionylated glyceraldehyde-3-phosphate dehydrogenase + reduced GRX3
glutathione + glyceraldehyde-3-phosphate dehydrogenase + oxidized GRX3
substrate is glutathionylated A4-GAPDH. A4-GAPDH activity is reversibly inhibited by glutathionylation
-
-
?
glutathionylated isocitrate lyase + dithiothreitol
glutathione dithiothreitol disulfide + isocitrate lyase
-
-
-
?
glutathionylated isocitrate lyase + glutathione
glutathione disulfide + isocitrate lyase
GSH + 5,5'-dithiobis(nitrobenzoic acid)
?
-
-
-
-
?
GSH + AtlS
GSSG + ?
-
-
-
-
?
GSH + insulin
GSSG + reduced insulin chain A and B
GSH + protein disulfide
GSSG + protein-dithiol
GSH + protein-disulfide
GSSG + protein-dithiol
GSH + vasotocin
?
-
-
-
-
?
GSSG + reduced ribonuclease
GSH + oxidized ribonuclease
hydroxyethyl disulfide + protein disulfide
?
-
-
-
-
?
insulin disulfide + dithiothreitol
insulin + dithiothreitol disulfide
L-cysteine + protein disulfide
cystine + protein-dithiol
reduced dithiothreitol + NADP+
oxidized dithiothreitol + NADPH + H+
-
-
-
-
r
SdbA carrying a disulfide bond + superantigen SpeA with reduced L-cysteine residues
SdbA with reduced L-cysteine residues + superantigen SpeA carrying a disulfide bond
thioglycolic acid + protein disulfide
?
-
-
-
-
?
additional information
?
-
2 glutathione + COX2-disulfide
glutathione-disulfide + COX2-dithiol
-
-
-
?
2 glutathione + COX2-disulfide
glutathione-disulfide + COX2-dithiol
-
-
-
?
2 glutathione + COX2-disulfide
glutathione-disulfide + COX2-dithiol
-
-
-
?
2 glutathione + insulin disulfide
glutathione disulfide + insulin
-
-
-
?
2 glutathione + insulin disulfide
glutathione disulfide + insulin
-
-
-
?
2 glutathione + pilin FimA-disulfide
glutathione-disulfide + pilin FimA-dithiol
-
-
-
-
?
2 glutathione + pilin FimA-disulfide
glutathione-disulfide + pilin FimA-dithiol
-
recombinant FimA expressed in Escherichia coli
-
-
?
2 glutathione + pilin FimA-disulfide
glutathione-disulfide + pilin FimA-dithiol
-
-
-
-
?
2 glutathione + pilin FimA-disulfide
glutathione-disulfide + pilin FimA-dithiol
-
recombinant FimA expressed in Escherichia coli
-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
-
-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
-
-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
-
-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
-
-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
-
-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
-
-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + SCO1-disulfide
glutathione-disulfide + SCO1-dithiol
-
-
-
?
2 glutathione + SCO1-disulfide
glutathione-disulfide + SCO1-dithiol
-
-
-
?
2 glutathione + SCO1-disulfide
glutathione-disulfide + SCO1-dithiol
-
-
-
?
2,3-dimercaptopropanol + protein disulfide
2,3-dimercaptopropanol disulfide + protein-dithiol
-
-
-
-
?
2,3-dimercaptopropanol + protein disulfide
2,3-dimercaptopropanol disulfide + protein-dithiol
-
-
-
-
?
2,3-dimercaptopropanol + protein disulfide
2,3-dimercaptopropanol disulfide + protein-dithiol
-
-
-
-
?
2,3-dimercaptopropanol + protein disulfide
2,3-dimercaptopropanol disulfide + protein-dithiol
-
-
-
-
?
2-mercaptoethanol + protein disulfide
2-mercaptoethanol disulfide + protein-dithiol
-
-
-
-
?
2-mercaptoethanol + protein disulfide
2-mercaptoethanol disulfide + protein-dithiol
-
-
-
-
?
2-mercaptoethanol glutathione disulfide + glutathione
2-mercaptoethanol disulfide + glutathione disulfide
-
-
-
?
2-mercaptoethanol glutathione disulfide + glutathione
2-mercaptoethanol disulfide + glutathione disulfide
-
-
-
?
2-mercaptoethanol glutathione disulfide + glutathione
2-mercaptoethanol disulfide + glutathione disulfide
-
-
-
-
?
apocytochrome c + glutathione disulfide
apocytochrome c disulfide + 2 glutathione
-
-
-
?
apocytochrome c + glutathione disulfide
apocytochrome c disulfide + 2 glutathione
-
-
-
?
cysteamine + protein disulfide
?
-
-
-
-
?
cysteamine + protein disulfide
?
-
-
-
-
?
cysteamine + protein disulfide
?
-
low activity
-
-
?
cysteamine + protein disulfide
?
-
-
-
-
?
cysteamine + protein disulfide
?
-
-
-
-
?
dihydrolipoate + protein disulfide
?
-
-
-
-
?
dihydrolipoate + protein disulfide
?
-
-
-
-
?
dihydrolipoic acid + protein disulfide
?
-
-
-
-
?
dihydrolipoic acid + protein disulfide
?
-
-
-
-
?
dihydrolipoic acid + protein disulfide
?
-
-
-
-
?
dihydrolipoic acid + protein disulfide
?
-
-
-
-
?
dithiothreitol + insulin disulfide
dithiothreitol disulfide + insulin
-
-
-
?
dithiothreitol + insulin disulfide
dithiothreitol disulfide + insulin
-
-
-
?
dithiothreitol + protein disulfide
?
-
-
-
-
?
dithiothreitol + protein disulfide
?
-
protein disulfide: insulin or thioredoxin
-
-
r
dithiothreitol + protein disulfide
?
-
-
-
-
r
dithiothreitol + protein disulfide
?
-
low activity
-
-
?
dithiothreitol + protein disulfide
?
-
-
-
-
?
glutathionylated glyceraldehyde-3-phosphate dehydrogenase + glutathione
glutathione disulfide + glyceraldehyde-3-phosphate dehydrogenase
substrate is glutathionylated A4-GAPDH. A4-GAPDH activity is reversibly inhibited by glutathionylation
-
-
?
glutathionylated glyceraldehyde-3-phosphate dehydrogenase + glutathione
glutathione disulfide + glyceraldehyde-3-phosphate dehydrogenase
substrate is glutathionylated A4-GAPDH. A4-GAPDH activity is reversibly inhibited by glutathionylation
-
-
?
glutathionylated isocitrate lyase + glutathione
glutathione disulfide + isocitrate lyase
-
-
-
?
glutathionylated isocitrate lyase + glutathione
glutathione disulfide + isocitrate lyase
-
substrate is glutathionylated isocitrate lyase of Chlamydomonas rheinhardtii
-
-
?
GSH + insulin
GSSG + reduced insulin chain A and B
-
-
3052, 394817, 394819, 394825, 394826, 394827, 394828, 394829, 394831, 394832, 394833, 394834, 394835, 394836, 394837, 394838, 394839, 394840, 394845, 394847, 394848, 394849, 394851 -
-
?
GSH + insulin
GSSG + reduced insulin chain A and B
-
proinsulin
-
-
?
GSH + insulin
GSSG + reduced insulin chain A and B
-
-
-
-
?
GSH + insulin
GSSG + reduced insulin chain A and B
-
-
-
-
?
GSH + insulin
GSSG + reduced insulin chain A and B
-
proinsulin
-
-
?
GSH + insulin
GSSG + reduced insulin chain A and B
-
proinsulin
-
-
?
GSH + insulin
GSSG + reduced insulin chain A and B
-
proinsulin
-
-
?
GSH + oxytoxin
?
-
-
-
-
?
GSH + oxytoxin
?
-
-
-
-
?
GSH + oxytoxin
?
-
-
-
-
?
GSH + oxytoxin
?
-
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
r
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
r
GSH + protein disulfide
GSSG + protein-dithiol
-
protein disulfide: e.g. of alcohol dehydrogenase, hexokinase, fructose-1,6-diphosphatase, malate dehydrogenase, glyceraldehyde phosphate dehydrogenase, glycerol phosphate dehydrogenase
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
prolactin is a poor substrate
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
physiological function
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
reductive degradation and assembly of proteins
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
modulation of enzymatic activity from latent to active form and vice versa
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
feedback control via insulin in the liver
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
protein disulfide: thioredoxin
-
-
r
GSH + protein disulfide
GSSG + protein-dithiol
-
very rapid disulfide interchange reaction
-
-
r
GSH + protein disulfide
GSSG + protein-dithiol
-
protein disulfide: enzyme itself
-
r
GSH + protein disulfide
GSSG + protein-dithiol
-
disulfide bonding step in folding pathway of many periplasmic and outer membrane proteins with structural disulfide bonds
-
-
r
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
physiological function
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
reductive degradation and assembly of proteins
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
modulation of enzymatic activity from latent to active form and vice versa
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
feedback control via insulin in the liver
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
physiological function
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
reductive degradation and assembly of proteins
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
modulation of enzymatic activity from latent to active form and vice versa
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
major contributor to the inactivation of oxytoxin by lactating mammary gland
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
feedback control via insulin in the liver
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
synthesis of protein disulfide bond
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
enzyme plays a role in formation of intramonomer bonds common to all immunoglobulin molecules
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
physiological function
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
reductive degradation and assembly of proteins
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
modulation of enzymatic activity from latent to active form and vice versa
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
enzyme not directly involved in the subcellular processing of receptor-bound internalized insulin
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
feedback control via insulin in the liver
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
initial step in sequential insulin degradation
-
-
?
GSH + protein-disulfide
GSSG + protein-dithiol
-
-
-
-
?
GSH + protein-disulfide
GSSG + protein-dithiol
-
-
-
-
?
GSH + vasopressin
?
-
-
-
-
?
GSH + vasopressin
?
-
-
-
-
?
GSH + vasopressin
?
-
-
-
-
?
GSH + vasopressin
?
-
-
-
-
?
GSSG + reduced ribonuclease
GSH + oxidized ribonuclease
-
-
-
-
?
GSSG + reduced ribonuclease
GSH + oxidized ribonuclease
-
-
-
r
insulin disulfide + dithiothreitol
insulin + dithiothreitol disulfide
-
-
-
-
?
insulin disulfide + dithiothreitol
insulin + dithiothreitol disulfide
-
-
-
?
L-cysteine + protein disulfide
cystine + protein-dithiol
-
-
-
-
?
L-cysteine + protein disulfide
cystine + protein-dithiol
-
-
-
-
?
SdbA carrying a disulfide bond + superantigen SpeA with reduced L-cysteine residues
SdbA with reduced L-cysteine residues + superantigen SpeA carrying a disulfide bond
-
-
-
-
?
SdbA carrying a disulfide bond + superantigen SpeA with reduced L-cysteine residues
SdbA with reduced L-cysteine residues + superantigen SpeA carrying a disulfide bond
-
the superantigen SpeA contains 3 cysteine residues (Cys 87, Cys90, and Cys98) and has a disulfide bond formed between Cys87 and Cys98
-
-
?
additional information
?
