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

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Cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating)
Identifiers
EC number2.1.1.196
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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 [math]\displaystyle{ \rightleftharpoons }[/math] 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. "The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase". Structure 10 (11): 1475–87. November 2002. doi:10.1016/S0969-2126(02)00876-6. PMID 12429089. 
  2. "Structural characterization of novel cobalt corrinoids synthesized by enzymes of the vitamin B12 anaerobic pathway". Bioorganic & Medicinal Chemistry 14 (3): 724–31. February 2006. 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. https://biocyc.org/META/NEW-IMAGE?type=PATHWAY&object=PWY-5507. Retrieved 2020-04-24. 

External links