Function and Biosynthetic Mechanism of Poly-γ-Glutamate, a Main Component of Natto Mucilage

MISONO Haruo, ASHIUCHI Makoto

doi:10.20632/vso.79.2_71

Bibliographic Information

Other Title

「納豆の糸」の主成分,ポリ-γ-グルタミン酸の機能と生合成機構(第56回大会シンポジウム(I))
「納豆の糸」の主成分,ポリ-γ-グルタミン酸の機能と生合成機構
ナットウノイトノシュセイブンポリガンマグルタミンサンノキノウトセイゴウセイキコウ

Search this article

Description

Poly-γ-glutamate (PGA) is an unusual polypeptide in which glutamate is polymerized via γ-amide linkages. PGA is produced by Bacillus strains, Natrialba aegyptiaca, and hydra. PGA, which is biodegradable and highly water-absorbent acidic polymer, is not attacked by proteases, evades mammalian immune defense mechanisms, binds Ca^<2+>, and serves as a cryoprotective material. PGA may physiologically function as an adaptation agent in various environments. Multifarious applications of PGA have been developed based on its function. PGA produced by Bacillus subtilis IFO 3336 contains a large amount of D-glutamate. D-Glutamate was formed from L-glutamate by glutamate racemase in this organism. Two kinds of glutamate racemase isozymes, Glr and YrpC, were found in B, subtilis IFO 3336, and Glr supplied D-glutamate for the PGA production. The pgsBCA genes encoding the membrane-associated PGA synthetase complex of B. subtilis IFO 3336 were isolated. The PgsBCA enzyme complex synthesized PGA in an amidoligation-like manner. The structure and function of the enzyme complex are also discussed.

Journal

VITAMINS

VITAMINS 79 (2), 71-78, 2005

THE VITAMIN SOCIETY OF JAPAN

Keywords

Details 詳細情報について

Export

Report a problem