Precorrin-2 C20-methyltransferase

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

S-adenosyl-L-methionine + precorrin-2 S-adenosyl-L-homocysteine + precorrin-3A

Thus, the two substrates of this enzyme are S-adenosyl methionine and precorrin 2, whereas 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. This enzyme participates in porphyrin and chlorophyll metabolism.

Structural studies

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


  • IUBMB entry for
  • BRENDA references for (Recommended.)
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  • 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: 73&ndash, 8. PMID 1451790.
  • Anousis N, Stolowich NJ, Holderman MT, Scott AI (1995). "Overexpression in Escherichia coli of 12 vitamin B12 biosynthetic enzymes". Protein. Expr. Purif. 6: 155&ndash, 63. 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: 7430&ndash, 40. PMID 8226690.

External links

Gene Ontology (GO) codes