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Literature summary extracted from
- Mechanistic investigation of cPMP synthase in molybdenum cofactor biosynthesis using an uncleavable substrate analogue (2015), Biochemistry, 54, 7229-7236 .
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.6.1.17 | (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-P-CH2-PP | compound is converted to an analogue of the MoaC reaction intermediate and causes mechanism-based inhibition. the reaction product harbors an acid-labile triaminopyrimidinone base without an established pyranopterin structure and forms a tight complex with MoaC likely through a covalent linkage | Escherichia coli |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.6.1.17 | Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.6.1.17 | (8S)-3',8-cyclo-7,8-dihydroguanosine-P[CH2]PP | - |
Escherichia coli | cyclic pyranopterin phosphate + diphosphate | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.6.1.17 | MoaC | - |
Escherichia coli |
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Release 2023.1 (January 2023)
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