- Choloylglycine hydrolase
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choloylglycine hydrolase Identifiers EC number 3.5.1.24 CAS number 37289-07-9 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 / EGO Search PMC articles PubMed articles 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 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.
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.
References
- 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 (1): 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 (1): 165–76. PMID 10993.
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