title: Molecular evolution and zinc ion binding motif of leukotriene A4 hydrolase.
abstract: Leukotriene A4 (LTA4) hydrolase belongs to the aminopeptidase N family. In order to investigate the molecular evolution and physiological significance of LTA4 hydrolase, the enzymes belonging to the family were aligned and a phylogenetic tree was constructed. From the alignment, it was found that three residues involved in zinc binding and one residue of the active sites of aminopeptidases N were conserved in LTA4 hydrolase. In agreement with the observation, LTA4 hydrolase is a zinc protein as determined by atomic absorption spectroscopy.
authors.affiliation: Protein Engineering Research Institute, Osaka, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Toh
authors.forename: M
authors.initials: M
authors.lastname: Minami
authors.forename: T
authors.initials: T
authors.lastname: Shimizu
mesh_terms: D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000235:genetics; D018826:CD13 Antigens; D003001:Cloning, Molecular; D004851:Epoxide Hydrolases / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D008667:Metalloproteins / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D010802:Phylogeny; D015032:Zinc / Q000378:metabolism*
chemical_list: D008667:Metalloproteins; D004851:Epoxide Hydrolases; D000626:Aminopeptidases; D018826:CD13 Antigens; D015032:Zinc; C043134:leukotriene A4 hydrolase