Structural highlights
Function
CBH_BIFLN 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 amid bond in all six major human 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). Is totally inactive toward penicillin V (PubMed:16905539).[1] [2]
References
- ↑ 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
- ↑ 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
