3fg3 | pdb_00003fg3
Crystal structure of Delta413-417:GS I805W LOX
Structural highlights
FunctionAOSL_PLEHO Bifunctional enzyme which is responsible for allene oxide biosynthesis via a two-step reaction which involves conversion of arachidonic acid to a 8R-hydroperoxide intermediate followed by conversion of the hydroperoxide to allene oxide.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedLipoxygenases (LOX) play pivotal roles in the biosynthesis of leukotrienes and other biologically active eicosanoids derived from arachidonic acid. A mechanistic understanding of substrate recognition, when lipoxygenases that recognize the same substrate generate different products, can be used to help guide the design of enzyme-specific inhibitors. We report here the 1.85 A resolution structure of an 8R-lipoxygenase from Plexaura homomalla, an enzyme with a sequence approximately 40% identical to that of human 5-LOX. The structure reveals a U-shaped channel, defined by invariant amino acids, that would allow substrate access to the catalytic iron. We demonstrate that mutations within the channel significantly impact enzyme activity and propose a novel model for substrate binding potentially applicable to other members of this enzyme family. The 1.85 A structure of an 8R-lipoxygenase suggests a general model for lipoxygenase product specificity.,Neau DB, Gilbert NC, Bartlett SG, Boeglin W, Brash AR, Newcomer ME Biochemistry. 2009 Aug 25;48(33):7906-15. PMID:19594169[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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