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

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

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

  1. 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.
  2. 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

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