chenodeoxycholoyltaurine hydrolase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 3.5.1.74 | ||||||||
CAS no. | 125752-75-2 | ||||||||
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 | ||||||||
|
In enzymology, a chenodeoxycholoyltaurine hydrolase (EC 3.5.1.74) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are chenodeoxycholoyltaurine and H2O, whereas its two products are chenodeoxycholate and taurine.
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 chenodeoxycholoyltaurine amidohydrolase. This enzyme participates in bile acid biosynthesis.
Hydrolase is a class of enzymes that commonly perform as biochemical catalysts that use water to break a chemical bond, which typically results in dividing a larger molecule into smaller molecules. Some common examples of hydrolase enzymes are esterases including lipases, phosphatases, glycosidases, peptidases, and nucleosidases.
In enzymology, a taurine-transporting ATPase (EC 3.6.3.36) is an enzyme that catalyzes the chemical reaction.
The enzyme α-amino-acid esterase (EC 3.1.1.43) catalyzes the reaction
In enzymology, a bile-acid-CoA hydrolase (EC 3.1.2.26) is an enzyme that catalyzes the chemical reaction
The enzyme choloyl-CoA hydrolase (EC 3.1.2.27) catalyzes the reaction
The enzyme sterol esterase (EC 3.1.1.13) catalyzes the reaction
In enzymology, a 6-aminohexanoate-dimer hydrolase (EC 3.5.1.46) is an enzyme that catalyzes the chemical reaction N-(6-aminohexanoyl)-6-aminohexanoate + H2O 2 6-aminohexanoate. Thus, the two substrates of this enzyme are N-(6-aminohexanoyl)-6-aminohexanoate and H2O, whereas its product is two molecules of 6-aminohexanoate.
In enzymology, an amidase (EC 3.5.1.4, acylamidase, acylase (misleading), amidohydrolase (ambiguous), deaminase (ambiguous), fatty acylamidase, N-acetylaminohydrolase (ambiguous)) is an enzyme that catalyzes the hydrolysis of an amide. In this way, the two substrates of this enzyme are an amide and H2O, whereas its two products are monocarboxylate and NH3.
In enzymology, a choloylglycine hydrolase (EC 3.5.1.24) is an enzyme that catalyzes the chemical reaction
In enzymology, a cyanoalanine nitrilase (EC 3.5.5.4) is an enzyme that catalyzes the chemical reaction
In enzymology, a hippurate hydrolase (EC 3.5.1.32) is an enzyme that catalyzes the chemical reaction
In enzymology, an imidazolonepropionase (EC 3.5.2.7) is an enzyme that catalyzes the chemical reaction
In enzymology, a mandelamide amidase (EC 3.5.1.86) is an enzyme that catalyzes the chemical reaction
In enzymology, a methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) is an enzyme that catalyzes the chemical reaction
In enzymology, a N-acyl-D-amino-acid deacylase (EC 3.5.1.81) is an enzyme that catalyzes the chemical reaction
In enzymology, Nα-benzyloxycarbonylleucine hydrolase (EC 3.5.1.64) is an enzyme that catalyzes the chemical reaction
In enzymology, a N-benzyloxycarbonylglycine hydrolase (EC 3.5.1.58) is an enzyme that catalyzes the chemical reaction
In enzymology, a N-carbamoyl-L-amino-acid hydrolase (EC 3.5.1.87) is an enzyme that catalyzes the chemical reaction
In enzymology, a pantothenase (EC 3.5.1.22) is an enzyme that catalyzes the chemical reaction
Bile salt hydrolases (BSH) are microbial enzymes that deconjugate primary bile acids. They catalyze the first step of bile acid metabolism and maintain the bile acid pool for further modification by the microbiota. BSH enzymes play a role in a range of host and microbe functions including host physiology, immunity, and protection from pathogens.