-
-
bdbC and bdbD catalyze the formation of disulfide bonds that are essential for the DNA binding and uptake machinery
-
-
?
additional information
?
-
-
bdbC and bdbD catalyze the formation of disulfide bonds that are essential for the DNA binding and uptake machinery
-
-
?
additional information
?
-
-
ResA, probably together with another thiol-disulfide oxidoreductase, CcdA, is required for the the reduction of the cysteinyls in the heme binding site of apocytochrome c
-
-
?
additional information
?
-
-
StoA is a thiol-disulfide oxidoreductase that is involved in breaking disulfide bonds in cortex components or in proteins important for cortex synthesis
-
-
?
additional information
?
-
-
reduction of choleragen
-
-
?
additional information
?
-
-
the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
-
-
?
additional information
?
-
-
the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
-
-
?
additional information
?
-
-
the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
-
-
?
additional information
?
-
-
the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
-
-
?
additional information
?
-
-
immunoglobulin IgM and IgG
-
-
?
additional information
?
-
-
immunoglobulin IgM and IgG
-
-
?
additional information
?
-
-
glutathione-insulin transhydrogenase EC 1.8.4.2 and protein disulfide-isomerase EC 5.3.4.1 activities are not both catalyzed by a single enzyme species
-
-
?
additional information
?
-
-
glutathione-insulin transhydrogenase EC 1.8.4.2 and protein disulfide-isomerase EC 5.3.4.1 activities are not both catalyzed by a single enzyme species
-
-
?
additional information
?
-
-
glutathione-insulin transhydrogenase EC 1.8.4.2 and protein disulfide-isomerase EC 5.3.4.1 activities are not both catalyzed by a single enzyme species
-
-
?
additional information
?
-
-
scrambled lysozyme
-
-
?
additional information
?
-
-
scrambled lysozyme
-
-
?
additional information
?
-
-
scrambled trypsin inhibitor and proinsulin
-
-
?
additional information
?
-
-
thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
-
-
?
additional information
?
-
-
thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
-
-
?
additional information
?
-
-
thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
-
-
?
additional information
?
-
-
enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease
-
-
?
additional information
?
-
-
enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease
-
-
?
additional information
?
-
-
enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease
-
-
?
additional information
?
-
-
reduction of ricin and other plant thiols
-
-
?
additional information
?
-
GRX1is a typical CPYC-type GRX, which is reduced by GSH and exhibits disulfide reductase, dehydroascorbate reductase, and deglutathionylation activities
-
-
-
additional information
?
-
GRX1is a typical CPYC-type GRX, which is reduced by GSH and exhibits disulfide reductase, dehydroascorbate reductase, and deglutathionylation activities
-
-
-
additional information
?
-
no substrate: insulin disulfide, 2-mercaptoethanol glutathione disulfide
-
-
-
additional information
?
-
no substrate: insulin disulfide, 2-mercaptoethanol glutathione disulfide
-
-
-
additional information
?
-
-
MdbACm directly catalyzes disulfide bond formation in proteins in vitro
-
-
-
additional information
?
-
-
MdbACm directly catalyzes disulfide bond formation in proteins in vitro
-
-
-
additional information
?
-
-
the enzyme is unable to reduce insulin
-
-
?
additional information
?
-
-
redox reaction between different Dsn proteins
-
-
?
additional information
?
-
-
DsbB protein re-oxidizes the reduced DsbA protein
-
-
?
additional information
?
-
-
DsbB protein re-oxidizes the reduced DsbA protein
-
-
?
additional information
?
-
-
the enzyme is required for efficient disulfide bond formation in the periplasm
-
-
?
additional information
?
-
-
the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
-
-
?
additional information
?
-
-
the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
-
-
?
additional information
?
-
-
immunoglobulin IgM and IgG
-
-
?
additional information
?
-
-
immunoglobulin IgM and IgG
-
-
?
additional information
?
-
-
scrambled lysozyme
-
-
?
additional information
?
-
-
scrambled lysozyme
-
-
?
additional information
?
-
-
scrambled trypsin inhibitor and proinsulin
-
-
?
additional information
?
-
-
thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
-
-
?
additional information
?
-
-
thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
-
-
?
additional information
?
-
-
enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease
-
-
?
additional information
?
-
-
enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease
-
-
?
additional information
?
-
-
multifunctional enzyme that efficiently catalyzes disulfide reduction, disulfide isomerization, and dithiol oxidation
-
-
?
additional information
?
-
COA6 interacts with COX2 and SCO proteins in vivo
-
-
-
additional information
?
-
at least in vitro SCO1 is the dominant interacting partner of COA6 compared to SCO2. H3 and C-terminal residues of COA6 are critical for its interaction with SCO1
-
-
-
additional information
?
-
-
the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
-
-
?
additional information
?
-
-
immunoglobulin IgM and IgG
-
-
?
additional information
?
-
-
scrambled lysozyme
-
-
?
additional information
?
-
-
thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
-
-
?
additional information
?
-
-
enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease
-
-
?
additional information
?
-
-
the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
-
-
?
additional information
?
-
-
the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
-
-
?
additional information
?
-
-
immunoglobulin IgM and IgG
-
-
?
additional information
?
-
-
immunoglobulin IgM and IgG
-
-
?
additional information
?
-
-
glutathione-insulin transhydrogenase EC 1.8.4.2 and protein disulfide-isomerase EC 5.3.4.1 activities are not both catalyzed by a single enzyme species
-
-
?
additional information
?
-
-
scrambled lysozyme
-
-
?
additional information
?
-
-
scrambled lysozyme
-
-
?
additional information
?
-
-
scrambled trypsin inhibitor and proinsulin
-
-
?
additional information
?
-
-
thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
-
-
?
additional information
?
-
-
thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
-
-
?
additional information
?
-
-
enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease
-
-
?
additional information
?
-
-
enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease
-
-
?
additional information
?
-
-
reduction of ricin and other plant thiols
-
-
?
additional information
?
-
COA6 interacts with COX2 and SCO proteins in vivo
-
-
-
additional information
?
-
yeast Coa6 interacts with both Sco1 and Sco2
-
-
-
additional information
?
-
COA6 interacts with COX2 and SCO proteins in vivo
-
-
-
additional information
?
-
yeast Coa6 interacts with both Sco1 and Sco2
-
-
-
additional information
?
-
oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed
-
-
-
additional information
?
-
oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed
-
-
-
additional information
?
-
oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed
-
-
-
additional information
?
-
oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed
-
-
-
additional information
?
-
oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed
-
-
-
additional information
?
-
oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed
-
-
-
additional information
?
-
oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed
-
-
-
additional information
?
-
-
addition of GSH-dependent protein disulfide oxidoreductase to flour significantly increases dough extensibility (from 17 to 49% for cultivars with different quality), which implies the ability of the enzyme to disrupt disulfide bonds in high-molecular-weight gluten polymers
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 glutathione + COX2-disulfide
glutathione-disulfide + COX2-dithiol
2 glutathione + pilin FimA-disulfide
glutathione-disulfide + pilin FimA-dithiol
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
2 glutathione + SCO1-disulfide
glutathione-disulfide + SCO1-dithiol
2 glutathione + SCO2-disulfide
glutathione-disulfide + SCO2-dithiol
-
-
-
?
GSH + AtlS
GSSG + ?
-
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
GSH + protein-disulfide
GSSG + protein-dithiol
SdbA carrying a disulfide bond + superantigen SpeA with reduced L-cysteine residues
SdbA with reduced L-cysteine residues + superantigen SpeA carrying a disulfide bond
-
-
-
-
?
additional information
?
-
2 glutathione + COX2-disulfide
glutathione-disulfide + COX2-dithiol
-
-
-
?
2 glutathione + COX2-disulfide
glutathione-disulfide + COX2-dithiol
-
-
-
?
2 glutathione + COX2-disulfide
glutathione-disulfide + COX2-dithiol
-
-
-
?
2 glutathione + pilin FimA-disulfide
glutathione-disulfide + pilin FimA-dithiol
-
-
-
-
?
2 glutathione + pilin FimA-disulfide
glutathione-disulfide + pilin FimA-dithiol
-
-
-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
-
-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
-
-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
-
-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
-
-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
-
-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
-
-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + SCO1-disulfide
glutathione-disulfide + SCO1-dithiol
-
-
-
?
2 glutathione + SCO1-disulfide
glutathione-disulfide + SCO1-dithiol
-
-
-
?
2 glutathione + SCO1-disulfide
glutathione-disulfide + SCO1-dithiol
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
physiological function
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
reductive degradation and assembly of proteins
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
modulation of enzymatic activity from latent to active form and vice versa
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
feedback control via insulin in the liver
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
disulfide bonding step in folding pathway of many periplasmic and outer membrane proteins with structural disulfide bonds
-
-
r
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
physiological function
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
reductive degradation and assembly of proteins
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
modulation of enzymatic activity from latent to active form and vice versa
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
feedback control via insulin in the liver
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
physiological function
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
reductive degradation and assembly of proteins
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
modulation of enzymatic activity from latent to active form and vice versa
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
major contributor to the inactivation of oxytoxin by lactating mammary gland
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
feedback control via insulin in the liver
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
synthesis of protein disulfide bond
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
enzyme plays a role in formation of intramonomer bonds common to all immunoglobulin molecules
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
-
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
physiological function
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
reductive degradation and assembly of proteins
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
modulation of enzymatic activity from latent to active form and vice versa
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
enzyme not directly involved in the subcellular processing of receptor-bound internalized insulin
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
feedback control via insulin in the liver
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
initial step in sequential insulin degradation
-
-
?
GSH + protein-disulfide
GSSG + protein-dithiol
-
-
-
-
?
GSH + protein-disulfide
GSSG + protein-dithiol
-
-
-
-
?
additional information
?
-
-
bdbC and bdbD catalyze the formation of disulfide bonds that are essential for the DNA binding and uptake machinery
-
-
?
additional information
?
-
-
bdbC and bdbD catalyze the formation of disulfide bonds that are essential for the DNA binding and uptake machinery
-
-
?
additional information
?
-
-
ResA, probably together with another thiol-disulfide oxidoreductase, CcdA, is required for the the reduction of the cysteinyls in the heme binding site of apocytochrome c
-
-
?
additional information
?
-
-
StoA is a thiol-disulfide oxidoreductase that is involved in breaking disulfide bonds in cortex components or in proteins important for cortex synthesis
-
-
?
additional information
?
-
-
the enzyme is required for efficient disulfide bond formation in the periplasm
-
-
?
additional information
?
-
COA6 interacts with COX2 and SCO proteins in vivo
-
-
-
additional information
?
-
COA6 interacts with COX2 and SCO proteins in vivo
-
-
-
additional information
?
