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Part of the book series: Springer Handbook of Enzymes ((HDBKENZYMES))

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Nomenclature

EC number

 2.3.1.190

Systematic name

 acetyl-CoA:acetoin O-acetyltransferase

Recommended name

 acetoin dehydrogenase

Synonyms

 AcoA <7> [4]

 AcoB <8> [4]

 Ao:DCPIP OR <2> [1]

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References

  1. Oppermann, F.B.; Schmidt, B.; Steinbuchel, A.: Purification and characterization of acetoin:2,6-dichlorophenolindophenol oxidoreductase, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase of the Pelobacter carbinolicus acetoin dehydrogenase enzyme system. J. Bacteriol., 173, 757-767 (1991)

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  2. Lorenzl, H.; Oppermann, F.; Schmidt, B.; Steinbuchel, A.: Purification and characterization of the E1 component of the Clostridium magnum acetoin dehydrogenase enzyme system. Antonie van Leeuwenhoek, 64, 9-15 (1993)

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  3. Payne, K.A.; Hough, D.W.; Danson, M.J.: Discovery of a putative acetoin dehydrogenase complex in the hyperthermophilic archaeon Sulfolobus solfataricus. FEBS Lett., 584, 1231-1234 (2010)

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  4. Huang, M.; Oppermann, F.B.; Steinbuechel, A.: Molecular characterization of the Pseudomonas putida 2,3-butanediol catabolic pathway. FEMS Microbiol. Lett., 124, 141-150 (1994)

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  5. Priefert, H.; Hein, S.; Krueger, N.; Zeh, K.; Schmidt, B.; Steinbuechel, A.: Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism. J. Bacteriol., 173, 4056-4071 (1991)

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  6. Krueger, N.; Oppermann, F.B.; Lorenzl, H.; Steinbuechel, A.: Biochemical and molecular characterization of the Clostridium magnum acetoin dehydrogenase enzyme system. J. Bacteriol., 176, 3614-3630 (1994)

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  7. Huang, M.; Oppermann-Sanio, F.B.; Steinbuechel, A.: Biochemical and molecular characterization of the Bacillus subtilis acetoin catabolic pathway. J. Bacteriol., 181, 3837-3841 (1999)

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Correspondence to Dietmar Schomburg .

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Schomburg, D., Schomburg, I. (2013). acetoin dehydrogenase 2.3.1.190. In: Schomburg, D., Schomburg, I. (eds) Class 2–3.2 Transferases, Hydrolases. Springer Handbook of Enzymes. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-36240-8_39

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