IDENTIFICATION OF THE ACTIVE-SITE SERINE OF THE X-PROLYL DIPEPTIDYL AMINOPEPTIDASE FROM LACTOCOCCUS-LACTIS

被引：32

作者：

CHICH, JF

CHAPOTCHARTIER, MP

RIBADEAUDUMAS, B

GRIPON, JC ^{[1
]}

机构：

[1] INRA,RECH LAITIERES STN,UNITE ENZYMOL,F-78352 JOUY EN JOSAS,FRANCE

[2] INRA,RECH LAITIERES STN,UNITE PROT,F-78352 JOUY EN JOSAS,FRANCE

来源：

FEBS LETTERS | 1992年 / 314卷 / 02期

关键词：

X-PROLYL DIPEPTIDYL AMINOPEPTIDASE; SERINE PROTEASE; ACTIVE SITE; DIISOPROPYLFLUOROPHOSPHATE; LACTOCOCCUS-LACTIS;

D O I：

10.1016/0014-5793(92)80960-O

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The active site serine of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis (PepX) was identified. The enzyme was labeled by [H-3]DFP, treated by CNBr and the resulting peptides were separated by reverse-phase-HPLC. The main radiolabeled peptide was sequenced. Ser-348, in the following sequence, Gly-Lys-Ser-Tyr-Leu-Gly, was identified as the active site serine. A sequence comparison between the active site of PepX and other serine proteases was made, showing only limited sequence homologies in this area. The consensus sequence surrounding the active site serine in the three known X-prolyl dipeptidyl aminopeptidases (mammalian DPPIV, yeast DPAB and PepX) is G-X-S-Y-X-G, where X is a non-conserved amino acid.

引用

页码：139 / 142

页数：4

共 18 条

[1] SERINE CARBOXYPEPTIDASES - A REVIEW [J].