-
COA6 interacts with COX2 and SCO proteins in vivo
-
-
-
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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evolution
DsbA is a periplasmic thiol-disulfide oxidoreductase that belongs to the thioredoxin family of proteins with a CxxC conserved domain
evolution
homologues of SdbA appear to be present in a range of Gram-positive bacteria that lack DsbA. SdbA is able to introduce a disulfide bond into its natural substrate, the major autolysin AtlS. This can be achieved with a single C-terminal cysteine in its CPDC active site, further suggesting SdbA is quite different from DsbA
evolution
-
the oxidoreductase MdbA identified from Corynebacterium matruchotii is highly homologous to the Corynebacterium diphtheriae thiol-disulfide oxidoreductase MdbA (MdbACd). The disulfide oxidoreductase activity requires the catalytic motif CXXC. MdbACm is a major thiol-disulfide oxidoreductase, which likely mediates posttranslocational protein folding in Corynebacterium matruchotii by a mechanism that is conserved in Actinobacteria, the enzyme is essential in the organism. Corynebacterium matruchotii MdbA can replace Corynebacterium diphtheriae MdbA in mutants to maintain normal cell growth and morphology, toxin production, and pilus assembly. The protein active site closely resembles active sites of other MdbA/DsbA enzymes. The superposition of Corynebacterium matruchotii and Corynebacterium diphtheriae MdbA active sites does not show notable changes of active-site arrangement, overview
evolution
-
homologues of SdbA appear to be present in a range of Gram-positive bacteria that lack DsbA. SdbA is able to introduce a disulfide bond into its natural substrate, the major autolysin AtlS. This can be achieved with a single C-terminal cysteine in its CPDC active site, further suggesting SdbA is quite different from DsbA
-
evolution
-
homologues of SdbA appear to be present in a range of Gram-positive bacteria that lack DsbA. SdbA is able to introduce a disulfide bond into its natural substrate, the major autolysin AtlS. This can be achieved with a single C-terminal cysteine in its CPDC active site, further suggesting SdbA is quite different from DsbA
-
evolution
-
DsbA is a periplasmic thiol-disulfide oxidoreductase that belongs to the thioredoxin family of proteins with a CxxC conserved domain
-
evolution
-
the oxidoreductase MdbA identified from Corynebacterium matruchotii is highly homologous to the Corynebacterium diphtheriae thiol-disulfide oxidoreductase MdbA (MdbACd). The disulfide oxidoreductase activity requires the catalytic motif CXXC. MdbACm is a major thiol-disulfide oxidoreductase, which likely mediates posttranslocational protein folding in Corynebacterium matruchotii by a mechanism that is conserved in Actinobacteria, the enzyme is essential in the organism. Corynebacterium matruchotii MdbA can replace Corynebacterium diphtheriae MdbA in mutants to maintain normal cell growth and morphology, toxin production, and pilus assembly. The protein active site closely resembles active sites of other MdbA/DsbA enzymes. The superposition of Corynebacterium matruchotii and Corynebacterium diphtheriae MdbA active sites does not show notable changes of active-site arrangement, overview
-
evolution
-
homologues of SdbA appear to be present in a range of Gram-positive bacteria that lack DsbA. SdbA is able to introduce a disulfide bond into its natural substrate, the major autolysin AtlS. This can be achieved with a single C-terminal cysteine in its CPDC active site, further suggesting SdbA is quite different from DsbA
-
evolution
-
homologues of SdbA appear to be present in a range of Gram-positive bacteria that lack DsbA. SdbA is able to introduce a disulfide bond into its natural substrate, the major autolysin AtlS. This can be achieved with a single C-terminal cysteine in its CPDC active site, further suggesting SdbA is quite different from DsbA
-
evolution
-
DsbA is a periplasmic thiol-disulfide oxidoreductase that belongs to the thioredoxin family of proteins with a CxxC conserved domain
-
evolution
-
homologues of SdbA appear to be present in a range of Gram-positive bacteria that lack DsbA. SdbA is able to introduce a disulfide bond into its natural substrate, the major autolysin AtlS. This can be achieved with a single C-terminal cysteine in its CPDC active site, further suggesting SdbA is quite different from DsbA
-
evolution
-
DsbA is a periplasmic thiol-disulfide oxidoreductase that belongs to the thioredoxin family of proteins with a CxxC conserved domain
-
evolution
-
homologues of SdbA appear to be present in a range of Gram-positive bacteria that lack DsbA. SdbA is able to introduce a disulfide bond into its natural substrate, the major autolysin AtlS. This can be achieved with a single C-terminal cysteine in its CPDC active site, further suggesting SdbA is quite different from DsbA
-
malfunction
gene sdbA mutants are defective in autolysis, extracellular DNA (eDNA) release, bacteriocin production, and genetic competence but form more biofilm. Inactivation of sdbA upregulates the CiaRH two-component regulatory system in Streptococcus gordonii, leading to the repression of the ComDE quorum sensing system, which results in the enhanced biofilm formation and the lack of bacteriocin production. The sdbB-ccdA2 mutant produces all of the phenotypes displayed by the sdbA mutant. The sdbB-sgo_1177 mutant is defective in eDNA release and bacteriocin production but not autolysis or genetic competence. The sdbB-ccdA1 mutant is defective in autolysis but not eDNA release, bacteriocin production, or genetic competence. The sgo_1177-ccdA2 mutant is partially defective in autolysis but not in other phenotypes. The ccdA1-ccdA2 mutant is defective only in bacteriocin production. AtlS, the natural substrate of SdbA, in the sdbB-ccdA2 mutant lacks activity and a disulfide bond. The lack of autolysis in the sdbB-ccdA2 mutant is due to a defect in the activity of AtlS. Enzyme mutant SdbAC89A variant forms mixed disulfide with SdbB in vivo
malfunction
-
SpeA in the culture supernatant remains reduced when gene sdbA is inactivated and restored to the oxidized state when a functional copy of sdbA is returned to the sdbA-knockout mutant. Complementation of sdbA deletion restores SpeA to an oxidized state. The enzyme mutant SdbAC49A forms a mixed disulfide with substrate mutant SpeAC87A. No reactions between SdbAC49A and SpeAC98A, SdbAC46A and SpeAC87A, or SdbAC46A and SpeAC98A
malfunction
the purple non-sulfur bacterium Rhodobacter capsulatus mutants lacking DsbA show severe temperature-sensitive and medium-dependent respiratory growth defects. Absence of thiol-disulfide oxidoreductase DsbA impairs cbb3-type cytochrome c oxidase (cbb3-Cox) biogenesis in Rhodobacter capsulatus. Absence of DsbA, besides impairing the maturation of the c-type cytochrome subunits, also affects the incorporation of Cu into the catalytic subunit of cbb3-Cox. Defective high affinity Cu acquisition pathway, which includes the MFS-type Cu importer CcoA, and lower production of the c-type cytochrome subunits lead together to improper assembly and degradation of cbb3-Cox. DsbA- and several cbb3-Cox biogenesis mutants exhibit similar phenotypes. Mutational analysis of enzyme function, overview
malfunction
the truncation mutation (E87X) clearly disrupts the CHCH domain by removing a large portion of the protein from helix 2 onward. The other two mutations, W59C and W66R, are found within the first helix of COA6, where the side chains of each tryptophan face the bulk solvent, suggesting that these residues may facilitate interactions with their client proteins. Overexpression of the wild-type and mutant alleles of COA6 in control and COA6 patient fibroblasts shows that the W66R variant fails to rescue CcO activity. In contrast, expression of the W59C mutant leads to a partial recovery of CcO activity and COX2 levels. It seems that in most cell types residual levels of the partially functional W59C allele are not sufficient to support CcO assembly and mitochondrial respiration because coa6DELTA cells expressing the W59C variant do not exhibit respiratory growth. The human patient with the W59C mutation exhibits a severe CcO deficiency in cardiac tissue
malfunction
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gene sdbA mutants are defective in autolysis, extracellular DNA (eDNA) release, bacteriocin production, and genetic competence but form more biofilm. Inactivation of sdbA upregulates the CiaRH two-component regulatory system in Streptococcus gordonii, leading to the repression of the ComDE quorum sensing system, which results in the enhanced biofilm formation and the lack of bacteriocin production. The sdbB-ccdA2 mutant produces all of the phenotypes displayed by the sdbA mutant. The sdbB-sgo_1177 mutant is defective in eDNA release and bacteriocin production but not autolysis or genetic competence. The sdbB-ccdA1 mutant is defective in autolysis but not eDNA release, bacteriocin production, or genetic competence. The sgo_1177-ccdA2 mutant is partially defective in autolysis but not in other phenotypes. The ccdA1-ccdA2 mutant is defective only in bacteriocin production. AtlS, the natural substrate of SdbA, in the sdbB-ccdA2 mutant lacks activity and a disulfide bond. The lack of autolysis in the sdbB-ccdA2 mutant is due to a defect in the activity of AtlS. Enzyme mutant SdbAC89A variant forms mixed disulfide with SdbB in vivo
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malfunction
-
gene sdbA mutants are defective in autolysis, extracellular DNA (eDNA) release, bacteriocin production, and genetic competence but form more biofilm. Inactivation of sdbA upregulates the CiaRH two-component regulatory system in Streptococcus gordonii, leading to the repression of the ComDE quorum sensing system, which results in the enhanced biofilm formation and the lack of bacteriocin production. The sdbB-ccdA2 mutant produces all of the phenotypes displayed by the sdbA mutant. The sdbB-sgo_1177 mutant is defective in eDNA release and bacteriocin production but not autolysis or genetic competence. The sdbB-ccdA1 mutant is defective in autolysis but not eDNA release, bacteriocin production, or genetic competence. The sgo_1177-ccdA2 mutant is partially defective in autolysis but not in other phenotypes. The ccdA1-ccdA2 mutant is defective only in bacteriocin production. AtlS, the natural substrate of SdbA, in the sdbB-ccdA2 mutant lacks activity and a disulfide bond. The lack of autolysis in the sdbB-ccdA2 mutant is due to a defect in the activity of AtlS. Enzyme mutant SdbAC89A variant forms mixed disulfide with SdbB in vivo
-
malfunction
-
the purple non-sulfur bacterium Rhodobacter capsulatus mutants lacking DsbA show severe temperature-sensitive and medium-dependent respiratory growth defects. Absence of thiol-disulfide oxidoreductase DsbA impairs cbb3-type cytochrome c oxidase (cbb3-Cox) biogenesis in Rhodobacter capsulatus. Absence of DsbA, besides impairing the maturation of the c-type cytochrome subunits, also affects the incorporation of Cu into the catalytic subunit of cbb3-Cox. Defective high affinity Cu acquisition pathway, which includes the MFS-type Cu importer CcoA, and lower production of the c-type cytochrome subunits lead together to improper assembly and degradation of cbb3-Cox. DsbA- and several cbb3-Cox biogenesis mutants exhibit similar phenotypes. Mutational analysis of enzyme function, overview
-
malfunction
-
gene sdbA mutants are defective in autolysis, extracellular DNA (eDNA) release, bacteriocin production, and genetic competence but form more biofilm. Inactivation of sdbA upregulates the CiaRH two-component regulatory system in Streptococcus gordonii, leading to the repression of the ComDE quorum sensing system, which results in the enhanced biofilm formation and the lack of bacteriocin production. The sdbB-ccdA2 mutant produces all of the phenotypes displayed by the sdbA mutant. The sdbB-sgo_1177 mutant is defective in eDNA release and bacteriocin production but not autolysis or genetic competence. The sdbB-ccdA1 mutant is defective in autolysis but not eDNA release, bacteriocin production, or genetic competence. The sgo_1177-ccdA2 mutant is partially defective in autolysis but not in other phenotypes. The ccdA1-ccdA2 mutant is defective only in bacteriocin production. AtlS, the natural substrate of SdbA, in the sdbB-ccdA2 mutant lacks activity and a disulfide bond. The lack of autolysis in the sdbB-ccdA2 mutant is due to a defect in the activity of AtlS. Enzyme mutant SdbAC89A variant forms mixed disulfide with SdbB in vivo
