KEGG   ENZYME: 2.2.1.12
Entry
EC 2.2.1.12                 Enzyme                                 
Name
3-acetyloctanal synthase;
pigD (gene name)
Class
Transferases;
Transferring aldehyde or ketonic groups;
Transketolases and transaldolases
Sysname
pyruvate:(E)-oct-2-enal acetaldehydetransferase (decarboxylating)
Reaction(IUBMB)
pyruvate + (E)-oct-2-enal = (S)-3-acetyloctanal + CO2 [RN:R11141]
Reaction(KEGG)
R11141
Substrate
pyruvate [CPD:C00022];
(E)-oct-2-enal [CPD:C21138]
Product
(S)-3-acetyloctanal [CPD:C21139];
CO2 [CPD:C00011]
Comment
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 alpha,beta-unsaturated carbonyl compounds, including aldehydes and ketones, and can catalyse both 1-2 and 1-4 carboligations depending on the substrate.
History
EC 2.2.1.12 created 2014
Pathway
ec00333  Prodigiosin biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K21428  3-acetyloctanal synthase
Genes
SMWSMWW4_v1c11010(pigD)
SRRSerAS9_1750
SRSSerAS12_1750
SRASerAS13_1751
SERFL085_23045
SERASer39006_020680
SERQCWC46_20685
SERMCLM71_22595
SSURATE40_002220
VGABSQ33_00970
VSRVspart_01681(pigD)
PRRAT705_06595
PXIJ5O05_20775
PVBJ5X90_18225
HCHHCH_06027
HAHEENC22_25960
SMOBJ7W19_06255
 » show all
Reference
1  [PMID:15853884]
  Authors
Williamson NR, Simonsen HT, Ahmed RA, Goldet G, Slater H, Woodley L, Leeper FJ, Salmond GP
  Title
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.
  Journal
Mol Microbiol 56:971-89 (2005)
DOI:10.1111/j.1365-2958.2005.04602.x
  Sequence
Reference
2  [PMID:20669204]
  Authors
Dresen C, Richter M, Pohl M, Ludeke S, Muller M
  Title
The enzymatic asymmetric conjugate umpolung reaction.
  Journal
Angew Chem Int Ed Engl 49:6600-3 (2010)
DOI:10.1002/anie.201000632
Reference
3  [PMID:24957249]
  Authors
Kasparyan E, Richter M, Dresen C, Walter LS, Fuchs G, Leeper FJ, Wacker T, Andrade SL, Kolter G, Pohl M, Muller M
  Title
Asymmetric Stetter reactions catalyzed by thiamine diphosphate-dependent enzymes.
  Journal
Appl Microbiol Biotechnol 98:9681-90 (2014)
DOI:10.1007/s00253-014-5850-0
Other DBs
ExplorEnz - The Enzyme Database: 2.2.1.12
IUBMB Enzyme Nomenclature: 2.2.1.12
ExPASy - ENZYME nomenclature database: 2.2.1.12
BRENDA, the Enzyme Database: 2.2.1.12

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