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Literature summary extracted from
- A novel mycothiol-dependent thiol-disulfide reductase in Corynebacterium glutamicum involving oxidative stress resistance (2021), 3 Biotech, 11, 372 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.8.4.15 | gene ncgl2478, quantitative real-time PCR analysis, sequence comparisons, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Corynebacterium glutamicum |
| 5.3.4.1 | gene ncgl2478, quantitative real?time PCR analysis, sequence comparisons, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Corynebacterium glutamicum |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.8.4.15 | C21S | site-directed mutagenesis, almost inactive mutant | Corynebacterium glutamicum |
| 1.8.4.15 | C24S | site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate | Corynebacterium glutamicum |
| 1.8.4.15 | additional information | ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress | Corynebacterium glutamicum |
| 5.3.4.1 | C21S | site-directed mutagenesis, almost inactive mutant | Corynebacterium glutamicum |
| 5.3.4.1 | C24S | site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate | Corynebacterium glutamicum |
| 5.3.4.1 | additional information | ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress | Corynebacterium glutamicum |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.8.4.15 | 2,4-dinitrochlorobenzene | - |
Corynebacterium glutamicum |  |
| 1.8.4.15 | cumene hydroperoxide | - |
Corynebacterium glutamicum | |
| 1.8.4.15 | hydrogen peroxide | - |
Corynebacterium glutamicum | |
| 1.8.4.15 | iodoacetamide | - |
Corynebacterium glutamicum | |
| 1.8.4.15 | sodium hypochlorite | - |
Corynebacterium glutamicum | |
| 5.3.4.1 | 2,4-dinitrochlorobenzene | - |
Corynebacterium glutamicum | |
| 5.3.4.1 | cumene hydroperoxide | - |
Corynebacterium glutamicum | |
| 5.3.4.1 | hydrogen peroxide | - |
Corynebacterium glutamicum | |
| 5.3.4.1 | iodoacetamide | - |
Corynebacterium glutamicum | |
| 5.3.4.1 | sodium hypochlorite | - |
Corynebacterium glutamicum | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.3.4.1 | 0.46 | - |
HED-SSM | recombinant mutant C24S, pH 7.6, 30°C | Corynebacterium glutamicum | |
| 5.3.4.1 | 0.51 | - |
HED-SSM | recombinant wild-type enzyme, pH 7.6, 30°C | Corynebacterium glutamicum | |
| 5.3.4.1 | 33.69 | - |
HED-SSM | recombinant mutant C21S, pH 7.6, 30°C | Corynebacterium glutamicum |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.1.15 | mycothione + NADPH + H+ | Corynebacterium glutamicum | - |
2 mycothiol + NADP+ | - |
? | |
| 5.3.4.1 | HED-SSM | Corynebacterium glutamicum | a mixed disulfide | MSH + HED | - |
? | |
| 5.3.4.1 | HED-SSM | Corynebacterium glutamicum LMG 3730 | a mixed disulfide | MSH + HED | - |
? | |
| 5.3.4.1 | HED-SSM | Corynebacterium glutamicum BCRC 11384 | a mixed disulfide | MSH + HED | - |
? | |
| 5.3.4.1 | HED-SSM | Corynebacterium glutamicum ATCC 13032 | a mixed disulfide | MSH + HED | - |
? | |
| 5.3.4.1 | HED-SSM | Corynebacterium glutamicum JCM 1318 | a mixed disulfide | MSH + HED | - |
? | |
| 5.3.4.1 | HED-SSM | Corynebacterium glutamicum NCIMB 10025 | a mixed disulfide | MSH + HED | - |
? | |
| 5.3.4.1 | HED-SSM | Corynebacterium glutamicum DSM 20300 | a mixed disulfide | MSH + HED | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.8.1.15 | Corynebacterium glutamicum | - |
- |
- |
| 1.8.4.15 | Corynebacterium glutamicum | Q8NMK6 | - |
- |
| 1.8.4.15 | Corynebacterium glutamicum ATCC 13032 | Q8NMK6 | - |
- |
| 1.8.4.15 | Corynebacterium glutamicum BCRC 11384 | Q8NMK6 | - |
- |
| 1.8.4.15 | Corynebacterium glutamicum DSM 20300 | Q8NMK6 | - |
- |
| 1.8.4.15 | Corynebacterium glutamicum JCM 1318 | Q8NMK6 | - |
- |
| 1.8.4.15 | Corynebacterium glutamicum LMG 3730 | Q8NMK6 | - |
- |
| 1.8.4.15 | Corynebacterium glutamicum NCIMB 10025 | Q8NMK6 | - |
- |
| 5.3.4.1 | Corynebacterium glutamicum | Q8NMK6 | - |
- |
| 5.3.4.1 | Corynebacterium glutamicum ATCC 13032 | Q8NMK6 | - |
- |
| 5.3.4.1 | Corynebacterium glutamicum BCRC 11384 | Q8NMK6 | - |
- |
| 5.3.4.1 | Corynebacterium glutamicum DSM 20300 | Q8NMK6 | - |
- |
| 5.3.4.1 | Corynebacterium glutamicum JCM 1318 | Q8NMK6 | - |
- |
| 5.3.4.1 | Corynebacterium glutamicum LMG 3730 | Q8NMK6 | - |
- |
