EC Number | Cloned (Comment) | Organism |
---|---|---|
2.1.1.315 | expression in Escherichia coli as a polyhistidine-tagged polypeptide | Amycolatopsis mediterranei |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.1.1.315 | Ca2+ | inhibits slightly | Amycolatopsis mediterranei | |
2.1.1.315 | Co2+ | strong inhibition | Amycolatopsis mediterranei | |
2.1.1.315 | Mg2+ | inhibits slightly | Amycolatopsis mediterranei | |
2.1.1.315 | Ni2+ | strong inhibition | Amycolatopsis mediterranei | |
2.1.1.315 | Zn2+ | strong inhibition | Amycolatopsis mediterranei |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.1.1.315 | 0.018 | - |
27-O-demethylrifamycin SV | pH 8.0, 30°C | Amycolatopsis mediterranei | |
2.1.1.315 | 0.0193 | - |
S-adenosyl-L-methionine | pH 8.0, 30°C | Amycolatopsis mediterranei |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.1.1.315 | additional information | the purified enzyme does not require a divalent cation for catalytic activity | Amycolatopsis mediterranei |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.1.1.315 | 33800 | - |
x * 33800, His-tagged protein, calculated from sequence | Amycolatopsis mediterranei |
2.1.1.315 | 100000 | - |
non-denaturing PAGE | Amycolatopsis mediterranei |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.1.315 | S-adenosyl-L-methionine + 27-O-demethylrifamycin SV | Amycolatopsis mediterranei | the enzyme is involved in biosynthesis of rifamycin B | S-adenosyl-L-homocysteine + rifamycin SV | - |
? | |
2.1.1.315 | S-adenosyl-L-methionine + 27-O-demethylrifamycin SV | Amycolatopsis mediterranei S699 | the enzyme is involved in biosynthesis of rifamycin B | S-adenosyl-L-homocysteine + rifamycin SV | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.1.315 | Amycolatopsis mediterranei | - |
- |
- |
2.1.1.315 | Amycolatopsis mediterranei S699 | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.1.315 | additional information | poor methylation of S-adenosyl-L-methionine | Amycolatopsis mediterranei | ? | - |
? | |
2.1.1.315 | additional information | poor methylation of S-adenosyl-L-methionine | Amycolatopsis mediterranei S699 | ? | - |
? | |
2.1.1.315 | S-adenosyl-L-methionine + 27-O-demethylrifamycin SV | the enzyme is involved in biosynthesis of rifamycin B | Amycolatopsis mediterranei | S-adenosyl-L-homocysteine + rifamycin SV | - |
? | |
2.1.1.315 | S-adenosyl-L-methionine + 27-O-demethylrifamycin SV | the enzyme does not catalyze the methylation of rifamycin SV or rifamycin W | Amycolatopsis mediterranei | S-adenosyl-L-homocysteine + rifamycin SV | - |
? | |
2.1.1.315 | S-adenosyl-L-methionine + 27-O-demethylrifamycin SV | the enzyme is involved in biosynthesis of rifamycin B | Amycolatopsis mediterranei S699 | S-adenosyl-L-homocysteine + rifamycin SV | - |
? | |
2.1.1.315 | S-adenosyl-L-methionine + 27-O-demethylrifamycin SV | the enzyme does not catalyze the methylation of rifamycin SV or rifamycin W | Amycolatopsis mediterranei S699 | S-adenosyl-L-homocysteine + rifamycin SV | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.1.1.315 | ? | x * 33800, His-tagged protein, calculated from sequence | Amycolatopsis mediterranei |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.1.1.315 | AdoMet:27-O-demethylrifamycin SV methyltransferase | - |
Amycolatopsis mediterranei |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.1.1.315 | 30 | - |
assay at | Amycolatopsis mediterranei |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.1.1.315 | 87 | - |
27-O-demethylrifamycin SV | pH 8.0, 30°C | Amycolatopsis mediterranei |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.1.1.315 | 7.5 | 8 | - |
Amycolatopsis mediterranei |
2.1.1.315 | 8 | - |
assay at | Amycolatopsis mediterranei |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
2.1.1.315 | 6 | 8.5 | pH 6.0: about 20% of maximal activity, pH 8.5: about 70% of maximal activity | Amycolatopsis mediterranei |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.1.1.315 | malfunction | frameshift inactivation of rif orf14 generates a mutant that produces no rifamycin B, but accumulates 27-O-demethylrifamycin SV as the major new metabolite, together with a small quantity of 27-O-demethyl-25-O-desacetylrifamycin SV | Amycolatopsis mediterranei |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.1.1.315 | 4833 | - |
27-O-demethylrifamycin SV | pH 8.0, 30°C | Amycolatopsis mediterranei |