Biology:Choloylglycine hydrolase
| 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 / QuickGO | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 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.[1][2]
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.
Research
A 2018 study has linked the enzyme in gut bacteria to obesity and carbohydrate metabolism dominating over fat metabolism.
References
- ↑ "Cloning and characterization of a conjugated bile acid hydrolase gene from Clostridium perfringens.". Appl Environ Microbiol 61 (7): 2514–20. 1995. doi:10.1128/AEM.61.7.2514-2520.1995. PMID 7618863. Bibcode: 1995ApEnM..61.2514C.
- ↑ "Conjugated bile acid hydrolase is a tetrameric N-terminal thiol hydrolase with specific recognition of its cholyl but not of its tauryl product.". Biochemistry 44 (15): 5739–48. 2005. doi:10.1021/bi0473206. PMID 15823032.
- "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. 1967. doi:10.1016/S0021-9258(18)96311-8. PMID 6016335.
- "Purification and characterization of bile salt hydrolase from Bacteroides fragilis subsp. fragilis". Biochim. Biophys. Acta 452 (1): 165–76. 1976. doi:10.1016/0005-2744(76)90068-1. PMID 10993.
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