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Biochem Biophys Res Commun. 2013 Aug 9;437(4):538-43. doi: 10.1016/j.bbrc.2013.06.109. Epub 2013 Jul 12.

Structural modelling of substrate binding and inhibition in penicillin V acylase from Pectobacterium atrosepticum.

Author information

1
Division of Biochemical Sciences, National Chemical Laboratory, Pune, India.

Abstract

Penicillin V acylases (PVAs) and bile salt hydrolases (BSHs) have considerable sequence and structural similarity; however, they vary significantly in their substrate specificity. We have identified a PVA from a Gram-negative organism, Pectobacterium atrosepticum (PaPVA) that turned out to be a remote homolog of the PVAs and BSHs reported earlier. Even though the active site residues were conserved in PaPVA it showed high specificity towards penV and interestingly the penV acylase activity was inhibited by bile salts. Comparative modelling and docking studies were carried out to understand the structural differences of the binding site that confer this characteristic property. We show that PaPVA exhibits significant differences in structure, which are in contrast to those of known PVAs and such enzymes from Gram-negative bacteria require further investigation.

KEYWORDS:

Bile salt hydrolase; Docking; Homology modelling; Inhibition; Pectobacterium; Penicillin acylase

PMID:
23850621
DOI:
10.1016/j.bbrc.2013.06.109
[Indexed for MEDLINE]

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