Purification and characterization of leukotriene A4 hydrolase from Xenopus laevis oocytes.
In mammals, leukotriene A4 hydrolase converts leukotriene A4 into the proinflammatory mediator leukotriene B4. We have purified and characterized a non-mammalian leukotriene A4 hydrolase from Xenopus laevis oocytes. This enzyme contains one zinc atom and catalyzes an anion-dependent peptidase activity, two key features of the mammalian enzymes. The amino acid sequence of an internal segment is 60% identical with human leukotriene A4 hydrolase but only 27% identical with rat aminopeptidase B. The Xenopus laevis enzyme is catalytically very efficient and, unlike the human enzyme, converts leukotriene A4 into two enzymatic metabolites, viz. leukotriene B4 and delta6-trans-delta8-cis-leukotriene B4.
Strömberg-Kull
F
F
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Haeggström
J Z
JZ
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004851:Epoxide Hydrolases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008322:Mammals; D008969:Molecular Sequence Data; D009865:Oocytes / Q000201:enzymology*; D010446:Peptide Fragments / Q000737:chemistry; D051381:Rats; D017386:Sequence Homology, Amino Acid; D014982:Xenopus laevis; D015032:Zinc / Q000032:analysis
D010446:Peptide Fragments; D004851:Epoxide Hydrolases; D015032:Zinc; C043134:leukotriene A4 hydrolase