EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.2.2.16 | additional information | MTAN is not inhibited by the highly reactive 5'-deoxyadenosyl radical | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.2.16 | additional information | - |
additional information | Michelis-Menten kinetics, substrate 5'-deoxyadenosine | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.2.16 | S-methyl-5'-thioadenosine + H2O | Escherichia coli | - |
S-methyl-5-thio-D-ribose + adenine | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.2.16 | Escherichia coli | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.2.16 | 5'-deoxyadenosine + H2O | i.e. DOA, MTAN can rapidly hydrolyse DOA | Escherichia coli | 5-deoxy-D-ribose + adenine | - |
? | |
3.2.2.16 | additional information | MTAN restores the activity of three S-adenosyl-L-methionine utilizing enzymes, biotin synthase, lipoyl synthase and tyrosine lyase, that are inhibited by the highly reactive 5'-deoxyadenosyl radical, overview | Escherichia coli | ? | - |
? | |
3.2.2.16 | S-methyl-5'-thioadenosine + H2O | - |
Escherichia coli | S-methyl-5-thio-D-ribose + adenine | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.2.16 | 5'-methylthioadenosine nucleosidase | - |
Escherichia coli |
3.2.2.16 | MTAN | - |
Escherichia coli |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.2.16 | 37 | - |
assay at | Escherichia coli |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.2.16 | 7.5 | - |
assay at | Escherichia coli |