Catalytic Properties of X-Prolyl Dipeptidyl Aminopeptidase from Lactococcus lactis subsp. cremoris nTR
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概要
- 論文の詳細を見る
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 k_<cat>/K_m value of the former was about 10-fold that of the latter. The K_i 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.
- 社団法人日本農芸化学会の論文
- 1992-05-23
著者
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Ho Shih-ching
Department Of Biotechnology The University Of Tokyo
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Ho Shih-ching
Department Of Bioengineering Tatung Institute Of Technology
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YAN Tsong-Rong
Department of Bioengineering, Tatung Institute of Technology
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Hou Chia-Lung
Department of Bioengineering, Tatung Institute of Technology
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Hou Chia-lung
Department Of Bioengineering Tatung Institute Of Technology
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Yan Tsong-rong
Department Of Bioengineering Tatung Institute Of Technology
関連論文
- Identification and Characterization of Porcine NP-190, a Novel Protein That Is Specifically Expressed in the Axonal Membrane during the Embryonic Period^1
- Isolation and Characterization of a 230 kDa Protein(p230) Specifically Expressed in Fetal Brains: Its Involvement in Neurite Outgrowth from Rat Cerebral Cortex Neurons Grown on Monolayer of Astrocytes
- Catalytic Properties of X-Prolyl Dipeptidyl Aminopeptidase from Lactococcus lactis subsp. cremoris nTR
- Isolation and Characterization of a 230 kDa Protein (p230) Specifically Expressed in Fetal Brains: Its Involvement in Neurite Outgrowth from Rat Cerebral Cortex Neurons Grown on Monolayer of Astrocytes.