| 5.3.4.1 | Corynebacterium glutamicum NCIMB 10025 | Q8NMK6 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.8.4.15 | recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Corynebacterium glutamicum |
| 5.3.4.1 | recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Corynebacterium glutamicum |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.8.4.15 | a [DsbA protein] carrying a disulfide bond + a [protein] with reduced L-cysteine residues = a [DsbA protein] with reduced L-cysteine residues + a [protein] carrying a disulfide bond | NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity | Corynebacterium glutamicum | |
| 5.3.4.1 | catalyses the rearrangement of -S-S- bonds in proteins | NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity | Corynebacterium glutamicum |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.1.15 | mycothione + NADPH + H+ | - |
Corynebacterium glutamicum | 2 mycothiol + NADP+ | - |
? | |
| 1.8.4.15 | additional information | NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurring via a dithiol mechanism | Corynebacterium glutamicum | ? | - |
- |
|
| 1.8.4.15 | additional information | NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurring via a dithiol mechanism | Corynebacterium glutamicum LMG 3730 | ? | - |
- |
|
| 1.8.4.15 | additional information | NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurring via a dithiol mechanism | Corynebacterium glutamicum BCRC 11384 | ? | - |
- |
|
| 1.8.4.15 | additional information | NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurring via a dithiol mechanism | Corynebacterium glutamicum ATCC 13032 | ? | - |
- |
|
| 1.8.4.15 | additional information | NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurring via a dithiol mechanism | Corynebacterium glutamicum JCM 1318 | ? | - |
- |
|
| 1.8.4.15 | additional information | NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurring via a dithiol mechanism | Corynebacterium glutamicum NCIMB 10025 | ? | - |
- |
|
| 1.8.4.15 | additional information | NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurring via a dithiol mechanism | Corynebacterium glutamicum DSM 20300 | ? | - |
- |
|
| 5.3.4.1 | HED-SSM | a mixed disulfide | Corynebacterium glutamicum | MSH + HED | - |
? | |
| 5.3.4.1 | HED-SSM | a mixed disulfide | Corynebacterium glutamicum LMG 3730 | MSH + HED | - |
? | |
| 5.3.4.1 | HED-SSM | a mixed disulfide | Corynebacterium glutamicum BCRC 11384 | MSH + HED | - |
? | |
| 5.3.4.1 | HED-SSM | a mixed disulfide | Corynebacterium glutamicum ATCC 13032 | MSH + HED | - |
? | |
| 5.3.4.1 | HED-SSM | a mixed disulfide | Corynebacterium glutamicum JCM 1318 | MSH + HED | - |
? | |
| 5.3.4.1 | HED-SSM | a mixed disulfide | Corynebacterium glutamicum NCIMB 10025 | MSH + HED | - |
? | |
| 5.3.4.1 | HED-SSM | a mixed disulfide | Corynebacterium glutamicum DSM 20300 | MSH + HED | - |
? | |
| 5.3.4.1 | additional information | NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism | Corynebacterium glutamicum | ? | - |
- |
|
| 5.3.4.1 | additional information | NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism | Corynebacterium glutamicum LMG 3730 | ? | - |
- |
|
| 5.3.4.1 | additional information | NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism | Corynebacterium glutamicum BCRC 11384 | ? | - |
- |
|
| 5.3.4.1 | additional information | NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism | Corynebacterium glutamicum ATCC 13032 | ? | - |
- |
|
| 5.3.4.1 | additional information | NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism | Corynebacterium glutamicum JCM 1318 | ? | - |
- |
|
| 5.3.4.1 | additional information | NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism | Corynebacterium glutamicum NCIMB 10025 | ? | - |
- |
|
| 5.3.4.1 | additional information | NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism | Corynebacterium glutamicum DSM 20300 | ? | - |
- |
|
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.8.4.15 | More | formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress | Corynebacterium glutamicum |
| 5.3.4.1 | More | formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress | Corynebacterium glutamicum |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.8.1.15 | MTR | - |
Corynebacterium glutamicum |
| 1.8.4.15 | More | see also EC 5.3.4.1 and EC 1.8.1.15 | Corynebacterium glutamicum |