-
malfunction
-
gene sdbA mutants are defective in autolysis, extracellular DNA (eDNA) release, bacteriocin production, and genetic competence but form more biofilm. Inactivation of sdbA upregulates the CiaRH two-component regulatory system in Streptococcus gordonii, leading to the repression of the ComDE quorum sensing system, which results in the enhanced biofilm formation and the lack of bacteriocin production. The sdbB-ccdA2 mutant produces all of the phenotypes displayed by the sdbA mutant. The sdbB-sgo_1177 mutant is defective in eDNA release and bacteriocin production but not autolysis or genetic competence. The sdbB-ccdA1 mutant is defective in autolysis but not eDNA release, bacteriocin production, or genetic competence. The sgo_1177-ccdA2 mutant is partially defective in autolysis but not in other phenotypes. The ccdA1-ccdA2 mutant is defective only in bacteriocin production. AtlS, the natural substrate of SdbA, in the sdbB-ccdA2 mutant lacks activity and a disulfide bond. The lack of autolysis in the sdbB-ccdA2 mutant is due to a defect in the activity of AtlS. Enzyme mutant SdbAC89A variant forms mixed disulfide with SdbB in vivo
-
malfunction
-
the purple non-sulfur bacterium Rhodobacter capsulatus mutants lacking DsbA show severe temperature-sensitive and medium-dependent respiratory growth defects. Absence of thiol-disulfide oxidoreductase DsbA impairs cbb3-type cytochrome c oxidase (cbb3-Cox) biogenesis in Rhodobacter capsulatus. Absence of DsbA, besides impairing the maturation of the c-type cytochrome subunits, also affects the incorporation of Cu into the catalytic subunit of cbb3-Cox. Defective high affinity Cu acquisition pathway, which includes the MFS-type Cu importer CcoA, and lower production of the c-type cytochrome subunits lead together to improper assembly and degradation of cbb3-Cox. DsbA- and several cbb3-Cox biogenesis mutants exhibit similar phenotypes. Mutational analysis of enzyme function, overview
-
malfunction
-
gene sdbA mutants are defective in autolysis, extracellular DNA (eDNA) release, bacteriocin production, and genetic competence but form more biofilm. Inactivation of sdbA upregulates the CiaRH two-component regulatory system in Streptococcus gordonii, leading to the repression of the ComDE quorum sensing system, which results in the enhanced biofilm formation and the lack of bacteriocin production. The sdbB-ccdA2 mutant produces all of the phenotypes displayed by the sdbA mutant. The sdbB-sgo_1177 mutant is defective in eDNA release and bacteriocin production but not autolysis or genetic competence. The sdbB-ccdA1 mutant is defective in autolysis but not eDNA release, bacteriocin production, or genetic competence. The sgo_1177-ccdA2 mutant is partially defective in autolysis but not in other phenotypes. The ccdA1-ccdA2 mutant is defective only in bacteriocin production. AtlS, the natural substrate of SdbA, in the sdbB-ccdA2 mutant lacks activity and a disulfide bond. The lack of autolysis in the sdbB-ccdA2 mutant is due to a defect in the activity of AtlS. Enzyme mutant SdbAC89A variant forms mixed disulfide with SdbB in vivo
-
malfunction
-
the purple non-sulfur bacterium Rhodobacter capsulatus mutants lacking DsbA show severe temperature-sensitive and medium-dependent respiratory growth defects. Absence of thiol-disulfide oxidoreductase DsbA impairs cbb3-type cytochrome c oxidase (cbb3-Cox) biogenesis in Rhodobacter capsulatus. Absence of DsbA, besides impairing the maturation of the c-type cytochrome subunits, also affects the incorporation of Cu into the catalytic subunit of cbb3-Cox. Defective high affinity Cu acquisition pathway, which includes the MFS-type Cu importer CcoA, and lower production of the c-type cytochrome subunits lead together to improper assembly and degradation of cbb3-Cox. DsbA- and several cbb3-Cox biogenesis mutants exhibit similar phenotypes. Mutational analysis of enzyme function, overview
-
malfunction
-
gene sdbA mutants are defective in autolysis, extracellular DNA (eDNA) release, bacteriocin production, and genetic competence but form more biofilm. Inactivation of sdbA upregulates the CiaRH two-component regulatory system in Streptococcus gordonii, leading to the repression of the ComDE quorum sensing system, which results in the enhanced biofilm formation and the lack of bacteriocin production. The sdbB-ccdA2 mutant produces all of the phenotypes displayed by the sdbA mutant. The sdbB-sgo_1177 mutant is defective in eDNA release and bacteriocin production but not autolysis or genetic competence. The sdbB-ccdA1 mutant is defective in autolysis but not eDNA release, bacteriocin production, or genetic competence. The sgo_1177-ccdA2 mutant is partially defective in autolysis but not in other phenotypes. The ccdA1-ccdA2 mutant is defective only in bacteriocin production. AtlS, the natural substrate of SdbA, in the sdbB-ccdA2 mutant lacks activity and a disulfide bond. The lack of autolysis in the sdbB-ccdA2 mutant is due to a defect in the activity of AtlS. Enzyme mutant SdbAC89A variant forms mixed disulfide with SdbB in vivo
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metabolism
-
the enzyme affects multiple phenotypes in Streptococcus gordonii and is required for production of disulfide-bonded proteins like Anti-CR1 scFv
metabolism
-
enzyme reacts with glutathionylated substrates in a GSH-dependent ping pong mechanism. The pKa of GrxS12 catalytic Cys29 is very low (3.9) and makes GrxS12 itself sensitive to oxidation by H2O2 and to direct glutathionylation by nitrosoglutathione. Glutathionylated-GrxS12 is temporarily inactive until it is deglutathionylated by GSH
metabolism
identification and characterization of the SdbA redox partners SdbB and CcdA2 (encoded by gene ccdA2) in Streptococcus gordonii. CcdA2 is annotated as cytochrome c biogenesis protein A. Thiol-disulfide oxidoreductase-associated lipoprotein SdbB, encoded by gene sgo_1177, constitutes the main pathway for SdbA reoxidation. SdbA has multiple redox partners, e.g. SdbB and CcdA2, forming a complex oxidative protein-folding pathway. This pathway is essential for autolysis, bacteriocin production, genetic competence, and extracellular DNA (eDNA) release in Streptococcus gordonii
metabolism
posttranslocational protein folding in the Gram-positive biofilm-forming actinobacterium Actinomyces oris is mediated by membrane-bound thiol-disulfide oxidoreductase, MdbA, which catalyzes oxidative folding of nascent polypeptides transported by the Sec translocon. Reoxidation of MdbA involves a bacterial vitamin K epoxide reductase (VKOR)-like protein that contains four cysteine residues, C93/C101 and C175/C178, with the latter forming a canonical CXXC thioredoxin-like motif. Topological view of the Actinomyces oris membrane-spanning protein VKOR with these four exoplasmic cysteine residues that participate in MdbA reoxidation. Like deletion of the VKOR gene, alanine replacement of individual cysteine residues abrogates polymicrobial interactions and biofilm formation, concomitant with the failure to form adhesive pili on the bacterial surface. Mutational analysis of VKOR function, overview. The C93 residue of VKOR is postulated to form a mixed disulfide bond with MdbA
metabolism
-
the actinobacterium Corynebacterium matruchotii has been implicated in nucleation of oral microbial consortia leading to biofilm formation
metabolism
-
identification and characterization of the SdbA redox partners SdbB and CcdA2 (encoded by gene ccdA2) in Streptococcus gordonii. CcdA2 is annotated as cytochrome c biogenesis protein A. Thiol-disulfide oxidoreductase-associated lipoprotein SdbB, encoded by gene sgo_1177, constitutes the main pathway for SdbA reoxidation. SdbA has multiple redox partners, e.g. SdbB and CcdA2, forming a complex oxidative protein-folding pathway. This pathway is essential for autolysis, bacteriocin production, genetic competence, and extracellular DNA (eDNA) release in Streptococcus gordonii
-
metabolism
-
identification and characterization of the SdbA redox partners SdbB and CcdA2 (encoded by gene ccdA2) in Streptococcus gordonii. CcdA2 is annotated as cytochrome c biogenesis protein A. Thiol-disulfide oxidoreductase-associated lipoprotein SdbB, encoded by gene sgo_1177, constitutes the main pathway for SdbA reoxidation. SdbA has multiple redox partners, e.g. SdbB and CcdA2, forming a complex oxidative protein-folding pathway. This pathway is essential for autolysis, bacteriocin production, genetic competence, and extracellular DNA (eDNA) release in Streptococcus gordonii
-
metabolism
-
the actinobacterium Corynebacterium matruchotii has been implicated in nucleation of oral microbial consortia leading to biofilm formation
-
metabolism
-
identification and characterization of the SdbA redox partners SdbB and CcdA2 (encoded by gene ccdA2) in Streptococcus gordonii. CcdA2 is annotated as cytochrome c biogenesis protein A. Thiol-disulfide oxidoreductase-associated lipoprotein SdbB, encoded by gene sgo_1177, constitutes the main pathway for SdbA reoxidation. SdbA has multiple redox partners, e.g. SdbB and CcdA2, forming a complex oxidative protein-folding pathway. This pathway is essential for autolysis, bacteriocin production, genetic competence, and extracellular DNA (eDNA) release in Streptococcus gordonii
-
metabolism
-
identification and characterization of the SdbA redox partners SdbB and CcdA2 (encoded by gene ccdA2) in Streptococcus gordonii. CcdA2 is annotated as cytochrome c biogenesis protein A. Thiol-disulfide oxidoreductase-associated lipoprotein SdbB, encoded by gene sgo_1177, constitutes the main pathway for SdbA reoxidation. SdbA has multiple redox partners, e.g. SdbB and CcdA2, forming a complex oxidative protein-folding pathway. This pathway is essential for autolysis, bacteriocin production, genetic competence, and extracellular DNA (eDNA) release in Streptococcus gordonii
-
metabolism
-
identification and characterization of the SdbA redox partners SdbB and CcdA2 (encoded by gene ccdA2) in Streptococcus gordonii. CcdA2 is annotated as cytochrome c biogenesis protein A. Thiol-disulfide oxidoreductase-associated lipoprotein SdbB, encoded by gene sgo_1177, constitutes the main pathway for SdbA reoxidation. SdbA has multiple redox partners, e.g. SdbB and CcdA2, forming a complex oxidative protein-folding pathway. This pathway is essential for autolysis, bacteriocin production, genetic competence, and extracellular DNA (eDNA) release in Streptococcus gordonii
-
metabolism
-
identification and characterization of the SdbA redox partners SdbB and CcdA2 (encoded by gene ccdA2) in Streptococcus gordonii. CcdA2 is annotated as cytochrome c biogenesis protein A. Thiol-disulfide oxidoreductase-associated lipoprotein SdbB, encoded by gene sgo_1177, constitutes the main pathway for SdbA reoxidation. SdbA has multiple redox partners, e.g. SdbB and CcdA2, forming a complex oxidative protein-folding pathway. This pathway is essential for autolysis, bacteriocin production, genetic competence, and extracellular DNA (eDNA) release in Streptococcus gordonii
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physiological function
a significant portion of protein HP_0377 is present in the oxidized form in an HP_0231 mutant
physiological function
gene deletion results in a severe growth defect at 37°C. By electron microscopy, the MdbA mutant is indistinguishable from wild-type at 30°C. At 37°C, the mutant becomes chained, clumped and coccoid in appearance. The mutant also fails to assemble pilus structures and is greatly defective in toxin production
physiological function
