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. 2022 Sep 19;23(18):10980. doi: 10.3390/ijms231810980

Figure 2.

Figure 2

Sequence analyses of the putative LcBSH and GfBSH. (A) Overall and (B) catalytic active site superposition images of LcBSH (blue) and GfBSH (green) with CpBSH from Clostridium perfringens (gray; PDB accession number 2RLC). The degradation products (glycine and cholic acid) of glycocholic acid by CpBSH are shown in magenta sticks. (C) Multiple alignment analysis of the putative LcBSH and GfBSH. Amino acid sequences of LcBSH and GfBSH were compared with characterized bile salt hydrolases (BSHs) from gut bacteria. The black and gray backgrounds indicate identical and similar amino acid residues, respectively. The conserved residues (Cys, Arg, Asp, Asn, and Arg) related to the catalytic active site are boxed in red lines. Abbreviated as: BlBSH (AAF67801) from Bifidobacterium longum SBT2928; CpBSH (P54965) from Clostridium perfringens 13; LgBSH (WP_020806888) from Lactobacillus gasseri FR4.