Hydrolysis of Synthetic Substrate, L-Pyroglutamyl p-Nitroanilide is Catalyzed Solely by Pyroglutamyl Aminopeptidase 1 in Rat Liver Cytosol

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  • Abe Koji
    Pharmacokinetics and Drug Delivery Research Laboratories, Sankyo Co., Ltd.
  • Watanabe Nobuaki
    Pharmacokinetics and Drug Delivery Research Laboratories, Sankyo Co., Ltd.
  • Kosaka Toshiyuki
    Biomedical Research Laboratories, Sankyo Co., Ltd.
  • Yamada Makiko
    Pharmacokinetics and Drug Delivery Research Laboratories, Sankyo Co., Ltd.
  • Tokui Taro
    Pharmacokinetics and Drug Delivery Research Laboratories, Sankyo Co., Ltd.
  • Ikeda Toshihiko
    Pharmacokinetics and Drug Delivery Research Laboratories, Sankyo Co., Ltd.

書誌事項

タイトル別名
  • Hydrolysis of Synthetic Substrate, <small>L</small>-Pyroglutamyl <i>p</i>-Nitroanilide is Catalyzed Solely by Pyroglutamyl Aminopeptidase I in Rat Liver Cytosol
  • Hydrolysis of synthetic substrate, L-pyroglutamyl p-nitroanilide is catalyzed solely by pyroglutamyl aminopeptidase I in rat liver cytosol

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説明

Pyroglutamyl aminopeptidase I (PAP-I) is a cytosolic cysteine peptidase, which hydrolytically removes the L-pyroglutamate residue from the amino terminus of endogenous proteins and peptides. L-Pyroglutamyl p-nitroanilide serves as the synthetic substrate of this enzyme, while there is a possibility of other hydrolases being involved in the hydrolysis of this xenobiotic substrate. We cloned a full-length cDNA encoding rat PAP-I from a rat liver cDNA library and expressed this cDNA in Escherichia coli to obtain a recombinant PAP-I as a single protein. The cDNA encoded a sequence of 209 amino acids with a calculated molecular weight of 22913 Da. The homology of the deduced amino acid sequence of rat PAP-I was 98.6 and 94.3% to mouse and human PAP-Is, respectively. The biochemical properties of the recombinant rat PAP-I were almost identical to those of the recombinant mouse and human PAP-Is and the purified rat liver cytosolic PAP-I in terms of the molecular weight, subunit structure, affinity to the substrate, inhibitor profile and pH optimum. Immunoblot analysis using an antibody raised against recombinant rat PAP-I showed that rat PAP-I is present almost exclusively in the cytosolic fraction of the rat liver. Moreover, the hydrolyzing activity for L-pyroglutamyl p-nitroanilide in rat liver cytosolic fraction was completely inhibited by the antibody, strongly suggesting that this xenobiotic substrate is hydrolyzed solely by PAP-I.

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