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

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Title
Physiological and biochemical characteristics of poly γ-glutamate synthetase complex of Bacillus subtilis
Author(s)
Makoto Ashiuchi; Chizuko Nawa; Tohru Kamei; Jae Jun Song; Seung Pyo Hong; Moon Hee Sung; Kenji Soda; Toshiharu Yagi; Haruo Misono
Bibliographic Citation
European Journal of Biochemistry, vol. 268, no. 20, pp. 5321-5328
Publication Year
2001
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.
Keyword
Gene disruptionIn vitro transcriptionMembranous amide ligaseNonribosomal polypeptide synthesisPoly γ-glutamate synthetase complexTranslation
ISSN
0014-2956
Publisher
Wiley
DOI
http://dx.doi.org/10.1046/j.0014-2956.2001.02475.x
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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