AN AMINOPEPTIDASE-P FROM LACTOCOCCUS-LACTIS WITH ORIGINAL SPECIFICITY

被引：27

作者：

MARS, I ^{[1
]}

MONNET, V ^{[1
]}

机构：

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

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS | 1995年 / 1243卷 / 02期

关键词：

AMINOPEPTIDASE P; BRADYKININ; (L-LACTIS);

D O I：

10.1016/0304-4165(94)00028-V

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：

An aminopeptidase P (E.C. 3.4.11.9) that cleaves the Arg-1-Pro-2 bond of bradykinin has been isolated far the first time from Lactococcus lactis. The peptidase was purified to homogeneity in a 3-step procedure and characterized. It is a monomeric metalloenzyme with a 43 kDa molecular mass, activated by Mn2+ and inhibited by DTT. It differs from the majority of aminopeptidases P already described by displaying a specificity for X-Pro-Pro N-termini and probably an extended binding site that could accommodate amino acid residues beyond the P'2 position of the substrate.

引用

页码：209 / 215

页数：7

共 31 条

[1] CLONING AND CHARACTERIZATION OF AN AMINOPEPTIDASE P-ENCODING GENE FROM STREPTOMYCES-LIVIDANS [J].