Catalytic properties of X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis subsp. cremoris nTR.

Article abstract of DOI:10.1271/bbb.56.704

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 beta-casomorphin as a model catalytic pattern was identified and some properties of the enzyme were further characterized.

Full text of DOI:10.1271/bbb.56.704

Bioscience, Biotechnology, and Biochemistry
ISSN: 0916-8451 (Print) 1347-6947 (Online) Journal homepage: http://www.tandfonline.com/loi/tbbb20
Catalytic Properties of X-Prolyl Dipeptidyl
Aminopeptidase from Lactococcus lactis subsp.
cremoris nTR
Tsong-Rong Yan, Shih-Ching Ho & Chia-Lung Hou
To cite this article: Tsong-Rong Yan, Shih-Ching Ho & Chia-Lung Hou (1992) Catalytic Properties
of X-Prolyl Dipeptidyl Aminopeptidase from Lactococcus lactis subsp. cremoris nTR, Bioscience,
Biotechnology, and Biochemistry, 56:5, 704-707, DOI: 10.1271/bbb.56.704
To link to this article: http://dx.doi.org/10.1271/bbb.56.704
Published online: 12 Jun 2014.
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