EC - 3-acetyloctanal synthase

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IntEnz Enzyme Nomenclature


Accepted name:
3-acetyloctanal synthase
Other name:
pigD (gene name)
Systematic name:
pyruvate:(E)-oct-2-enal acetaldehydetransferase (decarboxylating)




Requires thiamine diphosphate. The enzyme, characterized from the bacterium Serratia marcescens, participates in the biosynthesis of the antibiotic prodigiosin. The enzyme decarboxylates pyruvate, followed by attack of the resulting two-carbon fragment on (E)-oct-2-enal, resulting in a Stetter reaction. In vitro the enzyme can act on a number of α,β-unsaturated carbonyl compounds, including aldehydes and ketones, and can catalyse both 1-2 and 1-4 carboligations depending on the substrate.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB


  1. Williamson, N. R., Simonsen, H. T., Ahmed, R. A., Goldet, G., Slater, H., Woodley, L., Leeper, F. J., Salmond, G. P.
    Biosynthesis of the red antibiotic, prodigiosin, in Serratia: identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces.
    Mol. Microbiol. 56: 971-989 (2005). [PMID: 15853884]
  2. Dresen, C., Richter, M., Pohl, M., Ludeke, S., Muller, M.
    The enzymatic asymmetric conjugate umpolung reaction.
    Angew. Chem. Int. Ed. Engl. 49: 6600-6603 (2010). [PMID: 20669204]
  3. Kasparyan, E., Richter, M., Dresen, C., Walter, L. S., Fuchs, G., Leeper, F. J., Wacker, T., Andrade, S. L., Kolter, G., Pohl, M., Muller, M.
    Asymmetric Stetter reactions catalyzed by thiamine diphosphate-dependent enzymes.
    Appl. Microbiol. Biotechnol. 98: 9681-9690 (2014). [PMID: 24957249]

[EC created 2014]