Substrate Specificity of a Tripeptidase as a Metalloenzyme Purified from Lactococcus lactis subsp. lactis biovar. diacetylactis ATCC 13675
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概要
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The peptidase purified to homogeneity from Lactococcus lactis subsp. lactis biovar. diacetylactis ATCC 13675 was considered to be an aminotripeptidase (EC 3.4.11.4) from the results of substrate specificity. The K_m value showed a tendency to decrease with the number of alanine residues, but to increase with the number of glycine residues in the substrate tripeptide. The effects of divalent metal ions on enzyme activity were considerably different depending on the tripeptide used as a substrate. In the case of Mn^<2+>, Co^<2+>, Ni^<2+>, Cu^<2+>, Zn^<2+>and Cd^<2+>, there was apparent correlation between enzyme activities observed in the presence of metal ions and following metal ion replacement. The Zn^<2+>-enzyme showed almost the same K_m and k_<cat> values as the native enzyme, suggesting the enzyme to be a zinc metallopeptidase. The K_m of the divalent metal-re-placed enzyme increased in the order of Co^<2+>, Zn^<2+>, and Mn^<2+>. As a result of replacement with Co^<2+> an enzyme having 2.3-fold higher activity compared to the native enzyme for GGF as a substrate was obtained. Thus, the change in substrate specificity observed following metal replacement may suggest a highly specific interaction between the enzyme, metal and substrate, leading to the activity expression and stability of the tripeptidase.
- 公益社団法人日本生物工学会の論文
- 2002-04-25
著者
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KASUMI Takafumi
National Food Research Institute
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MORI Sumiko
National Food Research Institute
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SUMINO SHIORI
National Food Research Institute
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