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PEDS Advance Access published online on December 21, 2007
Protein Engineering Design and Selection, doi:10.1093/protein/gzm068
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© The Author 2007. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Streptomyces aminopeptidase P: biochemical characterization and insight into the roles of its N-terminal domain

Jiro Arima1, Yoshiko Uesugi, Masaki Iwabuchi and Tadashi Hatanaka2

Research Institute for Biological Sciences (RIBS), Okayama, 7549-1 Kibichuo-cho, Kaga-gun, Okayama 716-1241, Japan

2 To whom correspondence should be addressed. E-mail: hatanaka{at}bio-ribs.com

We purified and characterized the aminopeptidase P from Streptomyces costaricanus TH-4 (thAPP). This enzyme has a tetramer structure, a metal-ion preference toward Zn, broad substrate specificity and a narrow pH dependency for activity. The primary structure of thAPP, respectively, exhibits 91% and 65% identity with those of two other APPs—APP I and APP II—from Streptomyces lividans (slAPP I and slAPP II). We next overexpressed the genes encoding thAPP and slAPP II in Escherichia coli and characterized them. Two differences were apparent in their properties: slAPP II formed a dimer, whereas thAPP formed a tetramer; also, the alkaline side pKa for the catalytic action of slAPP II is higher than that of thAPP. Investigation using chimeras of both enzymes revealed that the N-terminal domain is associated with the determination of pKa values for catalytic action and quaternary structure.

Keywords: aminopeptidase P/homology modeling/pKa value for catalytic action/quaternary structure/Streptomyces

Received June 12, 2007; revised October 30, 2007; accepted October 31, 2007.

1 Present address: Department of Agricultural Chemistry, Faculty of Agriculture, Tottori University, Tottori 680-8553, Japan


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