EC number:2.2.1.12

Enzyme

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     2. Transferases
        2.2 Transferring aldehyde or ketonic groups
            2.2.1 Transketolases and transaldolases
ID:2.2.1.12
Description:3-acetyloctanal synthase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.2.1.12
BRENDA Enzyme Link: BRENDA 2.2.1.12
KEGG Enzyme Link: KEGG2.2.1.12
BioCyc Enzyme Link: BioCyc 2.2.1.12
ExPASy Enzyme Link: ExPASy2.2.1.12
EC2PDB Enzyme Link: EC2PDB 2.2.1.12
ExplorEnz Enzyme Link: ExplorEnz 2.2.1.12
PRIAM enzyme-specific profiles Link: PRIAM 2.2.1.12
IntEnz Enzyme Link: IntEnz 2.2.1.12
MEDLINE Enzyme Link: MEDLINE 2.2.1.12

EC number:2.2.1.12

MSA:

2.2.1.12;
Phylogenetic Tree:

2.2.1.12;
Uniprot:
M-CSA:
RHEA:42832 (2E)-octenal + H(+) + pyruvate = (S)-3-acetyloctanal + CO2
RULE(radius=1) [*:1]-[CH;+0:2]=[CH;+0:3]-[*:4].[*:5]=[C;H0;+0:6](-[OH;+0:7])-[C;H0;+0:8](=[*:9])-[*:10].[H+;H0:11]>>[*:9]=[C;H0;+0:8](-[*:10])-[CH;+0:3](-[*:4])-[CH2;+0:2]-[*:1].[*:5]=[C;H0;+0:6]=[O;H0;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Asymmetric Stetter reactions catalyzed by thiamine diphosphate-dependent enzymes.Kasparyan E, Richter M, Dresen C, Walter LS, Fuchs G, Leeper FJ, Wacker T, Andrade SL, Kolter G, Pohl M, Müller M2014 Dec24957249
The enzymatic asymmetric conjugate umpolung reaction.Dresen C, Richter M, Pohl M, Lüdeke S, Müller M2010 Sep 320669204
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.Williamson NR, Simonsen HT, Ahmed RA, Goldet G, Slater H, Woodley L, Leeper FJ, Salmond GP2005 May15853884