title: Leukotriene A4 hydrolase is a zinc-containing aminopeptidase.
abstract: A comparison of amino acid sequences revealed that leukotriene A4 (LTA4) hydrolase is homologous to various types of aminopeptidases. Consistently with the finding, the purified LTA4 hydrolases from both human and guinea pig sources contained equimolar zinc ion, as determined by atomic absorption spectrometry. The enzyme had a significant amount of aminopeptidase activity toward synthetic peptide substrates. Both LTA4 hydrolase and aminopeptidase activities were inhibited by o-phenanthroline, p-chloromercuribenzoic acid, and Leu-thiol with similar IC50 values. Co-purification as well as co-immunoprecipitation of both enzyme activities with an affinity-purified antibody against LTA4 hydrolase strongly suggest that the two enzyme activities reside in a single protein.
authors: Department of Physiological Chemistry and Nutrition, Faculty of Medicine, University of Tokyo, Japan.
authors: M
authors: M
authors: Minami
authors: N
authors: N
authors: Ohishi
authors: H
authors: H
authors: Mutoh
authors: T
authors: T
authors: Izumi
authors: H
authors: H
authors: Bito
authors: H
authors: H
authors: Wada
authors: Y
authors: Y
authors: Seyama
authors: H
authors: H
authors: Toh
authors: T
authors: T
authors: Shimizu
mesh_terms: D000626:Aminopeptidases / Q000378:metabolism*; D000818:Animals; D004851:Epoxide Hydrolases / Q000378:metabolism*; D006168:Guinea Pigs; D006801:Humans; D011233:Precipitin Tests; D011994:Recombinant Proteins / Q000378:metabolism; D013054:Spectrophotometry, Atomic; D015032:Zinc / Q000378:metabolism*
chemical_list: D011994:Recombinant Proteins; D004851:Epoxide Hydrolases; D000626:Aminopeptidases; D015032:Zinc; C043134:leukotriene A4 hydrolase