The active site of carboxypeptidase Taq possesses the active-site motif His-Glu-X-X-His of zinc-dependent endopeptidases and aminopeptidases |
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| Authors: | Lee Sang-Hyeon; Taguchi Hayao; Yoshimura Etsuro; Minagawa Etsuo; Kaminogawa Shuichi; Hiroshi M; Ohta Takahisa |
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| Affiliation: | Department of Agricultural Chemistry, The University of Tokyo 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113
1Department of Applied Biological Science,Science University of Tokyo Noda, Chiba 278
2Research Center, Yotsuba Milk Product Co. Ltd Wattsu, Hiroshima-cho, Sapporo-gun, Hokkaido 061-12
3Department of Applied Chemistry, Kogakuin University Nishiswinjuku, Shinjuku-ku, Tokyo 163-91, Japan |
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| Abstract: | Carboxypeptidase (CPase) Taq possesses the His–Glu–X–X–Hissequence, which is the consensus sequence in the active siteof zinc-dependent endopeptidases and amino-peptidases, at positions276–280. Amino acid replacement of the conserved His andGlu drastically diminished the activity of CPase Taq, and thezinc content of the enzyme was also greatly reduced when eitherof the two His residues was replaced with Arg or Tyr. The resultsindicate that this sequence actually functions as the activesite in CPase Taq, showing that CPase Taq is a novel type ofzinc-dependent CPase that possesses the His–Glu–X–X–Hisactive-site motif. |
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| Keywords: | active site// carboxypeptidase// extreme thermophile// metalloenzyme// thermostable enzyme |
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