Acetoin dehydrogenase

Acetoin dehydrogenase (EC 2.3.1.190, acetoin dehydrogenase complex, acetoin dehydrogenase enzyme system, AoDH ES) is an enzyme with systematic name acetyl-CoA:acetoin O-acetyltransferase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

acetoin + CoA + NAD⁺

\rightleftharpoons

This enzyme requires thiamine diphosphate.

References

Priefert H, Hein S, Krüger N, Zeh K, Schmidt B, Steinbüchel A (July 1991). "Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism". Journal of Bacteriology. 173 (13): 4056–71. doi:10.1128/jb.173.13.4056-4071.1991. PMC 208054. PMID 2061286.
Oppermann FB, Steinbüchel A (January 1994). "Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase enzyme system". Journal of Bacteriology. 176 (2): 469–85. doi:10.1128/jb.176.2.469-485.1994. PMC 205071. PMID 8110297.
Krüger N, Oppermann FB, Lorenzl H, Steinbüchel A (June 1994). "Biochemical and molecular characterization of the Clostridium magnum acetoin dehydrogenase enzyme system". Journal of Bacteriology. 176 (12): 3614–30. doi:10.1128/jb.176.12.3614-3630.1994. PMC 205551. PMID 8206840.
Huang M, Oppermann FB, Steinbüchel A (December 1994). "Molecular characterization of the Pseudomonas putida 2,3-butanediol catabolic pathway". FEMS Microbiology Letters. 124 (2): 141–50. doi:10.1111/j.1574-6968.1994.tb07276.x. PMID 7813883.
Huang M, Oppermann-Sanio FB, Steinbüchel A (June 1999). "Biochemical and molecular characterization of the Bacillus subtilis acetoin catabolic pathway". Journal of Bacteriology. 181 (12): 3837–41. PMC 93865. PMID 10368162.

Acetoin+dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH)

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Transferases: acyltransferases (EC 2.3)
2.3.1: other than amino-acyl groups	acetyltransferases: Acetyl-Coenzyme A acetyltransferase N-Acetylglutamate synthase Choline acetyltransferase Dihydrolipoyl transacetylase Acetyl-CoA C-acyltransferase Beta-galactoside transacetylase Chloramphenicol acetyltransferase N-acetyltransferase Serotonin N-acetyl transferase HGSNAT ARD1A Histone acetyltransferase P300/CBP NAT2 palmitoyltransferases: Carnitine O-palmitoyltransferase CPT1 CPT2 Serine C-palmitoyltransferase SPTLC1 SPTLC2 other: Acyltransferase like 2 Aminolevulinic acid synthase Beta-ketoacyl-ACP synthase Glyceronephosphate O-acyltransferase Lecithin—cholesterol acyltransferase Glycerol-3-phosphate O-acyltransferase 1-acylglycerol-3-phosphate O-acyltransferase 2-acylglycerol-3-phosphate O-acyltransferase ABHD5
2.3.2: Aminoacyltransferases	Gamma-glutamyl transpeptidase Peptidyl transferase Transglutaminase Tissue transglutaminase Keratinocyte transglutaminase Factor XIII
2.3.3: converted into alkyl on transfer	Citrate synthase Decylcitrate synthase Citrate (Re)-synthase Decylhomocitrate synthase 2-methylcitrate synthase 2-ethylmalate synthase 3-ethylmalate synthase ATP citrate lyase Malate synthase HMG-CoA synthase HMGCS2 2-hydroxyglutarate synthase 3-propylmalate synthase 2-isopropylmalate synthase Homocitrate synthase Sulfoacetaldehyde acetyltransferase

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)