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

FieldValue
NameCobalt-precorrin-7 (C15)-methyltransferase (decarboxylating)
EC_number2.1.1.196

Cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating) (, CbiT) is an enzyme with systematic name S-adenosyl-L-methionine:precorrin-7 C15-methyltransferase (C12-decarboxylating). This enzyme catalyses the following chemical reaction

: cobalt-precorrin-7 + S-adenosyl-L-methionine \rightleftharpoons 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 of adenosylcobalamin biosynthesis in bacteria such as Salmonella typhimurium, Bacillus megaterium, and Propionibacterium freudenreichii subsp. shermanii.

References

References

  1. (November 2002). "The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase". Structure.
  2. (February 2006). "Structural characterization of novel cobalt corrinoids synthesized by enzymes of the vitamin B12 anaerobic pathway". Bioorganic & Medicinal Chemistry.
  3. R. Caspi. (2013-09-25). "Pathway: adenosylcobalamin biosynthesis I (anaerobic)". MetaCyc Metabolic Pathway Database.
Wikipedia Source

This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page.

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