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Literature summary for 3.5.1.115 extracted from
- Functional characterization of Corynebacterium glutamicum mycothiol S-conjugate amidase (2014), PLoS ONE, 9, e115075.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene mca or NCgl0948, quantitative real-time PCR enzyme expression analysis, recombinant wild-type and mutant enzyme expression in Escherichia coli strain BL21(DE3) | Corynebacterium glutamicum |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D132A | site-directed mutagenesis, the mutant shows slightly decreased activity compared to the wild-type enzyme | Corynebacterium glutamicum |
| D141A | site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme | Corynebacterium glutamicum |
| D14A | site-directed mutagenesis, the mutant shows slightly decreased activity compared to the wild-type enzyme | Corynebacterium glutamicum |
| D15A | site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme | Corynebacterium glutamicum |
| E16A | site-directed mutagenesis, the mutant shows slightly decreased activity compared to the wild-type enzyme | Corynebacterium glutamicum |
| E43A | site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme | Corynebacterium glutamicum |
| H10A | site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme | Corynebacterium glutamicum |
| H12A | site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme | Corynebacterium glutamicum |
| H139A | site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme | Corynebacterium glutamicum |
| H142A | site-directed mutagenesis, the mutant shows slightly decreased activity compared to the wild-type enzyme | Corynebacterium glutamicum |
| additional information | construction of a mca deletion mutant | Corynebacterium glutamicum |
| Y137A | site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme | Corynebacterium glutamicum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Cd2+ | - |
Corynebacterium glutamicum |  |
| Cr2+ | - |
Corynebacterium glutamicum | |
| Cu2+ | - |
Corynebacterium glutamicum | |
| additional information | heavy metal ions, including Cd2+, Ni2+, Cr2+ and Cu2+, markedly inhibit growth of the mca mutant relative to the wild type strain | Corynebacterium glutamicum | |
| Ni2+ | - |
Corynebacterium glutamicum | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics of wild-type and mutant enzymes with substrate N-acetyl-D-glucosamine, overview | Corynebacterium glutamicum | |
| 92.34 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant wild-type enzyme | Corynebacterium glutamicum | |
| 93.37 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant E43A | Corynebacterium glutamicum | |
| 99.92 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant D132A | Corynebacterium glutamicum | |
| 107.5 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant E16A | Corynebacterium glutamicum | |
| 108.4 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant H10A | Corynebacterium glutamicum | |
| 111.6 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant H12A | Corynebacterium glutamicum | |
| 115.3 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant H142A | Corynebacterium glutamicum | |
| 128.8 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant D15A | Corynebacterium glutamicum | |
| 132.3 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant D14A | Corynebacterium glutamicum | |
| 138 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant D141A | Corynebacterium glutamicum | |
| 469.6 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant H139A | Corynebacterium glutamicum | |
| 542.4 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant Y137A | Corynebacterium glutamicum | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | metal ion requirement, activates | Corynebacterium glutamicum | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 35000 | - |
recombinant enzyme, gel filtration | Corynebacterium glutamicum |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Corynebacterium glutamicum | the wild-type enzyme is active on a mycothiol S-conjugate of monobromobimane (MSmB) in vivo | ? | - |
? | |
| additional information | Corynebacterium glutamicum DSM 20300 | the wild-type enzyme is active on a mycothiol S-conjugate of monobromobimane (MSmB) in vivo | ? | - |
? | |
| mycothiol bimane + H2O | Corynebacterium glutamicum | - |
mycothiol + bimane | - |
? | |
| mycothiol bimane + H2O | Corynebacterium glutamicum DSM 20300 | - |
mycothiol + bimane | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Corynebacterium glutamicum | Q8NRQ7 | RES167, gene mca or NCgl0948 | - |
| Corynebacterium glutamicum DSM 20300 | Q8NRQ7 | RES167, gene mca or NCgl0948 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) to homogeneity | Corynebacterium glutamicum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the wild-type enzyme is active on a mycothiol S-conjugate of monobromobimane (MSmB) in vivo | Corynebacterium glutamicum | ? | - |
? | |
| additional information | substrate specificity, overview. The enzyme also deacetylates N-acetyl-D-glucosamine | Corynebacterium glutamicum | ? | - |
? | |
| additional information | the wild-type enzyme is active on a mycothiol S-conjugate of monobromobimane (MSmB) in vivo | Corynebacterium glutamicum DSM 20300 | ? | - |
? | |
| additional information | substrate specificity, overview. The enzyme also deacetylates N-acetyl-D-glucosamine | Corynebacterium glutamicum DSM 20300 | ? | - |
? | |
| mycothiol bimane + H2O | - |
Corynebacterium glutamicum | mycothiol + bimane | - |
? | |
| mycothiol bimane + H2O | - |
Corynebacterium glutamicum DSM 20300 | mycothiol + bimane | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 35000, recombinant enzyme, SDS-PAGE | Corynebacterium glutamicum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MCA | - |
Corynebacterium glutamicum |
| mycothiol S-conjugate amidase | - |
Corynebacterium glutamicum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Corynebacterium glutamicum |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0048 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant H139A | Corynebacterium glutamicum | |
| 0.005 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant Y137A | Corynebacterium glutamicum | |
| 0.036 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant D14A | Corynebacterium glutamicum | |
| 0.046 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant D141A | Corynebacterium glutamicum | |
| 0.058 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant E43A | Corynebacterium glutamicum | |
| 0.059 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant wild-type enzyme | Corynebacterium glutamicum | |
| 0.065 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant D132A | Corynebacterium glutamicum | |
| 0.0655 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant H142A | Corynebacterium glutamicum | |
| 0.066 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant H12A | Corynebacterium glutamicum | |
| 0.068 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant H10A | Corynebacterium glutamicum | |
| 0.069 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant E16A | Corynebacterium glutamicum | |
| 0.078 | - |
mycothiol bimane | pH 7.5, 30°C, recombinant mutant D15A | Corynebacterium glutamicum | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | 8.5 | recombinant enzyme | Corynebacterium glutamicum |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Corynebacterium glutamicum | induced expression of Mca in Corynebacterium glutamicum under various stress conditions, directly under the control of the stress-responsive extracytoplasmic function-sigma (ECF-s) factor SigH, positive regulation of mca expression by SigH | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | some Gram-positive bacteria, such as members of Corynebacterium, Mycobacterium, Rhodococcus and Streptomyces, cannot produce GSH but instead synthesize its functional equivalent, mycothiol | Corynebacterium glutamicum |
| malfunction | mutants lacking the enzyme and mycothiol are more susceptible to alkylating agents and oxidants, e.g. monobromobimane, iodoacetamide, N-ethylmaleimide, 1-chloro-2,4-dinitrobenzene, and methyllglyoxal, or to some macrolides and beta-lactams, e.g. rifamycin S, than the wild-type enzyme. Heavy metal ions, including Cd2+, Ni2+, Cr2+ and Cu2+, markedly inhibit growth of the mca mutant relative to the wild type strain | Corynebacterium glutamicum |
| additional information | residues Asp14, Tyr137, His139 and Asp141 are important for enzyme activity | Corynebacterium glutamicum |
| physiological function | mycothiol S-conjugate amidase is a key enzyme involved in MSH-dependent detoxification. In detoxification process, mycothiol directly reacts with electrophilic compounds by its thiol moiety, forming MSH S-conjugates, regulation mechanism, potential roles of the enzyme in resistance to alkylating agents and oxidants and in the survival of Corynebacterium glutamicum by coping with multiple stresses and detoxifying toxins, overview | Corynebacterium glutamicum |
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