Purification and properties of an exocellular .GAMMA.-glutamyl arylamidase from Bacillus sp. strain No. 12.

スポンサーリンク

概要

• 論文の詳細を見る

• An exocellular γ-glutamyl arylamide-hydrolyzing enzyme was produced by a Bacillus sp. in L-glutamate-containing medium. This enzyme was a tetrameric simple protein composed of two heavy subunits (Mr 56, 000) and two light subunits (Mr 46, 000). It hydrolyzed γ-amido, acyl and aryl bonds in L- and D-glutamyl compounds, and the activity on L-glutamic acid γ-p-nitroanilide was inhibited by the addition of glutamate and γ-glutamyl compounds but not by α-glutamyl compounds. The activity was stimulated by various dipeptides but not by free amino acids. L-Alanine, glycine, L-serine and L-cysteine inhibited the enzyme competitively. Addition of hydroxylamine had no effect on the activity.

• 公益社団法人 日本農芸化学会の論文

著者

• HWANG Se

  Institute of Applied Microbiology, The University of Tokyo

関連論文

• Distribution of Highly Specific Arylamidase Activities in Bacteria
• Purification and properties of an exocellular .GAMMA.-glutamyl arylamidase from Bacillus sp. strain No. 12.

スポンサーリンク