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inactivation of SdbA results in enhanced biofilm formation. Biofilm formation is mediated by the interaction between the CiaRH and ComDE two-component signalling systems. CiaRH is upregulated in the SdbA mutant and is essential for the enhanced biofilm phenotype. The enhanced biofilm phenotype also corresponds to increased oral colonization in mice
physiological function
-
isoform DsbA1 is essential for the motility and autoagglutination phenotypes, and plays a critical role in the oxidative folding of alkaline phosphatase PhoX
physiological function
-
loss of isoform DsbA2 has no impact on motility and autoagglutination phenotypes. DsbA2 is crucial for the activity of arylsulfotransferase AstA
physiological function
reoxidation of MdbA involves bacterial vitamin K epoxide reductase-like protein that contains four cysteine residues, C93/C101 and C175/C178. Mutation C101A in this protein results in a high molecular weight complex of MdbA and bacterial vitamin K epoxide reductase-like protein
physiological function
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SdbA mutants lack bacteriocin activity due to strong repression of bacteriocin gene. The Com pathway is functional but not activated in the SdbA mutant. Repression of bacteriocin production is mediated by the CiaRH two-component system, which is strongly upregulated in the sdbA mutant. The CiaRH-induced protease DegP is also upregulated in the SdbA mutant
physiological function
CGFS-type GRX is not reduced by GSH and has an atypically low redox potential (-323 mV at pH 7.9). GRX3 can be reduced in the light by photoreduced ferredoxin and ferredoxin-thioredoxin reductase
physiological function
isoform GRX5 is not an efficient catalyst of protein deglutathionylation nor exhibits distinct substrate specificities
physiological function
isoform GRX6 is not an efficient catalyst of protein deglutathionylation nor exhibits distinct substrate specificities
physiological function
in eukaryotes, cellular respiration is driven by mitochondrial cytochrome c oxidase (CcO), an enzyme complex that requires copper cofactors for its catalytic activity. Insertion of copper into its catalytically active subunits, including COX2, is a complex process that requires metallochaperones and redox proteins including SCO1, SCO2, and COA6. COA6 is structurally tuned to function as a thiol-disulfide oxidoreductase in copper delivery to mitochondrial cytochrome c oxidase. COA6 can reduce the copper-coordinating disulfides of its client proteins, SCO1 and COX2, allowing for copper binding. Determination of the interaction surfaces and reduction potentials of COA6 and its client proteins provides a mechanism of how metallochaperone and disulfide reductase activities are coordinated to deliver copper to CcO, overview. COA6 acts as a disulfide reductase of SCO and COX2 proteins
physiological function
in eukaryotes, cellular respiration is driven by mitochondrial cytochrome c oxidase (CcO), an enzyme complex that requires copper cofactors for its catalytic activity. Insertion of copper into its catalytically active subunits, including COX2, is a complex process that requires metallochaperones and redox proteins including SCO1, SCO2, and COA6. COA6 is structurally tuned to function as a thiol-disulfide oxidoreductase in copper delivery to mitochondrial cytochrome c oxidase. COA6 can reduce the copper-coordinating disulfides of its client proteins, SCO1 and COX2, allowing for copper binding. Determination of the interaction surfaces and reduction potentials of COA6 and its client proteins provides a mechanism of how metallochaperone and disulfide reductase activities are coordinated to deliver copper to CcO, overview. COA6 function can be bypassed in a reducing environment. Coa6 has a redox as opposed to a metallochaperone function in Cu delivery to Cox2. COA6 acts as a disulfide reductase of SCO and COX2 proteins. COA6 can reduce the disulfides of SCO proteins, generating free sulfhydryl groups. COA6 can also reduce the cysteines of COX2
physiological function
posttranslocational protein folding in the Gram-positive biofilm-forming actinobacterium Actinomyces oris is mediated by membrane-bound thiol-disulfide oxidoreductase, MdbA, which catalyzes oxidative folding of nascent polypeptides transported by the Sec translocon
physiological function
-
SpyM18_2037, named SdbA, is the catalyst that introduces the disulfide bond in SpeA. Enzyme SdbA has a typical C46XXC49 active site motif commonly found in TDORs. The cysteines in the CXXC motif are required for the disulfide bond in SpeA to form. Interactions between SdbA and SpeA are examined using cysteine variant proteins. The results show that SdbAC49A forms a mixed disulfide with SpeAC87A, suggesting that the N-terminal Cys46 of SdbA and the C-terminal Cys98 of SpeA participate in the initial reaction. SpeA oxidized by SdbA displays biological activities suggesting that SpeA is properly folded following oxidation by SdbA. The enzyme substrate superantigen exotoxin A, SpeA (25 kDa) contains three cysteine residues (Cys87, Cys90, and Cys98). In the crystal structure of SpeA, Cys87 and Cys98 are linked by a disulfide bond. The disulfide bond and neighboring amino acids form a socalled disulfide loop, which is a conserved feature in all staphylococcal enterotoxins except the toxic shock syndrome toxin 1 (TSST-1). The importance of the disulfide bond in SpeA and staphylococcal enterotoxins (e.g. SEC2). SpeA and other streptococcal and staphylococcal superantigens are able to bind simultaneously to the major histocompatibility complex (MHC) class II molecules and the T-cell receptors, resulting in T cell activation and massive cytokine production
physiological function
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the organism encodes a large number of exported proteins containing paired cysteine residues. Proteins possessing 2 or more cysteine residues made up 58.4% of the Corynabacterium matruchotii proteome (1530 of 2619 proteins). In the Gram-positive actinobacteria, oxidative protein folding via disulfide bond formation appears to be the major pathway for posttranslocational folding of these unfolded proteins. The oxidoreductase MdbA identified from Corynebacterium matruchotii, MdbACm, catalyzes disulfide bond formation within the actinobacterial pilin FimA
physiological function
the thiol-disulfide oxidoreductase DsbA carries out oxidative folding of extra-cytoplasmic proteins by catalyzing the formation of intramolecular disulfide bonds. It has an important role in various cellular functions, including cell division. DsbA activity is required for full respiratory capability of Rhodobacter capsulatus, and in particular, for proper biogenesis of its cbb3-type cytochrome c oxidase (cbb3-Cox). Enzyme DsbA facilitates oxidative folding of extra-cytoplasmic proteins by catalyzing the formation of intramolecular disulfide bonds between two reactive Cys residues of its substrates, which include the c-type apocyts with their conserved CxxCH heme-binding sites. Reduced DsbA is re-oxidized by its recycling partner DsbB, which then transfers the reducing equivalents to the Q pool, and eventually to the electron transport chain
physiological function
thiol-disulfide oxidoreductase, SdbA, in Streptococcus gordonii forms disulfide bonds in substrate proteins and plays a role in multiple phenotypes. SdbA has multiple redox partners, e.g. SdbB and CcdA2, forming a complex oxidative protein-folding pathway. This pathway is essential for autolysis, bacteriocin production, genetic competence, and extracellular DNA (eDNA) release in Streptococcus gordonii. These cellular processes are considered to be important for the success of Streptococcus gordonii as a dental plaque organism. Homologues of SdbA appear to be present in a range of Gram-positive bacteria that lack DsbA. SdbA is able to introduce a disulfide bond into its natural substrate, the major autolysin AtlS. This can be achieved with a single C-terminal cysteine in its CPDC active site, further suggesting SdbA is quite different from DsbA
physiological function
-
thiol-disulfide oxidoreductase, SdbA, in Streptococcus gordonii forms disulfide bonds in substrate proteins and plays a role in multiple phenotypes. SdbA has multiple redox partners, e.g. SdbB and CcdA2, forming a complex oxidative protein-folding pathway. This pathway is essential for autolysis, bacteriocin production, genetic competence, and extracellular DNA (eDNA) release in Streptococcus gordonii. These cellular processes are considered to be important for the success of Streptococcus gordonii as a dental plaque organism. Homologues of SdbA appear to be present in a range of Gram-positive bacteria that lack DsbA. SdbA is able to introduce a disulfide bond into its natural substrate, the major autolysin AtlS. This can be achieved with a single C-terminal cysteine in its CPDC active site, further suggesting SdbA is quite different from DsbA
-
physiological function
-
inactivation of SdbA results in enhanced biofilm formation. Biofilm formation is mediated by the interaction between the CiaRH and ComDE two-component signalling systems. CiaRH is upregulated in the SdbA mutant and is essential for the enhanced biofilm phenotype. The enhanced biofilm phenotype also corresponds to increased oral colonization in mice
-
physiological function
-
SdbA mutants lack bacteriocin activity due to strong repression of bacteriocin gene. The Com pathway is functional but not activated in the SdbA mutant. Repression of bacteriocin production is mediated by the CiaRH two-component system, which is strongly upregulated in the sdbA mutant. The CiaRH-induced protease DegP is also upregulated in the SdbA mutant
-
physiological function
-
thiol-disulfide oxidoreductase, SdbA, in Streptococcus gordonii forms disulfide bonds in substrate proteins and plays a role in multiple phenotypes. SdbA has multiple redox partners, e.g. SdbB and CcdA2, forming a complex oxidative protein-folding pathway. This pathway is essential for autolysis, bacteriocin production, genetic competence, and extracellular DNA (eDNA) release in Streptococcus gordonii. These cellular processes are considered to be important for the success of Streptococcus gordonii as a dental plaque organism. Homologues of SdbA appear to be present in a range of Gram-positive bacteria that lack DsbA. SdbA is able to introduce a disulfide bond into its natural substrate, the major autolysin AtlS. This can be achieved with a single C-terminal cysteine in its CPDC active site, further suggesting SdbA is quite different from DsbA
-
physiological function
-
the thiol-disulfide oxidoreductase DsbA carries out oxidative folding of extra-cytoplasmic proteins by catalyzing the formation of intramolecular disulfide bonds. It has an important role in various cellular functions, including cell division. DsbA activity is required for full respiratory capability of Rhodobacter capsulatus, and in particular, for proper biogenesis of its cbb3-type cytochrome c oxidase (cbb3-Cox). Enzyme DsbA facilitates oxidative folding of extra-cytoplasmic proteins by catalyzing the formation of intramolecular disulfide bonds between two reactive Cys residues of its substrates, which include the c-type apocyts with their conserved CxxCH heme-binding sites. Reduced DsbA is re-oxidized by its recycling partner DsbB, which then transfers the reducing equivalents to the Q pool, and eventually to the electron transport chain
-
physiological function
-
the organism encodes a large number of exported proteins containing paired cysteine residues. Proteins possessing 2 or more cysteine residues made up 58.4% of the Corynabacterium matruchotii proteome (1530 of 2619 proteins). In the Gram-positive actinobacteria, oxidative protein folding via disulfide bond formation appears to be the major pathway for posttranslocational folding of these unfolded proteins. The oxidoreductase MdbA identified from Corynebacterium matruchotii, MdbACm, catalyzes disulfide bond formation within the actinobacterial pilin FimA
-
physiological function
-
