Precorrin-4 C11-methyltransferase

From Wikipedia, the free encyclopedia

In enzymology, a precorrin-4 C11-methyltransferase (EC 2.1.1.133) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + precorrin-4 $\rightleftharpoons$ S-adenosyl-L-homocysteine + precorrin-5

Thus, the two substrates of this enzyme are S-adenosyl methionine and precorrin 4, whereas its two products are S-adenosylhomocysteine and precorrin 5.

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 C11 methyltransferase. Other names in common use include precorrin-3 methylase, and CobM. This enzyme participates in porphyrin and chlorophyll metabolism.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1CBF and 2CBF.

[edit] References

IUBMB entry for 2.1.1.133
BRENDA references for 2.1.1.133 (Recommended.)
PubMed references for 2.1.1.133
PubMed Central references for 2.1.1.133
Google Scholar references for 2.1.1.133
Thibaut D, Debussche L (1990). "Genetic and sequence analysis of an 8.7-kilobase Pseudomonas denitrificans fragment carrying eight genes involved in transformation of precorrin-2 to cobyrinic acid". J. Bacteriol. 172: 5980–90. PMID 2211521.
Roth JR, Lawrence JG, Rubenfield M, Kieffer-Higgins S, Church GM (1993). "Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium". J. Bacteriol. 175: 3303–16. PMID 8501034.