Biology:Precorrin-8X methylmutase

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precorrin-8X methylmutase
1i1h.png
Crystal structure of precorrin-8x methyl mutase with bound hydrogenobyrinate. PDB 1i1h[1]
Identifiers
EC number5.4.99.61
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a precorrin-8X methylmutase (EC 5.4.99.61) is an enzyme that catalyzes the chemical reaction

precorrin-8X [math]\displaystyle{ \rightleftharpoons }[/math] hydrogenobyrinate

Hence, this enzyme has one substrate, precorrin 8X, and one product, hydrogenobyrinate.

This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is precorrin-8X 11,12-methylmutase. Other names in common use include precorrin isomerase, hydrogenobyrinic acid-binding protein and CobH. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.

See also

Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1F2V, 1I1H, 1OU0, 1V9C, 2AFR, and 2AFV.

References

  1. Shipman, L. W.; Li, D.; Roessner, C. A.; Scott, A. I.; Sacchettini, J. C. (2001). "Crystal structure of precorrin-8x methyl mutase". Structure 9 (7): 587–596. doi:10.1016/s0969-2126(01)00618-9. PMID 11470433.