thiol-disulfide oxidoreductase, SdbA, in Streptococcus gordonii forms disulfide bonds in substrate proteins and plays a role in multiple phenotypes. SdbA has multiple redox partners, e.g. SdbB and CcdA2, forming a complex oxidative protein-folding pathway. This pathway is essential for autolysis, bacteriocin production, genetic competence, and extracellular DNA (eDNA) release in Streptococcus gordonii. These cellular processes are considered to be important for the success of Streptococcus gordonii as a dental plaque organism. Homologues of SdbA appear to be present in a range of Gram-positive bacteria that lack DsbA. SdbA is able to introduce a disulfide bond into its natural substrate, the major autolysin AtlS. This can be achieved with a single C-terminal cysteine in its CPDC active site, further suggesting SdbA is quite different from DsbA
-
physiological function
-
gene deletion results in a severe growth defect at 37°C. By electron microscopy, the MdbA mutant is indistinguishable from wild-type at 30°C. At 37°C, the mutant becomes chained, clumped and coccoid in appearance. The mutant also fails to assemble pilus structures and is greatly defective in toxin production
-
physiological function
-
a significant portion of protein HP_0377 is present in the oxidized form in an HP_0231 mutant
-
physiological function
-
thiol-disulfide oxidoreductase, SdbA, in Streptococcus gordonii forms disulfide bonds in substrate proteins and plays a role in multiple phenotypes. SdbA has multiple redox partners, e.g. SdbB and CcdA2, forming a complex oxidative protein-folding pathway. This pathway is essential for autolysis, bacteriocin production, genetic competence, and extracellular DNA (eDNA) release in Streptococcus gordonii. These cellular processes are considered to be important for the success of Streptococcus gordonii as a dental plaque organism. Homologues of SdbA appear to be present in a range of Gram-positive bacteria that lack DsbA. SdbA is able to introduce a disulfide bond into its natural substrate, the major autolysin AtlS. This can be achieved with a single C-terminal cysteine in its CPDC active site, further suggesting SdbA is quite different from DsbA
-
physiological function
-
the thiol-disulfide oxidoreductase DsbA carries out oxidative folding of extra-cytoplasmic proteins by catalyzing the formation of intramolecular disulfide bonds. It has an important role in various cellular functions, including cell division. DsbA activity is required for full respiratory capability of Rhodobacter capsulatus, and in particular, for proper biogenesis of its cbb3-type cytochrome c oxidase (cbb3-Cox). Enzyme DsbA facilitates oxidative folding of extra-cytoplasmic proteins by catalyzing the formation of intramolecular disulfide bonds between two reactive Cys residues of its substrates, which include the c-type apocyts with their conserved CxxCH heme-binding sites. Reduced DsbA is re-oxidized by its recycling partner DsbB, which then transfers the reducing equivalents to the Q pool, and eventually to the electron transport chain
-
physiological function
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in eukaryotes, cellular respiration is driven by mitochondrial cytochrome c oxidase (CcO), an enzyme complex that requires copper cofactors for its catalytic activity. Insertion of copper into its catalytically active subunits, including COX2, is a complex process that requires metallochaperones and redox proteins including SCO1, SCO2, and COA6. COA6 is structurally tuned to function as a thiol-disulfide oxidoreductase in copper delivery to mitochondrial cytochrome c oxidase. COA6 can reduce the copper-coordinating disulfides of its client proteins, SCO1 and COX2, allowing for copper binding. Determination of the interaction surfaces and reduction potentials of COA6 and its client proteins provides a mechanism of how metallochaperone and disulfide reductase activities are coordinated to deliver copper to CcO, overview. COA6 acts as a disulfide reductase of SCO and COX2 proteins
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physiological function
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thiol-disulfide oxidoreductase, SdbA, in Streptococcus gordonii forms disulfide bonds in substrate proteins and plays a role in multiple phenotypes. SdbA has multiple redox partners, e.g. SdbB and CcdA2, forming a complex oxidative protein-folding pathway. This pathway is essential for autolysis, bacteriocin production, genetic competence, and extracellular DNA (eDNA) release in Streptococcus gordonii. These cellular processes are considered to be important for the success of Streptococcus gordonii as a dental plaque organism. Homologues of SdbA appear to be present in a range of Gram-positive bacteria that lack DsbA. SdbA is able to introduce a disulfide bond into its natural substrate, the major autolysin AtlS. This can be achieved with a single C-terminal cysteine in its CPDC active site, further suggesting SdbA is quite different from DsbA
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physiological function
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the thiol-disulfide oxidoreductase DsbA carries out oxidative folding of extra-cytoplasmic proteins by catalyzing the formation of intramolecular disulfide bonds. It has an important role in various cellular functions, including cell division. DsbA activity is required for full respiratory capability of Rhodobacter capsulatus, and in particular, for proper biogenesis of its cbb3-type cytochrome c oxidase (cbb3-Cox). Enzyme DsbA facilitates oxidative folding of extra-cytoplasmic proteins by catalyzing the formation of intramolecular disulfide bonds between two reactive Cys residues of its substrates, which include the c-type apocyts with their conserved CxxCH heme-binding sites. Reduced DsbA is re-oxidized by its recycling partner DsbB, which then transfers the reducing equivalents to the Q pool, and eventually to the electron transport chain
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physiological function
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thiol-disulfide oxidoreductase, SdbA, in Streptococcus gordonii forms disulfide bonds in substrate proteins and plays a role in multiple phenotypes. SdbA has multiple redox partners, e.g. SdbB and CcdA2, forming a complex oxidative protein-folding pathway. This pathway is essential for autolysis, bacteriocin production, genetic competence, and extracellular DNA (eDNA) release in Streptococcus gordonii. These cellular processes are considered to be important for the success of Streptococcus gordonii as a dental plaque organism. Homologues of SdbA appear to be present in a range of Gram-positive bacteria that lack DsbA. SdbA is able to introduce a disulfide bond into its natural substrate, the major autolysin AtlS. This can be achieved with a single C-terminal cysteine in its CPDC active site, further suggesting SdbA is quite different from DsbA
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additional information
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the enzyme structure of MdbACm possesses two conserved features found in actinobacterial MdbA enzymes, a thioredoxin-like fold and an extended alpha-helical domain. The MdbA alpha-helical domain comprises 7 alpha-helices. The conserved catalytic CHYC motif (residues 91 to 94) forms the active site together with a conserved cis-Pro loop (residues S221 and P222). Structure modeling and structure comparisons, overview
additional information
the solution structure of COA6 reveals a coiled-coil-helix-coiled-coil-helix domain typical of redox-active proteins found in the mitochondrial inter-membrane space. COA6 structure analysis by NMR spectroscopy, overview
additional information
the solution structure of COA6 reveals a coiled-coil-helix-coiled-coil-helix domain typical of redox-active proteins found in the mitochondrial inter-membrane space. COA6 structure analysis by NMR spectroscopy, overview. The conserved tryptophans W59 and W66 are critical for COA6 stability and possibly for their interactions with client proteins
additional information
VKOR-mediated reactivation of MdbA appears to be conserved in the Actinobacteria. Formation of the MdbA-VKOR mixed disulfide complex requires C93. The signal of this MdbA-VKOR complex is greatly diminished when the sample is treated with 2-mercaptoethanol. The complex is not found when both C93 and C101 are mutated to alanine. The results suggest that when C101 is mutated, VKOR forms a complex with MdbA via the VKOR C93 residue
additional information
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VKOR-mediated reactivation of MdbA appears to be conserved in the Actinobacteria. Formation of the MdbA-VKOR mixed disulfide complex requires C93. The signal of this MdbA-VKOR complex is greatly diminished when the sample is treated with 2-mercaptoethanol. The complex is not found when both C93 and C101 are mutated to alanine. The results suggest that when C101 is mutated, VKOR forms a complex with MdbA via the VKOR C93 residue
additional information
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the enzyme structure of MdbACm possesses two conserved features found in actinobacterial MdbA enzymes, a thioredoxin-like fold and an extended alpha-helical domain. The MdbA alpha-helical domain comprises 7 alpha-helices. The conserved catalytic CHYC motif (residues 91 to 94) forms the active site together with a conserved cis-Pro loop (residues S221 and P222). Structure modeling and structure comparisons, overview
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additional information
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the solution structure of COA6 reveals a coiled-coil-helix-coiled-coil-helix domain typical of redox-active proteins found in the mitochondrial inter-membrane space. COA6 structure analysis by NMR spectroscopy, overview
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C101A
site-directed mutagenesis, the mutation of the cysteine at position 101 to alanine results in a high-molecular-weight complex that is positive for MdbA and VKOR by immunoblotting and is absent in other alanine substitution mutants and the C93A/C101A double mutation and after treatment with the reducing agent 2-mercaptoethanol
H33G
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the mutant shows a loss of the capacity of the protein to isomerize, or shuffle, incorrect disulfides of scrambled RNase A yielding 10% active RNase A only
H32PY34R/Q35L/F36I/E37Y
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active variant
P31H/H32A/Y34G/Q35L/F36R/E37Y
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active variant
P31H/H32D/Y34S/Q35E/E37S
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active variant
P31H/H32T/Y34A/Q35S/F36T/E37R
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inactive variant
P31K/Y34P/Q35V/F36P/E37T
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inactive variant
P31R/H32G/Y34N/Q35K/F36L/E37A
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semi-active variant
P31R/H32I/Y34F/F36V/E37P
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inactive variant
P31R/H32S/Y34C/Q35T/F36Y/E37R
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semi-active variant
P31Y/H32E/Y34T/Q35A/F36D/E37H
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inactive variant
C57S
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site-directed mutagenesis, reduced activity
C57S/C60S
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site-directed mutagenesis, no activity
C60S
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site-directed mutagenesis, no activity
W59C/E87X
naturally occuring mutation in a human mitochondrial disease patient, mapping onto the COA6 structure. The truncation mutation (E87X) clearly disrupts the CHCH domain by removing a large portion of the protein from helix 2 onward. Mutation W59C is found within the first helix of COA6, where the side chain of the tryptophan faces the bulk solvent. The missense mutation disrupts COA6 function or expression. The patient with the W59C mutation exhibits a severe CcO deficiency in cardiac tissue
