Mutagenic definition of a papain-like catalytic triad, sufficiency of the N-terminal domain for single-site core catalytic enzyme acylation, and C-terminal domain for augmentative metal activation of a eukaryotic phytochelatin synthase.

@article{Romanyuk2006MutagenicDO,
  title={Mutagenic definition of a papain-like catalytic triad, sufficiency of the N-terminal domain for single-site core catalytic enzyme acylation, and C-terminal domain for augmentative metal activation of a eukaryotic phytochelatin synthase.},
  author={Nataliya D Romanyuk and Daniel J. Rigden and Olena K. Vatamaniuk and Albert Lang and Rebecca E Cahoon and Joseph M Jez and Philip A. Rea},
  journal={Plant physiology},
  year={2006},
  volume={141 3},
  pages={858-69}
}
Phytochelatin (PC) synthases are gamma-glutamylcysteine (gamma-Glu-Cys) dipeptidyl transpeptidases that catalyze the synthesis of heavy metal-binding PCs, (gamma-Glu-Cys)nGly polymers, from glutathione (GSH) and/or shorter chain PCs. Here it is shown through investigations of the enzyme from Arabidopsis (Arabidopsis thaliana; AtPCS1) that, although the N-terminal half of the protein, alone, is sufficient for core catalysis through the formation of a single-site enzyme acyl intermediate, it is… CONTINUE READING
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MEROPS : the peptidase database

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