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An aminopeptidase P from Lactococcus lactis with original specificity.

作者信息

Mars I, Monnet V

机构信息

Station de Recherches Laitières, I.N.R.A., Jouy en Josas, France.

出版信息

Biochim Biophys Acta. 1995 Feb 23;1243(2):209-15. doi: 10.1016/0304-4165(94)00028-v.

DOI:10.1016/0304-4165(94)00028-v
PMID:7873564
Abstract

An aminopeptidase P (E.C. 3.4.11.9) that cleaves the Arg-1-Pro-2 bond of bradykinin has been isolated for 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-terminal and probably an extended binding site that could accommodate amino acid residues beyond the P'2 position of the substrate.

摘要

相似文献

1
An aminopeptidase P from Lactococcus lactis with original specificity.
Biochim Biophys Acta. 1995 Feb 23;1243(2):209-15. doi: 10.1016/0304-4165(94)00028-v.
2
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Degradation and debittering of a tryptic digest from beta-casein by aminopeptidase N from Lactococcus lactis subsp. cremoris Wg2.乳酸乳球菌乳脂亚种Wg2来源的氨肽酶N对β-酪蛋白胰蛋白酶消化物的降解和脱苦
Appl Environ Microbiol. 1993 May;59(5):1430-6. doi: 10.1128/aem.59.5.1430-1436.1993.

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4
Genetic characterization of pepP, which encodes an aminopeptidase P whose deficiency does not affect Lactococcus lactis growth in milk, unlike deficiency of the X-prolyl dipeptidyl aminopeptidase.pepP的遗传特征分析，pepP编码一种氨肽酶P，与X-脯氨酰二肽基氨肽酶缺乏不同，其缺乏并不影响乳酸乳球菌在牛奶中的生长。
Appl Environ Microbiol. 1998 Nov;64(11):4591-5. doi: 10.1128/AEM.64.11.4591-4595.1998.
5
The proteolytic systems of lactic acid bacteria.乳酸菌的蛋白水解系统。
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