Journal Article

The active site of carboxypeptidase Taq possesses the active-site motif His–Glu–X–X-His of zinc-dependent endopeptidases and aminopeptidases

Sang-Hyeon Lee, Hayao Taguchi, Etsuro Yoshimura, Etsuo Minagawa, Shuichi Kaminogawa, M Hiroshi and Takahisa Ohta

in Protein Engineering, Design and Selection

Volume 9, issue 6, pages 467-469
Published in print June 1996 | ISSN: 1741-0126
e-ISSN: 1741-0134 | DOI: https://dx.doi.org/10.1093/protein/9.6.467
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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Carboxypeptidase (CPase) Taq possesses the His–Glu–X–X–His sequence, which is the consensus sequence in the active site of zinc-dependent endopeptidases and amino-peptidases, at positions 276–280. Amino acid replacement of the conserved His and Glu drastically diminished the activity of CPase Taq, and the zinc content of the enzyme was also greatly reduced when either of the two His residues was replaced with Arg or Tyr. The results indicate that this sequence actually functions as the active site in CPase Taq, showing that CPase Taq is a novel type of zinc-dependent CPase that possesses the His–Glu–X–X–His active-site motif.

Keywords: active site/; carboxypeptidase/; extreme thermophile/; metalloenzyme/; thermostable enzyme

Journal Article.  0 words. 

Subjects: Proteins

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