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Literature summary for 4.2.1.84 extracted from
- The alpha subunit of nitrile hydratase is sufficient for catalytic activity and post-translational modification (2014), Biochemistry, 53, 3990-3994.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| genes toyJKL and toyJ, recombinant expression of N-terminally His6-tagged trimeric and monomeric subunits in Escherichia coli | Streptomyces rimosus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | comparisons of the steady state kinetic parameters of the single subunit variant to the heterotrimeric protein show that the additional subunits impart substrate specificity and catalytic efficiency | Streptomyces rimosus | |
| 0.028 | - |
Toyocamycin | pH 65, temperature not specified in the publication, recombinant trimeric enzyme | Streptomyces rimosus |  |
| 15 | - |
Toyocamycin | pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme | Streptomyces rimosus | |
| 99 | - |
3-Cyanopyridine | pH 65, temperature not specified in the publication, recombinant trimeric enzyme | Streptomyces rimosus | |
| 1100 | - |
3-Cyanopyridine | pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme | Streptomyces rimosus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | the metal cofactor is located in the alpha-subunit at the interfacial active site of the heterodimeric enzyme | Streptomyces rimosus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| toyocamycin + H2O | Streptomyces rimosus | - |
toyocamycin acid amide | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces rimosus | B6CWJ3 | gene toyJ; genes toyJ, toyK, and toyL encoding the three subunits of the enzyme | - |
| Streptomyces rimosus | B6CWJ4 | gene toyK; genes toyJ, toyK, and toyL encoding the three subunits of the enzyme | - |
| Streptomyces rimosus | B6CWJ5 | gene toyL; genes toyJ, toyK, and toyL encoding the three subunits of the enzyme | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-cyanopyridine + H2O | a niacin precursor | Streptomyces rimosus | pyridine-3-carbamide | - |
? | |
| additional information | substrate specificity of trimeric enzyme compared to the isolated alpha-subunit, overview. Activity of the alpha-subunit of a nitrile hydratase distinguishes among possible mechanisms of nitrile hydration by adding significant weight to those that rely solely on residues derived from the alpha-subunit. No activity with thiocyanate | Streptomyces rimosus | ? | - |
? | |
| toyocamycin + H2O | - |
Streptomyces rimosus | toyocamycin acid amide | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterotrimer | comparisons of the steady state kinetic parameters of the single subunit variant to the heterotrimeric protein show that the additional subunits impart substrate specificity and catalytic efficiency. The alpha-subunit is the minimal sequence needed for nitrile hydration providing a simplified scaffold to study the mechanism and posttranslational modification of this important class of catalysts | Streptomyces rimosus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| NHase | - |
Streptomyces rimosus |
| TNHase | - |
Streptomyces rimosus |
| toyocamycin nitrile hydratase | - |
Streptomyces rimosus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.44 | - |
Toyocamycin | pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme | Streptomyces rimosus | |
| 35 | - |
3-Cyanopyridine | pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme | Streptomyces rimosus | |
| 79 | - |
3-Cyanopyridine | pH 65, temperature not specified in the publication, recombinant trimeric enzyme | Streptomyces rimosus | |
| 159 | - |
Toyocamycin | pH 65, temperature not specified in the publication, recombinant trimeric enzyme | Streptomyces rimosus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | - |
assay at | Streptomyces rimosus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | toyocamycin nitrile hydratase is a unique three-subunit member of the nitrile hydratase family | Streptomyces rimosus |
| additional information | the alpha-subunit is the minimal sequence needed for nitrile hydration providing a simplified scaffold to study the mechanism and posttranslational modification of this important class of catalysts | Streptomyces rimosus |
| physiological function | toyocamycin nitrile hydratase is involved in the biosynthesis of pyrrolopyrimidine antibiotics | Streptomyces rimosus |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.03 | - |
Toyocamycin | pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme | Streptomyces rimosus | |
| 0.032 | - |
3-Cyanopyridine | pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme | Streptomyces rimosus | |
| 0.8 | - |
3-Cyanopyridine | pH 65, temperature not specified in the publication, recombinant trimeric enzyme | Streptomyces rimosus | |
| 5700 | - |
Toyocamycin | pH 65, temperature not specified in the publication, recombinant trimeric enzyme | Streptomyces rimosus | |
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