Cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating)
| Cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.1.1.196 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating) (EC 2.1.1.196, CbiT) is an enzyme with system name S-adenosyl-L-methionine:precorrin-7 C15-methyltransferase (C-12-decarboxylating).[1][2] This enzyme catalyses the following chemical reaction
- cobalt-precorrin-7 + S-adenosyl-L-methionine
cobalt-precorrin-8x + S-adenosyl-L-homocysteine + CO2
This enzyme catalyses both methylation at C-15 and decarboxylation of the C-12 acetate side chain of cobalt-precorrin-7.
References
- ↑ Keller, J.P., Smith, P.M., Benach, J., Christendat, D., deTitta, G.T. and Hunt, J.F. (2002). "The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase". Structure 10 (11): 1475–1487. doi:10.1016/S0969-2126(02)00876-6. PMID 12429089.
- ↑ Santander, P.J., Kajiwara, Y., Williams, H.J. and Scott, A.I. (2006). "Structural characterization of novel cobalt corrinoids synthesized by enzymes of the vitamin B12 anaerobic pathway". Bioorg. Med. Chem. 14 (3): 724–731. doi:10.1016/j.bmc.2005.08.062. PMID 16198574.
External links
- Cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating) at the US National Library of Medicine Medical Subject Headings (MeSH)