Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Catalytic Properties of X-Prolyl Dipeptidyl Aminopeptidase from Lactococcus lactis subsp. cremoris nTR
Tsong-Rong YANShih-Ching HoChia-Lung Hou
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1992 Volume 56 Issue 5 Pages 704-707

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Abstract

An X-prolyl dipeptidyl aminopeptidase (X-PDAP ; EC 3.4.14.5) was identified to be loosely bound on the inner cell membrane fraction of Lactococcus lactis subsp. cremoris nTR. The biosynthesis of X-PDAP was continuously increased before the late-log growth phase of the bacteria. Both Gly-Pro-pNA and Ala-Ala-pNA were hydrolyzed by X-PDAP ; the kcat/Km value of the former was about 10-fold that of the latter. The Ki of X-Pro and Pro-X were more specific to X-PDAP than those of X-Ala. The enzyme splitting a dipeptide sequentially from β-casomorphin as a model catalytic pattern was identified and some properties of the enzyme were further characterized.

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