Abstract
Bile salt hydrolase (BSH) and penicillin V acylase (PVA) are related enzymes that are classified as choloylglycine hydrolases (CGH). BSH enzymes have attracted significant interest for their ability to modulate the composition of the bile acid pool, alter bile acid signaling events mediated by the host bile acid receptors FXR and TGR5 and influence cholesterol homeostasis in the host, while PVA enzymes have been widely utilised in an industrial capacity in the production of semi-synthetic antibiotics. The similarities between BSH and PVA enzymes suggest common evolution of these enzymes and shared mechanisms for substrate binding and catalysis. Here, we compare BSH and PVA through analysis of the distribution, phylogeny and biochemistry of these microbial enzymes. The development of new annotation approaches based upon functional enzyme analyses and the potential implications of BSH enzymes for host health are discussed.
Highlights
A recent study utilising deletion mutations of Bile salt hydrolase (BSH) in L. acidophilus and L. gasseri strains showed that, while BSH enzymes contributed to enhanced survival against specific bile acids in vitro, the enzymes were dispensable for survival in germ-free mice and in an ex vivo caecal survival model [27]
This study found all four BSH to exhibit significant catalytic activity towards conjugated bile salts and argued that all four putative proteins in L. plantarum are necessary for activity
Cloned BSH expressed in E. coli delivered to the GI tract was capable of altering systemic bile acid profiles in gnotobiotic mice and influenced a wide variety of host signalling pathways, a specific role for farnesoid X receptor (FXR) was not examined [79]
Summary
Microorganisms 2021, 9, Bile salt hydrolase (BSH) and penicillin V acylase (PVA) are related enzymes that are classified as choloylglycine hydrolases (CGH) within the Ntn (N-terminal nucleophile) hydrolase enzyme superfamily [1]. This superfamily is characterised by the catalytic mechanism which involves a nucleophilic attack by the N-terminal residue on the substrate carbonyl carbon of the amide bond [2,3]. BSH proteins were typically found in gut-related bacterial communities, whereas genes encoding PVA were found in marine and soil metagenomes. The amide bonds hydrolysed by either bile salt hydrolase (BSH) or penicillin V acylase (PVA) are annotated by the green arrow
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