P54965 · CBH_CLOPE
- ProteinBile salt hydrolase/transferase
- Genecbh
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids329 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Possesses dual functions in bile acid metabolism (PubMed:38326608).
Acts as a bile salt hydrolase that catalyzes the deconjugation of glycine- and taurine-linked bile salts, which occurs naturally in the intestines of humans, releasing amino acid residues and deconjugated bile salts (bile acids). Can hydrolyze the amide bond in major human conjugated bile salts, such as glycocholate (GCA), taurocholate (TCA) and taurodeoxycholate (TDCA) (PubMed:7618863, PubMed:15823032, PubMed:38326608).
Shows a slight preference for taurine-conjugated bile acids as substrates (PubMed:7618863).
Also acts as an amine N-acyltransferase that conjugates a wide variety of amino acids to conjugated and non-conjugated bile acids, thus producing bacterial bile acid amidates (BBAAs) - also named microbially conjugated bile acids (MCBAs) - in the gastrointestinal tract (PubMed:38326608).
These BBAAs may facilitate communication between the microbiota and host through the activation of human ligand-activated transcription factors (By similarity).
Acts as a bile salt hydrolase that catalyzes the deconjugation of glycine- and taurine-linked bile salts, which occurs naturally in the intestines of humans, releasing amino acid residues and deconjugated bile salts (bile acids). Can hydrolyze the amide bond in major human conjugated bile salts, such as glycocholate (GCA), taurocholate (TCA) and taurodeoxycholate (TDCA) (PubMed:7618863, PubMed:15823032, PubMed:38326608).
Shows a slight preference for taurine-conjugated bile acids as substrates (PubMed:7618863).
Also acts as an amine N-acyltransferase that conjugates a wide variety of amino acids to conjugated and non-conjugated bile acids, thus producing bacterial bile acid amidates (BBAAs) - also named microbially conjugated bile acids (MCBAs) - in the gastrointestinal tract (PubMed:38326608).
These BBAAs may facilitate communication between the microbiota and host through the activation of human ligand-activated transcription factors (By similarity).
Catalytic activity
- glycocholate + H2O = cholate + glycineThis reaction proceeds in the forward direction.
- cholate + taurine = H2O + taurocholateThis reaction proceeds in the backward direction.
- H2O + taurodeoxycholate = deoxycholate + taurineThis reaction proceeds in the forward direction.
- glycodeoxycholate + H2O = deoxycholate + glycineThis reaction proceeds in the forward direction.
- chenodeoxycholate + glycine = glycochenodeoxycholate + H2OThis reaction proceeds in the backward direction.
- H2O + taurochenodeoxycholate = chenodeoxycholate + taurineThis reaction proceeds in the forward direction.
- an L-alpha-amino acid + cholate = an N-choloyl-L-alpha-amino acid + H2OThis reaction proceeds in the forward direction.
- an L-alpha-amino acid + taurocholate = an N-choloyl-L-alpha-amino acid + taurineThis reaction proceeds in the forward direction.
- an L-alpha-amino acid + glycocholate = an N-choloyl-L-alpha-amino acid + glycineThis reaction proceeds in the forward direction.
- cholate + L-histidine = H2O + L-histidocholateThis reaction proceeds in the forward direction.
- L-histidine + taurocholate = L-histidocholate + taurineThis reaction proceeds in the forward direction.
- glycocholate + L-histidine = glycine + L-histidocholateThis reaction proceeds in the forward direction.
- cholate + L-arginine = H2O + L-arginocholateThis reaction proceeds in the forward direction.
- L-arginine + taurocholate = L-arginocholate + taurineThis reaction proceeds in the forward direction.
- glycocholate + L-arginine = glycine + L-arginocholateThis reaction proceeds in the forward direction.
- cholate + L-phenylalanine = H2O + L-phenylalanocholateThis reaction proceeds in the forward direction.
- L-phenylalanine + taurocholate = L-phenylalanocholate + taurineThis reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.443 mM | taurocholate | in the TCA deconjugation assay |
pH Dependence
Hydrolase activity occurs over a broad pH range (pH 3-7) with an optimum pH of 5.5 (PubMed:38326608, PubMed:7618863).
Optimum pH is 5.3 for acyltransferase activity, which is close to that of lower human gastrointestinal tract (PubMed:38326608).
Optimum pH is 5.3 for acyltransferase activity, which is close to that of lower human gastrointestinal tract (PubMed:38326608).
Pathway
Lipid metabolism; bile acid biosynthesis.
Features
Showing features for active site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | chenodeoxycholoyltaurine hydrolase activity | |
Molecular Function | choloylglycine hydrolase activity | |
Molecular Function | transferase activity | |
Biological Process | bile acid biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameBile salt hydrolase/transferase
- Short namesBSH/T
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Clostridiaceae > Clostridium
Accessions
- Primary accessionP54965
Proteomes
Phenotypes & Variants
Disruption phenotype
Cells lacking this gene continue to express conjugated bile acid hydrolase activity at 86% of wild-type levels.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 2 | Loss of both hydrolase and acyltransferase activities. | ||||
Sequence: C → A | ||||||
Mutagenesis | 82 | Impaired MCBA production. No change in hydrolase activity. | ||||
Sequence: N → Y |
Chemistry
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000073019 | 2-329 | Bile salt hydrolase/transferase | |||
Sequence: CTGLALETKDGLHLFGRNMDIEYSFNQSIIFIPRNFKCVNKSNKKELTTKYAVLGMGTIFDDYPTFADGMNEKGLGCAGLNFPVYVSYSKEDIEGKTNIPVYNFLLWVLANFSSVEEVKEALKNANIVDIPISENIPNTTLHWMISDITGKSIVVEQTKEKLNVFDNNIGVLTNSPTFDWHVANLNQYVGLRYNQVPEFKLGDQSLTALGQGTGLVGLPGDFTPASRFIRVAFLRDAMIKNDKDSIDLIEFFHILNNVAMVRGSTRTVEEKSDLTQYTSCMCLEKGIYYYNTYENNQINAIDMNKENLDGNEIKTYKYNKTLSINHVN |
Structure
Sequence
- Sequence statusComplete
- Length329
- Mass (Da)37,185
- Last updated2007-01-23 v3
- ChecksumB0643160A27A368D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U20191 EMBL· GenBank· DDBJ | AAC43454.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BA000016 EMBL· GenBank· DDBJ | BAB80415.1 EMBL· GenBank· DDBJ | Genomic DNA |