Purification and Characterization of Porcine Skeletal Muscle Aminopeptidase T, a Novel Metallopeptidase Homologous to Leukotriene A<sub>4</sub>Hydrolase

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  • SARKER Mohammed Alamgir
    Graduate School of Biosphere Science, Hiroshima University National Research Institute of Brewing
  • MATSUDA Shinji
    Graduate School of Biosphere Science, Hiroshima University
  • MIZUTANI Osamu
    National Research Institute of Brewing
  • RAO Shengbin
    Graduate School of Biosphere Science, Hiroshima University National Research Institute of Brewing
  • MIGITA Koshiro
    Faculty of Food Science and Technology, Nippon Veterinary and Life Science University
  • GOTO-YAMAMOTO Nami
    Graduate School of Biosphere Science, Hiroshima University National Research Institute of Brewing
  • IEFUJI Haruyuki
    Graduate School of Biosphere Science, Hiroshima University National Research Institute of Brewing
  • NISHIMURA Toshihide
    Faculty of Food Science and Technology, Nippon Veterinary and Life Science University

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  • Purification and Characterization of Porcine Skeletal Muscle Aminopeptidase T, a Novel Metallopeptidase Homologous to Leukotriene A4 Hydrolase

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A novel aminopeptidase, Aminopeptidase T (APase T), was purified from porcine skeletal muscle following successive column chromatography: twice on DEAE-cellulose, hydroxyapatite, and Sephacryl S-200 HR using Leu-β-naphthylamide (LeuNap) as a substrate. The molecular mass of the enzyme was 69 kDa on SDS–PAGE. The optimum pH towards LeuNap of the enzyme was about 7. The enzyme activity was strongly inhibited by bestatin and was negatively affected by ethylenediaminetetraacetic acid (EDTA). Chlorine-activated APase T liberated Leu, Ala, Met, Pro, and Arg from Nap derivatives. The APase T gene consisted of an ORF of 1,836 bp encoding a protein of 611 amino acid residues. The APase T was highly homologous to bovine, human, and mouse Leukotriene A4 hydrolase (LTA4H), a bifunctional enzyme which exhibits APase and epoxide hydrolase activity.

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