来自弧菌属T1800的新型耐酒精金属蛋白酶维梅溶素的底物特异性。

Substrate specificity of a novel alcohol resistant metalloproteinase, vimelysin, from Vibrio sp. T1800.

作者信息

Takahashi S, Okayama K, Kunugi S, Oda K

机构信息

Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology, Japan.

出版信息

Biosci Biotechnol Biochem. 1996 Oct;60(10):1651-4. doi: 10.1271/bbb.60.1651.

DOI:10.1271/bbb.60.1651

PMID:8987663

Abstract

Vimelysin is a novel alcohol resistant metalloproteinase from Vibrio sp. T1800. The substrate specificity of vimelysin was studied by using natural and furylacryloyl dipeptide substrates. Vimelysin cleaved mainly Pro7-Phe8 bond and slightly Tyr4-Ile5 bond in human angiotensin I. Vimelysin also cleaved mainly Phe24-Phe25 and Tyr16-Leu17 bonds, and slightly His5-Leu6, His10-Leu11, Ala14-Leu15, and Gly23-Phe24 bonds in oxidized insulin B-chain. The substrate specificity of vimelysin, by using furylacryloyl (Fua) dipeptides were also studied. The ratio of kcat/Km for Fua-Gly-Phe-NH2/Fua-Gly-Leu-NH2, Fua-Phe-Leu-NH2/Fua-Gly-Leu-NH2, and Fua-Phe-Phe-NH2/Fua-Gly-Leu-NH2 were 15.9, 27.8, and 59.0, respectively. These results indicate that vimelysin easily recognizes phenylalanine in P1' positions, which is different from thermolysin.

摘要

维米溶素是一种来自弧菌属T1800的新型耐酒精金属蛋白酶。通过使用天然和呋喃丙烯酰二肽底物研究了维米溶素的底物特异性。维米溶素主要切割人血管紧张素I中的Pro7 - Phe8键，对Tyr4 - Ile5键的切割作用较弱。维米溶素还主要切割氧化胰岛素B链中的Phe24 - Phe25和Tyr16 - Leu17键，对His5 - Leu6、His10 - Leu11、Ala14 - Leu15和Gly23 - Phe24键的切割作用较弱。还研究了使用呋喃丙烯酰（Fua）二肽时维米溶素的底物特异性。Fua - Gly - Phe - NH2/Fua - Gly - Leu - NH2、Fua - Phe - Leu - NH2/Fua - Gly - Leu - NH2和Fua - Phe - Phe - NH2/Fua - Gly - Leu - NH2的kcat/Km比值分别为15.9、27.8和59.0。这些结果表明，维米溶素易于识别P1'位置的苯丙氨酸，这与嗜热菌蛋白酶不同。