Amino-acid sequence and tissue distribution of guinea-pig leukotriene A4 hydrolase.
The guinea-pig leukotriene A4 hydrolase (LTA4H)-encoding cDNA was isolated from a guinea-pig lung cDNA library by cross-hybridization using a human probe. The deduced amino acid (aa) sequence consists of 611 aa (68 756 Da) and contains all twelve internal peptide and N-terminal sequences determined from the purified enzyme from guinea-pig intestine. The aa identity of the guinea-pig enzyme with its human, mouse and rat counterparts was 92.9, 90.5 and 90.4%, respectively. The previously characterized zinc-binding motif and a putative active site were highly conserved, supporting the aminopeptidase activity described for this enzyme. RNA blot analysis demonstrated ubiquitous expression of the LTA4H mRNA.
Minami
M
M
Department of Biochemistry, Faculty of Medicine, University of Tokyo, Japan.
Mutoh
H
H
Ohishi
N
N
Honda
Z
Z
Bito
H
H
Shimizu
T
T
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D015342:DNA Probes; D018076:DNA, Complementary / Q000235:genetics; D004851:Epoxide Hydrolases / Q000235:genetics*; D006168:Guinea Pigs; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D051381:Rats; D013045:Species Specificity; D014018:Tissue Distribution
D015342:DNA Probes; D018076:DNA, Complementary; D012333:RNA, Messenger; D004851:Epoxide Hydrolases; C043134:leukotriene A4 hydrolase