Speaker: Xavi Carpena
IRB Barcelona, IBMB-CSIC

Host

Judith Linacero, PCB

Wednesday, 8 July 2009, 12.00h Aula Fèlix Serratosa

Abstract

The structure of lipoxygenase from Pseudomonas aeruginosa, the first determined from a prokaryote, presents major differences with respect to the well characterized eukaryotic enzymes. An insertion in the catalytic domain of a pair of long antiparallel α-helices contributes to shape a binding pocket containing a complete phospholipid: a phosphatidylethanolamine with branches of 14 and 18 carbons in length, respectively. The specificity towards phospholipids invites to reformulate the roles of lipoxygenases in prokaryotes.

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