Precorrin-3B C17-methyltransferase
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Precorrin-3B C17-methyltransferase (EC 2.1.1.131) is an enzyme that catalyzes the chemical reaction
| Precorrin-3B C17-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.131 | ||||||||
| CAS no. | 152787-64-9 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The two substrates of this enzyme are the chlorin, precorrin-3B and S-adenosyl methionine. Its products are precorrin-4 and S-adenosylhomocysteine.[1][2][3]
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:precorrin-3B C17-methyltransferase. Other names in common use include precorrin-3 methyltransferase, and CobJ. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria and during this step the macrocycle ring-contracts so that the corrin core of the vitamin is formed.
