Author:
Rayamajhi Nabin,Joo Jeong Chan,Cha Seung Bin,Pokherl Subarna,Shin Min Kyung,Yoo Young Je,Yoo Han Sang
Abstract
Abstract
Background
The aim of this study was to analyze the significance of leucine to proline substitution at position 138(Leu138Pro) on the hydrolysis of penicillin and ampicillin that we identified in the bla
SHV gene of clinical Escherichia coli swine isolate.
Results
Kinetic analysis of the mutant proteins showed that K
m
value of the purified L138P mutant was comparatively higher than SHV-1, SHV-33 and SHV-33(L138P) enzyme for penicillin and ampicillin. Docking simulation of the SHV-1 and SHV-(L138P) enzymes also confirmed that β-lactamases preferred penicillin to ampicillin and the SHV-1 had a higher binding affinity for antibiotics compared to the SHV-(L138P) and other mutants.
Conclusions
Our result demonstrated that L138P has a reduced role in penicillin and ampicillin hydrolyzing properties of SHV β-lactamases. These naturally occurring mutations rendering reduced function of the existing protein could trigger the emergence or acquisition of more effective alternative mechanisms for β-lactam hydrolysis.
Publisher
Springer Science and Business Media LLC
Subject
Microbiology (medical),Microbiology
Cited by
3 articles.
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