Cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating)
Cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating) | |||||||||
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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 systematic 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.; 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.; 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)
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