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