Precorrin-2 C20-methyltransferase

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precorrin-2 C20-methyltransferase
Identifiers
EC no.2.1.1.130
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a precorrin-2 C20-methyltransferase (EC 2.1.1.130) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + precorrin-2 S-adenosyl-L-homocysteine + precorrin-3A
precorrin-2 substrate of the enzyme

The two substrates of this enzyme are S-adenosyl methionine and precorrin 2 and its two products are S-adenosylhomocysteine and precorrin 3A.

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-4 C20-methyltransferase and another names in common use is CobI. The enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.

See also[edit]

Structural studies[edit]

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2E0K and 2E0N.

References[edit]

  • Stolowich NJ, Iida K, Scott AI (1992). "Expression of 9 Salmonella typhimurium enzymes for cobinamide synthesis. Identification of the 11-methyl and 20-methyl transferases of corrin biosynthesis". FEBS Lett. 301 (1): 73–8. doi:10.1016/0014-5793(92)80213-Z. PMID 1451790. S2CID 20198692.
  • Anousis N, Stolowich NJ, Holderman MT, Scott AI (1995). "Overexpression in Escherichia coli of 12 vitamin B12 biosynthetic enzymes". Protein Expr. Purif. 6 (2): 155–63. doi:10.1006/prep.1995.1019. PMID 7606163.
  • 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. doi:10.1128/jb.175.22.7430-7440.1993. PMC 206888. PMID 8226690.