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J. Biol. Chem., Vol. 277, Issue 45, 43536-43543, November 8, 2002
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From the Division of Integrated Life Science, Graduate School of
Biostudies, Kyoto University, Kitashirakawa, Sakyo-ku,
Kyoto 606-8502, Japan
Autocatalytic Processing of
-Glutamyltranspeptidase*
and
-Glutamyltranspeptidase is the key
enzyme in glutathione metabolism, and we previously presented evidence
suggesting that it belongs to the N-terminal nucleophile hydrolase
superfamily. Enzymatically active -glutamyltranspeptidase, which
consists of one large subunit and one small subunit, is generated from an inactive common precursor through post-translational proteolytic processing. The processing mechanism for -glutamyltranspeptidase of
Escherichia coli K-12 has been analyzed by means of
in vitro studies using purified precursors. Here we show
that the processing of a precursor of -glutamyltranspeptidase is an
intramolecular autocatalytic event and that the catalytic nucleophile
for the processing reaction is the oxygen atom of the side chain of
Thr-391 (N-terminal residue of the small (
) subunit), which is also
the nucleophile for the enzymatic reaction.
*
This work was supported by Grants-in-aid for Scientific
Research 13660090 (to H. S.) and 10306007 (to H. K.) from the
Ministry of Education, Culture, Sports, Science, and Technology of
Japan and by Novozymes Enzyme Fund 2001 (to H. S.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Tel.
81-75-753-6278; Fax: 81-75-753-6275; E-mail:
hideyuki@lif.kyoto-u.ac.jp.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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