Cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating)

Cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating)
Identifiers
EC no.2.1.1.196
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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 (C12-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 in the anaerobic pathway[3] of adenosylcobalamin biosynthesis in bacteria such as Salmonella typhimurium, Bacillus megaterium, and Propionibacterium freudenreichii subsp. shermanii.

See also

References

  1. ^ Keller JP, Smith PM, Benach J, Christendat D, deTitta GT, Hunt JF (November 2002). "The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase". Structure. 10 (11): 1475–87. doi:10.1016/S0969-2126(02)00876-6. PMID 12429089.
  2. ^ Santander PJ, Kajiwara Y, Williams HJ, Scott AI (February 2006). "Structural characterization of novel cobalt corrinoids synthesized by enzymes of the vitamin B12 anaerobic pathway". Bioorganic & Medicinal Chemistry. 14 (3): 724–31. doi:10.1016/j.bmc.2005.08.062. PMID 16198574.
  3. ^ R. Caspi (2013-09-25). "Pathway: adenosylcobalamin biosynthesis I (anaerobic)". MetaCyc Metabolic Pathway Database. Retrieved 2020-04-24.