3-deoxy-8-phosphooctulonate synthase () is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme first characterised from Pseudomonas aeruginosa are phosphoenolpyruvate, D-arabinose 5-phosphate, and water. Its products are 3-deoxy-α-D-manno-2-octulosonic acid 8-phosphate (3-deoxy-8-phosphooctulonic acid) and orthophosphate (Pi). The enzyme isolated from Helicobacter pylori was shown to be a zinc-containing metalloprotein. Its crystal structure has been determined.
Nomenclature This enzyme is a transferase, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is phosphoenolpyruvate:D-arabinose-5-phosphate C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming). Other names in common use include 2-dehydro-3-deoxy-D-octonate-8-phosphate, D-arabinose-5-phosphate-lyase (pyruvate-phosphorylating), 2-dehydro-3-deoxy-phosphooctonate aldolase, 2-keto-3-deoxy-8-phosphooctonic synthetase, 3-deoxy-D-manno-octulosonate-8-phosphate synthase, 3-deoxy-D-mannooctulosonate-8-phosphate synthetase, 3-deoxyoctulosonic 8-phosphate synthetase, KDOP synthase, and phospho-2-keto-3-deoxyoctonate aldolase. It is part of the pathway to nucleotide sugars.
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