Hippurate hydrolase
Appearance
hippurate hydrolase | |||||||||
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Identifiers | |||||||||
EC no. | 3.5.1.32 | ||||||||
CAS no. | 37278-43-6 | ||||||||
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 hippurate hydrolase (EC 3.5.1.32) is an enzyme that catalyzes the chemical reaction
- hippurate + H2O benzoate + glycine
Thus, the two substrates of this enzyme are hippurate and H2O, whereas its two products are benzoate 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 N-benzoylamino-acid amidohydrolase. This enzyme participates in phenylalanine metabolism.
Hippurate hydrolysis test is used in the presumptive identification of Gardnerella vaginalis, Campylobacter jejuni, Listeria monocytogenes and group B streptococci by detecting the ability of the organism to hydrolyze hippurate.[1]
References
[edit]- Tsoi E, Akmal S, Geerts L, Jeffery B, Nicolaides KH (2006). "Sonographic measurement of cervical length and fetal fibronectin testing in threatened preterm labor". Ultrasound Obstet. Gynecol. 27 (4): 368–72. doi:10.1002/uog.2723. PMID 16526097.
- Tsoi E, Akmal S, Geerts L, Jeffery B, Nicolaides KH (2006). "Sonographic measurement of cervical length and fetal fibronectin testing in threatened preterm labor". Ultrasound Obstet. Gynecol. 27 (4): 368–72. doi:10.1002/uog.2723. PMID 16526097.
- Rohrmann K, Niemann R, Buddecke E (1985). "Two N-acetylgalactosaminyltransferase are involved in the biosynthesis of chondroitin sulfate". Eur. J. Biochem. 148 (3): 463–9. doi:10.1111/j.1432-1033.1985.tb08862.x. PMID 3922754.