Aminopeptidases: structure and function

@article{Taylor1993AminopeptidasesSA,
  title={Aminopeptidases: structure and function},
  author={Allen Taylor},
  journal={The FASEB Journal},
  year={1993},
  volume={7},
  pages={290 - 298}
}
  • A. Taylor
  • Published 1 February 1993
  • Biology, Medicine
  • The FASEB Journal
Aminopeptidases catalyze the cleavage of amino acids from the amino terminus of protein or peptide substrates. They are widely distributed throughout the animal and plant kingdoms and are found in many subcellular organelles, in cytoplasm, and as membrane components. Several aminopeptidases perform essential cellular functions. Many, but not all, of these peptidases are zinc metalloenzymes and are inhibited by the transition‐state analog bestatin. Some are monomeric, and others are assemblies… Expand
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TLDR
This data indicates that the active site in the blLAP is in the carboxyl-terminal one-third of the protomer, which is likely that this photoaffinity label will be useful in identifying active sites in other aminopeptidases as well. Expand
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
The design rationale and synthesis of novel peptidyl diamino thiol inhibitors of rat brain aminopeptidase are presented, along with accompanying structure-activity analysis, and speculations on the possible mode of enzyme-inhibitor binding of bestatin are offered. Expand
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  • Biology, Medicine
  • The Journal of biological chemistry
  • 1989
TLDR
Results suggest that the primary structure of rat kidney aminopeptidase N is established, and only a single gene homologous to KZP DNA is present in the rat and human genomes. Expand
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TLDR
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TLDR
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