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Literature summary extracted from

  • Wenzl, M.V.; Beretta, M.; Gorren, A.C.; Zeller, A.; Baral, P.K.; Gruber, K.; Russwurm, M.; Koesling, D.; Schmidt, K.; Mayer, B.
    Role of the general base Glu-268 in nitroglycerin bioactivation and superoxide formation by aldehyde dehydrogenase-2 (2009), J. Biol. Chem., 284, 19878-19886.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.3 C302S the mutation leads to more than 90% loss of all enzyme activities (0.29% residual dehydrogenase activity at pH 9.0 and 0.32% residual dehydrogenase activity at pH 7.5 compared to the wild type enzyme) Homo sapiens
1.2.1.3 E268Q the mutant shows 1.39% residual dehydrogenase activity at pH 9.0 and 0.88% residual dehydrogenase activity at pH 7.5 compared to the wild type enzyme. The mutant exhibits virtually unaffected rates of nitroglycerin denitration despite low dehydrogenase and esterase activities. The mutant exhibits about 50% lower rates of superoxide formation than the wild type enzyme Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.3 Chloral hydrate
-
 Homo sapiens
1.2.1.3 nitroglycerin complete inhibition at 0.05 mM nitroglycerin which can be reversed by the addition of 0.4 mM dithiothreitol Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.2.1.3 mitochondrion
-
 Homo sapiens 5739
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.3 54000
-
 4 * 54000 Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.3 Homo sapiens P05091
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.3 acetaldehyde + NAD+ + H2O
-
 Homo sapiens acetate + NADH + H+
-
 ?
1.2.1.3 formaldehyde + NAD+ + H2O
-
 Homo sapiens formate + NADH + H+
-
 ?
1.2.1.3 additional information ALDH2 denitrates nitroglycerin to 1,2-glyceryl dinitrate and nitrite but also catalyzes reduction of nitroglycerin to NO. In addition to aldehyde oxidation, ALDH2 catalyzes ester hydrolysis. The esterase activity is stimulated by NAD+, but the cofactor is not essential for the reaction Homo sapiens ?
-
 ?
1.2.1.3 additional information the enzyme shows esterase activity with 4-nitrophenyl acetate Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.3 homotetramer 4 * 54000 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.2.1.3 aldehyde dehydrogenase-2
-
 Homo sapiens
1.2.1.3 ALDH2
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.3 NAD+
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
1.2.1.3 physiological function ALDH2 plays an essential role in nitroglycerin bioactivation. ALDH2-catalyzed superoxide formation may essentially contribute to oxidative stress in nitroglycerin-exposed blood vessels Homo sapiens