Choloylglycine hydrolase - Misplaced Pages

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

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.

v t e Hydrolases: carbon-nitrogen non-peptide (EC 3.5)
3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aminoacylase ACY1 Aspartoacylase(ACY2) ACY3 Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin
3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase Dihydroorotase
3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase
3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase
3.5.5: Nitriles/ Aminohydrolases	Nitrilase
3.5.99: Other	Riboflavinase Thiaminase II

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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