Purification and characterization of leukotriene A 4  hydrolase from  Xenopus laevis  oocytes | Zendy

Strömberg-Kull Filippa | Zendy; Haeggström Jesper Z. | Zendy

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Purification and characterization of leukotriene A 4 hydrolase from Xenopus laevis oocytes

Author(s) -

Strömberg-Kull Filippa,

Haeggström Jesper Z.

Publication year - 1998

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/s0014-5793(98)00918-1

Subject(s) - xenopus , hydrolase , leukotriene , leukotriene b4 , enzyme , leukotriene c4 , biochemistry , leukotriene e4 , leukotriene d4 , aminopeptidase , biology , chemistry , microbiology and biotechnology , stereochemistry , amino acid , inflammation , immunology , gene , leucine , asthma

In mammals, leukotriene A 4 hydrolase converts leukotriene A 4 into the proinflammatory mediator leukotriene B 4 . We have purified and characterized a non‐mammalian leukotriene A 4 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 A 4 hydrolase but only 27% identical with rat aminopeptidase B. The Xenopus laevis enzyme is catalytically very efficient and, unlike the human enzyme, converts leukotriene A 4 into two enzymatic metabolites, viz. leukotriene B 4 and Δ 6 ‐ trans ‐ Δ 8 ‐ cis ‐leukotriene B 4 .

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