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.
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页码：209 / 215
页数：7
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