8esi

Structural highlights

Function

CBH_BIFLN Possesses dual functions in bile acid metabolism (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 all six major human conjugated bile salts, namely glycocholate (GCA), glycodeoxycholate (GDCA), glycochenodeoxycholate (GCDCA), taurocholate (TCA), taurodeoxycholate (TDCA) and taurochenodeoxycholate (TCDCA). Shows a slight preference for glycine-conjugated bile acids as substrates (PubMed:10831430, PubMed:16905539). 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. These BBAAs may facilitate communication between the microbiota and host through the activation of human ligand-activated transcription factors (By similarity). Is totally inactive toward penicillin V (PubMed:16905539).[UniProtKB:P0DXD2]^{[1] [2]}

References

1. ↑ Tanaka H, Hashiba H, Kok J, Mierau I. Bile salt hydrolase of Bifidobacterium longum-biochemical and genetic characterization. Appl Environ Microbiol. 2000 Jun;66(6):2502-12. PMID:10831430 doi:10.1128/AEM.66.6.2502-2512.2000
2. ↑ Kumar RS, Brannigan JA, Prabhune AA, Pundle AV, Dodson GG, Dodson EJ, Suresh CG. Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase. J Biol Chem. 2006 Oct 27;281(43):32516-25. Epub 2006 Aug 11. PMID:16905539 doi:10.1074/jbc.M604172200