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• W2046509736 abstract "Leukotriene A4 hydrolase in mammals is a bifunctional zinc metalloenzyme that catalyzes the hydrolysis of leukotriene A4 into the proinflammatory mediator leukotriene B4, and also possesses an aminopeptidase activity. Recently we cloned and characterized an leukotriene A4 hydrolase from Saccharomyces cerevisiae as a leucyl aminopeptidase with an epoxide hydrolase activity. Here we show that S. cerevisiae leukotriene A4 hydrolase is a metalloenzyme containing one zinc atom complexed to His-340, His-344, and Glu-363. Mutagenetic analysis indicates that the aminopeptidase activity follows a general base mechanism with Glu-341 and Tyr-429 as the base and proton donor, respectively. Furthermore, the yeast enzyme hydrolyzes leukotriene A4 into three compounds, viz., 5S,6S-dihydroxy-7,9-trans-11,14-cis-eicosatetraenoic acid, leukotriene B4, and Δ6-trans-Δ8-cis-leukotriene B4, with a relative formation of 1:0.2:0.1. In addition, exposure of S. cerevisiae leukotriene A4 hydrolase to leukotriene A4 selectively inactivates the epoxide hydrolase activity with a simultaneous stimulation of the aminopeptidase activity. Moreover, kinetic analyses of wild-type and mutated S. cerevisiae leukotriene A4 hydrolase suggest that leukotriene A4 binds in one catalytic mode and one tight-binding, regulatory mode. Exchange of a Phe-424 in S. cerevisiae leukotriene A4 hydrolase for a Tyr, the corresponding residue in human leukotriene A4 hydrolase, results in a protein that converts leukotriene A4 into leukotriene B4 with an improved efficiency and specificity. Hence, by a single point mutation, we could make the active site better suited to bind and turn over the substrate leukotriene A4, thus mimicking a distinct step in the molecular evolution of S. cerevisiae leukotriene A4 hydrolase toward its mammalian counterparts." @default.
• W2046509736 created "2016-06-24" @default.
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• W2046509736 date "2001-09-27" @default.
• W2046509736 modified "2023-10-14" @default.
• W2046509736 title "<i>Saccharomyces cerevisiae</i> Leukotriene A₄ Hydrolase: Formation of Leukotriene B₄ and Identification of Catalytic Residues" @default.
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• W2046509736 doi "https://doi.org/10.1021/bi011348p" @default.
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