IntEnz

EC 1.2.1.10 - Acetaldehyde dehydrogenase (acetylating)

IntEnz Enzyme Nomenclature
EC 1.2.1.10

Names

Reaction

• 23288 [IUBMB]
  acetaldehyde

  acetaldehyde

  Name origin: UniProt - CHECKED (C)

  CHEBI:15343

  Formula: C2H4O
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  +

  CoA

  CoA

  Name origin: UniProt - CHECKED (C)

  CHEBI:57287

  Formula: C21H32N7O16P3S
  Charge: -4

  ChEBI compound status: CHECKED (C)

  

  +

  NAD⁺

  NAD(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:57540

  Formula: C21H26N7O14P2
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

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  acetyl-CoA

  acetyl-CoA

  Name origin: UniProt - CHECKED (C)

  CHEBI:57288

  Formula: C23H34N7O17P3S
  Charge: -4

  ChEBI compound status: CHECKED (C)

  

  +

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  NADH

  NADH

  Name origin: UniProt - CHECKED (C)

  CHEBI:57945

  Formula: C21H27N7O14P2
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

Comments:

Also acts, more slowly, on glycolaldehyde, propanal and butanal. In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.87, propanal dehydrogenase (propanoylating). Involved in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechols. NADP⁺ can replace NAD⁺ but the rate of reaction is much slower [3].

Links to other databases

References

1. Burton, R.M. and Stadtman, E.R.
   The oxidation of acetaldehyde to acetyl coenzyme A.
   J. Biol. Chem. 202: 873-890 (1953). [PMID: 13061511]
2. Smith, L.T. and Kaplan, N.O.
   Purification, properties, and kinetic mechanism of coenzyme A-linked aldehyde dehydrogenase from Clostridium kluyveri.
   Arch. Biochem. Biophys. 203: 663-675 (1980). [PMID: 7458347]
3. Powlowski, J., Sahlman, L. and Shingler, V.
   Purification and properties of the physically associated meta-cleavage pathway enzymes 4-hydroxy-2-ketovalerate aldolase and aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain CF600.
   J. Bacteriol. 175: 377-385 (1993). [PMID: 8419288]
4. Baker, P., Pan, D., Carere, J., Rossi, A., Wang, W., Seah, S. Y.
   Characterization of an aldolase-dehydrogenase complex that exhibits substrate channeling in the polychlorinated biphenyls degradation pathway.
   Biochemistry 48: 6551-6558 (2009). [PMID: 19476337]
5. Baker, P., Hillis, C., Carere, J., Seah, S. Y.
   Protein-protein interactions and substrate channeling in orthologous and chimeric aldolase-dehydrogenase complexes.
   Biochemistry 51: 1942-1952 (2012). [PMID: 22316175]

[EC 1.2.1.10 created 1961, modified 2006, modified 2011]