W66R
naturally occuring mutation in a human mitochondrial disease patient, mapping onto the COA6 structure. Mutation W66R is found within the first helix of COA6, where the side chain of the tryptophan faces the bulk solvent. The missense mutation disrupts COA6 function or expression
C29S
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specific activity about 5% of wild-type
C87S
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specific activity simiular to wild-type
C46A
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site-directed mutagenesis
C49A
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site-directed mutagenesis, SdbAC49A forms a mixed disulfide with SpeAC87A
C58S
complete loss of oxidoreductase activtiy
C95S
complete loss of oxidoreductase activtiy
C91A/C94A
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site-directed mutagenesis, catalytically inactive mutant
C91A/C94A
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site-directed mutagenesis, catalytically inactive mutant
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C89A
site-directed mutagenesis, the single-cysteine active site variant, SdbAC89A, forms a number of mixed disulfide complexes in the mutant
C89A
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site-directed mutagenesis, the single-cysteine active site variant, SdbAC89A, forms a number of mixed disulfide complexes in the mutant
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C89A
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site-directed mutagenesis, the single-cysteine active site variant, SdbAC89A, forms a number of mixed disulfide complexes in the mutant
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C89A
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site-directed mutagenesis, the single-cysteine active site variant, SdbAC89A, forms a number of mixed disulfide complexes in the mutant
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C89A
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site-directed mutagenesis, the single-cysteine active site variant, SdbAC89A, forms a number of mixed disulfide complexes in the mutant
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C89A
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site-directed mutagenesis, the single-cysteine active site variant, SdbAC89A, forms a number of mixed disulfide complexes in the mutant
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C89A
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site-directed mutagenesis, the single-cysteine active site variant, SdbAC89A, forms a number of mixed disulfide complexes in the mutant
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additional information
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heterologous expression of MdbACm in the Corynebacterium diphtheriae DELTAmdbA mutant rescues its known defects in cell growth and morphology, toxin production, and pilus assembly, and this thiol-disulfide oxidoreductase activity requires the catalytic motif CXXC. MdbA gene deletion in Corynebacterium matruchotii by gene replacement method. The Corynebacterium diphtheriae DELTAmdbA mutant is able to grow only at 30°C. This defect is rescued by expression of MdbACd. Expression of MdbACm in this mutant also rescues the growth defect. Generation of a MdbA gene deletion mutant of Corynebacterium matruchotii by gene replacement method
additional information
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heterologous expression of MdbACm in the Corynebacterium diphtheriae DELTAmdbA mutant rescues its known defects in cell growth and morphology, toxin production, and pilus assembly, and this thiol-disulfide oxidoreductase activity requires the catalytic motif CXXC. MdbA gene deletion in Corynebacterium matruchotii by gene replacement method. The Corynebacterium diphtheriae DELTAmdbA mutant is able to grow only at 30°C. This defect is rescued by expression of MdbACd. Expression of MdbACm in this mutant also rescues the growth defect. Generation of a MdbA gene deletion mutant of Corynebacterium matruchotii by gene replacement method
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additional information
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DsbA and DsbB insertion mutants are sensitive to dithiothreitol and benzylpenicillin or Cd2+, Hg2+ and Zn2+, pleitropic phenotype
additional information
introduction of the patient mutations (W59C/E87X and W66R) into a human-yeast chimera (hyCOA6) that consists of the bulk of the human protein and the N-terminal 24 amino acid residues of yeast Coa6 to facilitate mitochondrial targeting. The respiratory growth of the knockout mutant coa6DELTA cells is restored by the chimeric mutant hyCOA6, but not by either of the tryptophan variants, suggesting that these missense mutations disrupt COA6 function or expression. The hyCOA6W26C mutant is expressed and localizes to mitochondria, while hyCOA6W33R and the truncated protein hyCOA6E54X are undetectable. Overexpression of the wild-type and mutant alleles of COA6 in control and COA6 patient fibroblasts shows that the W66R variant fails to rescue CcO activity. In contrast, expression of the W59C mutant leads to a partial recovery of CcO activity and COX2 levels
additional information
generation of DsbA- mutants from strain MT1131, which form filamentous and osmosensitive cells at 35°C under Res growth conditions on enriched medium, where bioavailable Cu is limited. In contrast, these mutants grow normally at 25°C, but they produce very low levels of cbb3-Cox. Upon supplementation of the growth media with redox-active chemicals, they can grow normally and produce active cbb3-Cox. Overproduction of the Cu importer CcoA partially restores the cbb3-Cox defect, suggesting defective Cu incorporation into this enzyme in the absence of DsbA. Generation of DsbA- cbb3-Cox- and DsbA- bd-Qox- double mutants. Strain MD20 (1dsbA::kan) is used as a recipient, selecting for antibiotic resistance under growth permissive conditions. The double mutants thus obtained are tested for their temperature sensitive Res growth (ResTs) and Cu2+-suppressible phenotypes on MPYE at 35°C. Appropriate merodiploids are constructed by introducing the plasmids pDsbA, pSenC and pBK69 (CcoA) carrying wild-type alleles of dsbA, senC and ccoA, respectively into the DsbA- and DsbA- SenC-mutants using triparental crosses. Mutants lacking DsbA are able to grow via photosynthesis, albeit at a slower rate, on both enriched and minimal growth media, but can grow by aerobic respiration only on minimal, and not on enriched medium, at normal temperature (35°C). The DsbADELTA mutants revert readily on enriched medium at 35°C to regain Res growth ability. Proteomic analyses show that in the absence of DsbA the protease DegP is overproduced, and that the revertants contain mutations that lower DegP activity. DegP is usually less abundant and acts as a chaperone at lower temperatures. Phenotypes, overview
additional information
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generation of DsbA- mutants from strain MT1131, which form filamentous and osmosensitive cells at 35°C under Res growth conditions on enriched medium, where bioavailable Cu is limited. In contrast, these mutants grow normally at 25°C, but they produce very low levels of cbb3-Cox. Upon supplementation of the growth media with redox-active chemicals, they can grow normally and produce active cbb3-Cox. Overproduction of the Cu importer CcoA partially restores the cbb3-Cox defect, suggesting defective Cu incorporation into this enzyme in the absence of DsbA. Generation of DsbA- cbb3-Cox- and DsbA- bd-Qox- double mutants. Strain MD20 (1dsbA::kan) is used as a recipient, selecting for antibiotic resistance under growth permissive conditions. The double mutants thus obtained are tested for their temperature sensitive Res growth (ResTs) and Cu2+-suppressible phenotypes on MPYE at 35°C. Appropriate merodiploids are constructed by introducing the plasmids pDsbA, pSenC and pBK69 (CcoA) carrying wild-type alleles of dsbA, senC and ccoA, respectively into the DsbA- and DsbA- SenC-mutants using triparental crosses. Mutants lacking DsbA are able to grow via photosynthesis, albeit at a slower rate, on both enriched and minimal growth media, but can grow by aerobic respiration only on minimal, and not on enriched medium, at normal temperature (35°C). The DsbADELTA mutants revert readily on enriched medium at 35°C to regain Res growth ability. Proteomic analyses show that in the absence of DsbA the protease DegP is overproduced, and that the revertants contain mutations that lower DegP activity. DegP is usually less abundant and acts as a chaperone at lower temperatures. Phenotypes, overview
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additional information
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generation of DsbA- mutants from strain MT1131, which form filamentous and osmosensitive cells at 35°C under Res growth conditions on enriched medium, where bioavailable Cu is limited. In contrast, these mutants grow normally at 25°C, but they produce very low levels of cbb3-Cox. Upon supplementation of the growth media with redox-active chemicals, they can grow normally and produce active cbb3-Cox. Overproduction of the Cu importer CcoA partially restores the cbb3-Cox defect, suggesting defective Cu incorporation into this enzyme in the absence of DsbA. Generation of DsbA- cbb3-Cox- and DsbA- bd-Qox- double mutants. Strain MD20 (1dsbA::kan) is used as a recipient, selecting for antibiotic resistance under growth permissive conditions. The double mutants thus obtained are tested for their temperature sensitive Res growth (ResTs) and Cu2+-suppressible phenotypes on MPYE at 35°C. Appropriate merodiploids are constructed by introducing the plasmids pDsbA, pSenC and pBK69 (CcoA) carrying wild-type alleles of dsbA, senC and ccoA, respectively into the DsbA- and DsbA- SenC-mutants using triparental crosses. Mutants lacking DsbA are able to grow via photosynthesis, albeit at a slower rate, on both enriched and minimal growth media, but can grow by aerobic respiration only on minimal, and not on enriched medium, at normal temperature (35°C). The DsbADELTA mutants revert readily on enriched medium at 35°C to regain Res growth ability. Proteomic analyses show that in the absence of DsbA the protease DegP is overproduced, and that the revertants contain mutations that lower DegP activity. DegP is usually less abundant and acts as a chaperone at lower temperatures. Phenotypes, overview
-
additional information
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generation of DsbA- mutants from strain MT1131, which form filamentous and osmosensitive cells at 35°C under Res growth conditions on enriched medium, where bioavailable Cu is limited. In contrast, these mutants grow normally at 25°C, but they produce very low levels of cbb3-Cox. Upon supplementation of the growth media with redox-active chemicals, they can grow normally and produce active cbb3-Cox. Overproduction of the Cu importer CcoA partially restores the cbb3-Cox defect, suggesting defective Cu incorporation into this enzyme in the absence of DsbA. Generation of DsbA- cbb3-Cox- and DsbA- bd-Qox- double mutants. Strain MD20 (1dsbA::kan) is used as a recipient, selecting for antibiotic resistance under growth permissive conditions. The double mutants thus obtained are tested for their temperature sensitive Res growth (ResTs) and Cu2+-suppressible phenotypes on MPYE at 35°C. Appropriate merodiploids are constructed by introducing the plasmids pDsbA, pSenC and pBK69 (CcoA) carrying wild-type alleles of dsbA, senC and ccoA, respectively into the DsbA- and DsbA- SenC-mutants using triparental crosses. Mutants lacking DsbA are able to grow via photosynthesis, albeit at a slower rate, on both enriched and minimal growth media, but can grow by aerobic respiration only on minimal, and not on enriched medium, at normal temperature (35°C). The DsbADELTA mutants revert readily on enriched medium at 35°C to regain Res growth ability. Proteomic analyses show that in the absence of DsbA the protease DegP is overproduced, and that the revertants contain mutations that lower DegP activity. DegP is usually less abundant and acts as a chaperone at lower temperatures. Phenotypes, overview
