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
SMW: SMWW4_v1c11010(pigD)
SRR: SerAS9_1750
SRS: SerAS12_1750
SRA: SerAS13_1751
SERF: L085_23045
SERA: Ser39006_020680
SERQ: CWC46_20685
SERM: CLM71_22595
VGA: BSQ33_00970
PRR: AT705_06595
HCH: HCH_06027
 » 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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