In enzymology, a choloylglycine hydrolase (EC 3.5.1.24) is an enzyme that catalyzes the chemical reaction
| choloylglycine hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.24 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
- 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.[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
editAs of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 2BJF, 2BJG, 2HEZ, and 2HF0.
Research
editA 2018 study has linked the enzyme in gut bacteria to obesity and carbohydrate metabolism dominating over fat metabolism.
References
edit- ^ Coleman JP, Hudson LL (1995). "Cloning and characterization of a conjugated bile acid hydrolase gene from Clostridium perfringens". Appl Environ Microbiol. 61 (7): 2514–20. Bibcode:1995ApEnM..61.2514C. doi:10.1128/AEM.61.7.2514-2520.1995. PMC 167523. PMID 7618863.
- ^ Rossocha M, Schultz-Heienbrok R, von Moeller H, Coleman JP, Saenger W (2005). "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. doi:10.1021/bi0473206. PMID 15823032.
- 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. doi:10.1016/S0021-9258(18)96311-8. 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. doi:10.1016/0005-2744(76)90068-1. PMID 10993.
