Purification and characterization of leukotriene A4 hydrolase from Xenopus laevis oocytes

FEBS Letters

Strömberg-Kull, Filippa¹  Haeggström, Jesper Z.¹ 

[1] Department of Medical Biochemistry and Biophysics, Division of Chemistry II, Karolinska Institutet, S-171 77 Stockholm, Sweden

关键词: Leukotriene A4 hydrolase;    Leukotriene B4;    Aminopeptidase;    Inflammation;    Xenopus laevis;    LTA4;    leukotriene A4;    5S-trans-5;    6-oxido-7;    9-trans-11;    14-cis-eicosastetraenoic acid;    LTB4;    leukotriene B4;    5S;    12R-dihydroxy-6;    14-cis-8;    10-trans-eicosatetraenoic acid;    Δ 6-trans-Δ 8-cis-LTB4;    5S;    12R-diHETE;    5S;    12R-dihydroxy-6;    10-trans-8;    14-cis-meicosatetraenoic acid;    FPLC;    fast protein liquid chromatography;   

DOI  :  10.1016/S0014-5793(98)00918-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Δ ⁶-trans-Δ ⁸-cis-leukotriene B₄.

【 授权许可】

Unknown