Format

Send to

Choose Destination
Eur J Biochem. 2001 Oct;268(20):5321-8.

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

Author information

1
Department of Bioresources Science, Faculty of Agriculture, Kochi University, Nankoku, Japan. ashiuchi@cc.kochi-u.ac.jp

Erratum in

  • Eur J Biochem 2001 Nov;268(22):6003.

Abstract

An enzymatic system for poly gamma-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.

[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center