Choloylglycine hydrolase

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
choloylglycine hydrolase
Identifiers
EC no.3.5.1.24
CAS no.37289-07-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

  1. 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.
  2. 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.


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