aminopeptidase love

Definitions

from The American Heritage® Dictionary of the English Language, 4th Edition

  • n. Any of various enzymes that catalyze the hydrolysis of the terminal peptide bond at the amino end of a polypeptide.

from Wiktionary, Creative Commons Attribution/Share-Alike License

  • n. Any of several enzymes that catalyze the hydrolysis of the peptide bond of the terminal amino acid at the amino end of a polypeptide or protein

Etymologies

Sorry, no etymologies found.

Examples

  • During experiments, Wendy Peer, a research assistant professor of horticulture, found that inserting a similar protein found in humans, called insulin responsive aminopeptidase, or IRAP, also rescued the plants.

    PhysOrg.com - latest science and technology news stories

  • The aminopeptidase M1 protein, or APM1, is critical for root development in plants.

    PhysOrg.com - latest science and technology news stories

  • The new investigation was conducted using the aminopeptidase M1 protein (APM1), usually found in plants, and a similar, human protein, called insulin responsive aminopeptidase, or IRAP, PhysOrg reports.

    Softpedia News - Global

  • M1 aminopeptidase activity is such a fundamental process that it's been conserved evolutionarily.

    Softpedia News - Global

  • Gluzman I, Goldberg DE (2004) A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation.

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  • Two of them, coding for a cadherin and a leucine aminopeptidase, were further examined at the sequence and gene expression levels.

    BioMed Central - Latest articles

  • Specific inhibitors of dipeptidyl peptidase IV, kallikrein, and aminopeptidase P prevented the production of NPY3-36, NPY3-35, and NPY

    Journal of Biological Chemistry current issue

  • Kirshenbaum AS, Goff JP, Semere T, Foster B, Scott LM, et al. (1999) Demonstration that human mast cells arise from a progenitor cell population that is CD34 (+), c-kit (+), and expresses aminopeptidase N (CD13).

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  • ERAP1 has been characterized before as a leucine aminopeptidase because it preferably degrades dipeptide fluorigenic substrates that have a leucine at their N-terminus

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  • Such specificity effects originating from side-chains distal from the scissile N-terminal peptide bond are, to our knowledge and up to date, unique to this aminopeptidase and have only been partially observed before as differential substrate specificity depending on the C-terminus of an unrelated series of peptides

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