Precorrin-6A synthase (deacetylating)

In enzymology, precorrin-6A synthase (deacetylating) (EC 2.1.1.152) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + precorrin-5 + H2O S-adenosyl-L-homocysteine + precorrin-6A + acetate
precorrin-6A synthase (deacetylating)
Identifiers
EC no.2.1.1.152
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

The 3 substrates of this enzyme are S-adenosyl methionine, precorrin 5, and H2O. Its 3 products are S-adenosylhomocysteine, precorrin 6A, and acetate.

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:precorrin-5 C1-methyltransferase (deacetylating). Other names in common use include precorrin-6X synthase (deacetylating), and CobF. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.

See also

References

    • Debussche L, Thibaut D, Cameron B, Crouzet J, Blanche F (1993). "Biosynthesis of the corrin macrocycle of coenzyme B12 in Pseudomonas denitrificans". J. Bacteriol. 175 (22): 7430–40. PMC 206888. PMID 8226690.
    • Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC (2002). "The biosynthesis of adenosylcobalamin (vitamin B12)". Nat. Prod. Rep. 19 (4): 390–412. doi:10.1039/b108967f. PMID 12195810.


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