Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodobacter capsulatus | P26168 | - |
- |
Rhodobacter capsulatus ATCC BAA-309 | P26168 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine | - |
Rhodobacter capsulatus | 131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine | - |
? | |
131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine | - |
Rhodobacter capsulatus ATCC BAA-309 | 131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine | - |
? | |
131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine | - |
Rhodobacter capsulatus | 3,8-divinyl protochlorophyllide a + 5'-deoxyadenosine + L-methionine | - |
? | |
131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine | - |
Rhodobacter capsulatus ATCC BAA-309 | 3,8-divinyl protochlorophyllide a + 5'-deoxyadenosine + L-methionine | - |
? | |
magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine + H2O | - |
Rhodobacter capsulatus | 131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine | - |
? | |
magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine + H2O | - |
Rhodobacter capsulatus ATCC BAA-309 | 131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
Cobalamin | vitamin B12-requiring mutants of the bluE and bluB genes of Rhodobacter capsulatus, grown without B12, accumulate Mg-protoporphyrin monomethyl ester and its 3-vinyl-8-ethyl derivative. Cyclase activity in the B12-dependent mutants requires vitamin B12 but not protein synthesis | Rhodobacter capsulatus |
General Information | Comment | Organism |
---|---|---|
metabolism | proposed reaction mechanism for the Mg-protoporphyrin monomethyl ester-cyclase reaction starts with adenosylcobalamin forming the adenosyl radical, which leads to withdrawal of a hydrogen atom and formation of the benzylic-type 131-radical of Mg-protoporphyrin monomethyl ester. Withdrawal of an electron gives the 131-cation of Mg-protoporphyrin monomethyl ester. Hydroxyl ion attack on the cation gives 131-hydroxy-Mg-protoporphyrin monomethyl ester. Withdrawal of three hydrogen atoms leads successively to 131-keto-Mg-protoporphyrin monomethyl ester, its 132-Mg-protoporphyrin monomethyl ester, and cyclization to protochlorophyllide | Rhodobacter capsulatus |