-
additional information
gene sdbA mutants are defective in autolysis, extracellular DNA (eDNA) release, bacteriocin production, and genetic competence but form more biofilm. Inactivation of sdbA upregulates the CiaRH two-component regulatory system in Streptococcus gordonii, leading to the repression of the ComDE quorum sensing system, which results in the enhanced biofilm formation and the lack of bacteriocin production. The sdbB-ccdA2 mutant produces all of the phenotypes displayed by the sdbA mutant. The sdbB-sgo_1177 mutant is defective in eDNA release and bacteriocin production but not autolysis or genetic competence. The sdbB-ccdA1 mutant is defective in autolysis but not eDNA release, bacteriocin production, or genetic competence. The sgo_1177-ccdA2 mutant is partially defective in autolysis but not in other phenotypes. The ccdA1-ccdA2 mutant is defective only in bacteriocin production. The phenotypes exhibited by the sdbB-ccdA2 mutant are reversed when functional copies of sdbB and ccdA2 are knocked back into the same location on the chromosome. Quantitative realtime PCR analysis of the sdbB-ccdA2 mutant shows that the genes immediately upstream (sgo_1174) and downstream (sgo_1170) of the mutated genes are transcribed, indicating that the mutation does not affect the expression of adjacent genes. The levels of sgo_1174 and sgo_1170 expression are similar between the parent, sdbBccdA2 mutant, and sdbB-ccdA2 knockin mutant
additional information
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gene sdbA mutants are defective in autolysis, extracellular DNA (eDNA) release, bacteriocin production, and genetic competence but form more biofilm. Inactivation of sdbA upregulates the CiaRH two-component regulatory system in Streptococcus gordonii, leading to the repression of the ComDE quorum sensing system, which results in the enhanced biofilm formation and the lack of bacteriocin production. The sdbB-ccdA2 mutant produces all of the phenotypes displayed by the sdbA mutant. The sdbB-sgo_1177 mutant is defective in eDNA release and bacteriocin production but not autolysis or genetic competence. The sdbB-ccdA1 mutant is defective in autolysis but not eDNA release, bacteriocin production, or genetic competence. The sgo_1177-ccdA2 mutant is partially defective in autolysis but not in other phenotypes. The ccdA1-ccdA2 mutant is defective only in bacteriocin production. The phenotypes exhibited by the sdbB-ccdA2 mutant are reversed when functional copies of sdbB and ccdA2 are knocked back into the same location on the chromosome. Quantitative realtime PCR analysis of the sdbB-ccdA2 mutant shows that the genes immediately upstream (sgo_1174) and downstream (sgo_1170) of the mutated genes are transcribed, indicating that the mutation does not affect the expression of adjacent genes. The levels of sgo_1174 and sgo_1170 expression are similar between the parent, sdbBccdA2 mutant, and sdbB-ccdA2 knockin mutant
-
additional information
-
gene sdbA mutants are defective in autolysis, extracellular DNA (eDNA) release, bacteriocin production, and genetic competence but form more biofilm. Inactivation of sdbA upregulates the CiaRH two-component regulatory system in Streptococcus gordonii, leading to the repression of the ComDE quorum sensing system, which results in the enhanced biofilm formation and the lack of bacteriocin production. The sdbB-ccdA2 mutant produces all of the phenotypes displayed by the sdbA mutant. The sdbB-sgo_1177 mutant is defective in eDNA release and bacteriocin production but not autolysis or genetic competence. The sdbB-ccdA1 mutant is defective in autolysis but not eDNA release, bacteriocin production, or genetic competence. The sgo_1177-ccdA2 mutant is partially defective in autolysis but not in other phenotypes. The ccdA1-ccdA2 mutant is defective only in bacteriocin production. The phenotypes exhibited by the sdbB-ccdA2 mutant are reversed when functional copies of sdbB and ccdA2 are knocked back into the same location on the chromosome. Quantitative realtime PCR analysis of the sdbB-ccdA2 mutant shows that the genes immediately upstream (sgo_1174) and downstream (sgo_1170) of the mutated genes are transcribed, indicating that the mutation does not affect the expression of adjacent genes. The levels of sgo_1174 and sgo_1170 expression are similar between the parent, sdbBccdA2 mutant, and sdbB-ccdA2 knockin mutant
-
additional information
-
gene sdbA mutants are defective in autolysis, extracellular DNA (eDNA) release, bacteriocin production, and genetic competence but form more biofilm. Inactivation of sdbA upregulates the CiaRH two-component regulatory system in Streptococcus gordonii, leading to the repression of the ComDE quorum sensing system, which results in the enhanced biofilm formation and the lack of bacteriocin production. The sdbB-ccdA2 mutant produces all of the phenotypes displayed by the sdbA mutant. The sdbB-sgo_1177 mutant is defective in eDNA release and bacteriocin production but not autolysis or genetic competence. The sdbB-ccdA1 mutant is defective in autolysis but not eDNA release, bacteriocin production, or genetic competence. The sgo_1177-ccdA2 mutant is partially defective in autolysis but not in other phenotypes. The ccdA1-ccdA2 mutant is defective only in bacteriocin production. The phenotypes exhibited by the sdbB-ccdA2 mutant are reversed when functional copies of sdbB and ccdA2 are knocked back into the same location on the chromosome. Quantitative realtime PCR analysis of the sdbB-ccdA2 mutant shows that the genes immediately upstream (sgo_1174) and downstream (sgo_1170) of the mutated genes are transcribed, indicating that the mutation does not affect the expression of adjacent genes. The levels of sgo_1174 and sgo_1170 expression are similar between the parent, sdbBccdA2 mutant, and sdbB-ccdA2 knockin mutant
-
additional information
-
gene sdbA mutants are defective in autolysis, extracellular DNA (eDNA) release, bacteriocin production, and genetic competence but form more biofilm. Inactivation of sdbA upregulates the CiaRH two-component regulatory system in Streptococcus gordonii, leading to the repression of the ComDE quorum sensing system, which results in the enhanced biofilm formation and the lack of bacteriocin production. The sdbB-ccdA2 mutant produces all of the phenotypes displayed by the sdbA mutant. The sdbB-sgo_1177 mutant is defective in eDNA release and bacteriocin production but not autolysis or genetic competence. The sdbB-ccdA1 mutant is defective in autolysis but not eDNA release, bacteriocin production, or genetic competence. The sgo_1177-ccdA2 mutant is partially defective in autolysis but not in other phenotypes. The ccdA1-ccdA2 mutant is defective only in bacteriocin production. The phenotypes exhibited by the sdbB-ccdA2 mutant are reversed when functional copies of sdbB and ccdA2 are knocked back into the same location on the chromosome. Quantitative realtime PCR analysis of the sdbB-ccdA2 mutant shows that the genes immediately upstream (sgo_1174) and downstream (sgo_1170) of the mutated genes are transcribed, indicating that the mutation does not affect the expression of adjacent genes. The levels of sgo_1174 and sgo_1170 expression are similar between the parent, sdbBccdA2 mutant, and sdbB-ccdA2 knockin mutant
-
additional information
-
gene sdbA mutants are defective in autolysis, extracellular DNA (eDNA) release, bacteriocin production, and genetic competence but form more biofilm. Inactivation of sdbA upregulates the CiaRH two-component regulatory system in Streptococcus gordonii, leading to the repression of the ComDE quorum sensing system, which results in the enhanced biofilm formation and the lack of bacteriocin production. The sdbB-ccdA2 mutant produces all of the phenotypes displayed by the sdbA mutant. The sdbB-sgo_1177 mutant is defective in eDNA release and bacteriocin production but not autolysis or genetic competence. The sdbB-ccdA1 mutant is defective in autolysis but not eDNA release, bacteriocin production, or genetic competence. The sgo_1177-ccdA2 mutant is partially defective in autolysis but not in other phenotypes. The ccdA1-ccdA2 mutant is defective only in bacteriocin production. The phenotypes exhibited by the sdbB-ccdA2 mutant are reversed when functional copies of sdbB and ccdA2 are knocked back into the same location on the chromosome. Quantitative realtime PCR analysis of the sdbB-ccdA2 mutant shows that the genes immediately upstream (sgo_1174) and downstream (sgo_1170) of the mutated genes are transcribed, indicating that the mutation does not affect the expression of adjacent genes. The levels of sgo_1174 and sgo_1170 expression are similar between the parent, sdbBccdA2 mutant, and sdbB-ccdA2 knockin mutant
-
additional information
-
gene sdbA mutants are defective in autolysis, extracellular DNA (eDNA) release, bacteriocin production, and genetic competence but form more biofilm. Inactivation of sdbA upregulates the CiaRH two-component regulatory system in Streptococcus gordonii, leading to the repression of the ComDE quorum sensing system, which results in the enhanced biofilm formation and the lack of bacteriocin production. The sdbB-ccdA2 mutant produces all of the phenotypes displayed by the sdbA mutant. The sdbB-sgo_1177 mutant is defective in eDNA release and bacteriocin production but not autolysis or genetic competence. The sdbB-ccdA1 mutant is defective in autolysis but not eDNA release, bacteriocin production, or genetic competence. The sgo_1177-ccdA2 mutant is partially defective in autolysis but not in other phenotypes. The ccdA1-ccdA2 mutant is defective only in bacteriocin production. The phenotypes exhibited by the sdbB-ccdA2 mutant are reversed when functional copies of sdbB and ccdA2 are knocked back into the same location on the chromosome. Quantitative realtime PCR analysis of the sdbB-ccdA2 mutant shows that the genes immediately upstream (sgo_1174) and downstream (sgo_1170) of the mutated genes are transcribed, indicating that the mutation does not affect the expression of adjacent genes. The levels of sgo_1174 and sgo_1170 expression are similar between the parent, sdbBccdA2 mutant, and sdbB-ccdA2 knockin mutant
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additional information
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generation of a sdbA-knockout mutant by insertional inactivation using pG1host5 carrying an internal portion of the gene. SpeA in the culture supernatant remains reduced when gene sdbA is inactivated and restored to the oxidized state when a functional copy of sdbA is returned to the sdbA-knockout mutant. Complementation of sdbA deletion restores SpeA to an oxidized state
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Hillson, D.A.; Freedman, R.B.
Resolution of protein disulphide-isomerase and glutathione-insulin transhydrogenase activities by covalent chromatography
Biochem. J.
191
373-388
1980
Bos taurus
brenda
Hawkins, H.C.; Freedman, R.B.
Thiol-protein disulphide oxidoreductases. Differences between protein disulphide-isomerase and glutathione-insulin transhydrogenase activities in ox liver
Biochem. J.
159
385-393
1976
Bos taurus
brenda
Ibbetson, A.L.; Freedman, R.B.
Thiol-protein disulphide oxidoreductases. Assay of microsomal membrane-bound glutathione-insulin transhydrogenase and comparison with protein disulphide-isomerase
Biochem. J.
159
377-384
1976
Rattus norvegicus
brenda
Varandani, P.T.
Glutathione-insulin transhydrogenase (protein-disulfide interchange enzyme)
Coenzymes and cofactors, Glutathione, Chem. Biochem. Med. Aspects Pt. A (Dolphin D, Poulson R, Avromonic O, eds. ) John Wiley & Sons, New York
3
753-765
1989
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
-
brenda
Varandani, P.T.
Mechanistic and structural aspects of glutathione-insulin transhydogenase (protein-disulfide interchange enzyme)
Dev. Biochem.
1
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