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Title 

Physiological and biochemical characteristics of poly γ-glutamate synthetase complex of Bacillus subtilis

Authors 

Makoto AshiuchiChizuko NawaTohru KameiJae Jun SongSeung Pyo HongMoon Hee SungKenji SodaToshiharu YagiHaruo Misono

Publisher 

Federation of European Biochemical Societies

Issue Date 

2001

Citation 

European Journal of Biochemistry, vol. 268, no. 20, pp. 5321-5328

Keywords 

gene disruptionin vitro transcriptionmembranous amide ligasenonribosomal polypeptide synthesispoly γ-glutamate synthetase complextranslationglutamate synthasepoly gamma glutamate synthetasebacillus subtilismultienzyme complexes

Abstract 

An enzymatic system for poly γ-glutamate (PGA) synthesis in Bacillus subtilis, the PgsBCA system, was investigated. The gene-disruption experiment showed that the enzymatic system was the sole machinery of PGA synthesis in B. subtilis. We succeeded in achieving the enzymatic synthesis of elongated PGAs with the cell membrane of the Escherichia coli clone producing PgsBCA in the presence of ATP and D-glutamate. The enzyme preparation solubilized from the membrane with 8 mM Chaps catalyzed ADP-forming ATP hydrolysis only in the presence of glutamate; the D-enantiomer was the best cosubstrate, followed by the L-enantiomer. Each component of the system, PgsB, PgsC, and PgsA, was translated in vitro and the glutamate-dependent ATPase reaction was kinetically analyzed. The PGA synthetase complex, PgsBCA, was suggested to be an atypical amide ligase.

ISSN 

0014-2956

Link 

http://dx.doi.org/10.1046/j.0014-2956.2001.02475.x

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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