| 1.8.4.15 | MSH-dependent thiol-disulfide reductase | - |
Corynebacterium glutamicum |
| 1.8.4.15 | mycothiol-dependent thiol-disulfide reductase | - |
Corynebacterium glutamicum |
| 1.8.4.15 | ncgl2478 | - |
Corynebacterium glutamicum |
| 1.8.4.15 | thiol-disulfide oxidoreductase | - |
Corynebacterium glutamicum |
| 5.3.4.1 | dithiol-disulfide isomerase | - |
Corynebacterium glutamicum |
| 5.3.4.1 | More | see also EC 1.8.4.2 | Corynebacterium glutamicum |
| 5.3.4.1 | ncgl2478 | - |
Corynebacterium glutamicum |
| 5.3.4.1 | thiol-disulfide oxidoreductase | - |
Corynebacterium glutamicum |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.8.4.15 | 30 | - |
assay at | Corynebacterium glutamicum |
| 5.3.4.1 | 30 | - |
assay at | Corynebacterium glutamicum |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.3.4.1 | 0.0009 | - |
HED-SSM | recombinant mutant C21S, pH 7.6, 30°C | Corynebacterium glutamicum | |
| 5.3.4.1 | 8.55 | - |
HED-SSM | recombinant wild-type enzyme, pH 7.6, 30°C | Corynebacterium glutamicum | |
| 5.3.4.1 | 11.37 | - |
HED-SSM | recombinant mutant C24S, pH 7.6, 30°C | Corynebacterium glutamicum |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.8.4.15 | 7.6 | - |
assay at | Corynebacterium glutamicum |
| 5.3.4.1 | 7.6 | - |
assay at | Corynebacterium glutamicum |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.8.1.15 | NADPH | dependent on | Corynebacterium glutamicum | |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 1.8.4.15 | Corynebacterium glutamicum | ncgl2478 expression is induced in the stress-responsive extra-cytoplasmic function-sigma (ECF-sigma) factor SigH-dependent manner by stress. SigH positively regulates NCgl2478 expression in Corynebacterium glutamicum. SigH directly activates the expression of ncgl2478 by specifically recognizing an operator within the ncgl2478 promoter region | up |
| 5.3.4.1 | Corynebacterium glutamicum | ncgl2478 expression is induced in the stress-responsive extra-cytoplasmic function-sigma (ECF-sigma) factor SigH-dependent manner by stress. SigH positively regulates NCgl2478 expression in Corynebacterium glutamicum. SigH directly activates the expression of ncgl2478 by specifically recognizing an operator within the ncgl2478 promoter region | up |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.8.4.15 | malfunction | deletion of the ncgl2478 gene increases the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress | Corynebacterium glutamicum |
| 1.8.4.15 | metabolism | the enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway, see EC 5.3.4.1 and EC 1.8.1.15 | Corynebacterium glutamicum |
| 1.8.4.15 | additional information | the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1, EC 1.20.4.3) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress | Corynebacterium glutamicum |
| 1.8.4.15 | physiological function | enzyme NCgl2478 plays an important role in stress resistance. The enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr, EC 1.8.1.15)/NADPH pathway. NCgl2478 protects against various stresses by acting as an MSH-dependent thiol-disulfide reductase, belonging to a DsbA-Mrx1 cluster | Corynebacterium glutamicum |
| 5.3.4.1 | malfunction | deletion of the ncgl2478 gene increases the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress | Corynebacterium glutamicum |
| 5.3.4.1 | metabolism | the enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway | Corynebacterium glutamicum |
| 5.3.4.1 | additional information | the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress | Corynebacterium glutamicum |
| 5.3.4.1 | physiological function | enzyme NCgl2478 plays an important role in stress resistance. The enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway. NCgl2478 protects against various stresses by acting as an MSH-dependent thiol-disulfide reductase, belonging to a DsbA-Mrx1 cluster | Corynebacterium glutamicum |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.3.4.1 | 0.000027 | - |
HED-SSM | recombinant mutant C21S, pH 7.6, 30°C | Corynebacterium glutamicum | |
| 5.3.4.1 | 16.77 | - |
HED-SSM | recombinant wild-type enzyme, pH 7.6, 30°C | Corynebacterium glutamicum | |
| 5.3.4.1 | 24.72 | - |
HED-SSM | recombinant mutant C24S, pH 7.6, 30°C | Corynebacterium glutamicum |
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