Precorrin-2 C20-methyltransferase

precorrin-2 C20-methyltransferase
Identifiers
EC no.	2.1.1.130
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

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 ${\displaystyle \rightleftharpoons }$ 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

• Cobalamin biosynthesis

Structural studies

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

References

• 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. Bibcode:1992FEBSL.301...73R. 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.