Choloylglycine hydrolase

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In enzymology, a choloylglycine hydrolase (EC 3.5.1.24) is an enzyme that catalyzes the chemical reaction

3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-oylglycine + H₂O $\rightleftharpoons$ 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine

Thus, the two substrates of this enzyme are 3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-oylglycine and H₂O, whereas its two products are 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate and glycine.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-oylglycine amidohydrolase. Other names in common use include glycocholase, bile salt hydrolase, and choloyltaurine hydrolase. This enzyme participates in bile acid biosynthesis.

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

[edit] Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 2BJF, 2BJG, 2HEZ, and 2HF0.

[edit] References

IUBMB entry for 3.5.1.24
BRENDA references for 3.5.1.24 (Recommended.)
PubMed references for 3.5.1.24
PubMed Central references for 3.5.1.24
Google Scholar references for 3.5.1.24
Nair PP, Gordon M, Reback J (1967). "The enzymatic cleavage of the carbon-nitrogen bond in 3-alpha, 7-alpha, 12-alpha-trihydroxy-5-beta-cholan-24-oylglycine". J. Biol. Chem. 242: 7–11. PMID 6016335.
Stellwag EJ, Hylemon PB (1976). "Purification and characterization of bile salt hydrolase from Bacteroides fragilis subsp. fragilis". Biochim. Biophys. Acta. 452: 165–76. PMID 10993.