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Microbiology 151 (2005), 2017-2023; DOI  10.1099/mic.0.27767-0
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Microbiology 151 (2005), 2017-2023; DOI  10.1099/mic.0.27767-0
© 2005 Society for General Microbiology

The leucyl aminopeptidase from Helicobacter pylori is an allosteric enzyme

Lei Dong1,{dagger}, Ni Cheng1,{dagger}, Ming-Wei Wang2, Junfeng Zhang1, Chang Shu1 and De-Xu Zhu1

1 State Key Laboratory of Pharmaceutical Biotechnology, Department of Biochemistry, Nanjing University, Nanjing 210093, P. R. China
2 The National Center for Drug Screening, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, P. R. China

Correspondence
De-Xu Zhu
zjq{at}nju.edu.cn

This study describes the cloning, genetic analysis and biochemical characterization of a leucyl aminopeptidase (LAP) from Helicobacter pylori. A gene encoding LAP was cloned from H. pylori and the expressed 55 kDa protein displayed homology to aminopeptidases from Gram-negative bacteria, plants and mammals. This LAP demonstrated amidolytic activity against L-leucine-p-nitroanilide. Optimal activity was observed at pH 8·0 and 45 °C, with Vmax of 232 µmol min–1 (mg protein)–1 and S0·5 of 0·65 mM. The data suggest that LAP could be allosteric (nH=2·27), with regulatory homohexamers, and its activity was inhibited by ion chelators and enhanced by divalent manganese, cobalt and nickel cations. Bestatin inhibited both LAP activity (IC50=49·9 nM) and H. pylori growth in vitro. The results point to the potential use of LAP as a drug target to develop novel anti-H. pylori agents.

Abbreviations: ICP-AES, inductively coupled plasma-atomic emission spectrometry; LAP, leucyl aminopeptidase; L-Leu-p-NA, L-leucine-p-nitroanilide

{dagger}These authors contributed equally to this work.




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