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Literature summary extracted from

  • Rodriguez-Zavala, J.S.; Weiner, H.
    Structural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation (2002), Biochemistry, 41, 8229-8237.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.3 ALDH-H3tail aldehyde dehydrogenase class 1 with the addition of the C-terminal tail of class 3, KM-value for propionaldehyde is 2.6fold higher than the KM-value of the wild-type enzyme, KM-value for NAD+ is 2fold higher than the KM-value of the wild-type enzyme Homo sapiens
1.2.1.3 ALDH1-5AA aldehyde dehydrogenase class 1 with the addition of five amino acids at the C-terminus, KM-value for propionaldehyde is 67% of the KM-value of the wild-type enzyme, KM-value for NAD+ is 73% of the KM-value of the wild-type enzyme Homo sapiens
1.2.1.3 D80G KM-value for propionaldehyde is 24% of the KM-value of the wild-type enzyme, KM-value for NAD+ is 32% of the KM-value of the wild-type enzyme Homo sapiens
1.2.1.3 D80G/S82A the maximal velocity of the mutant enzyme is 7.5% of the activity of the wild-type enzyme Homo sapiens
1.2.1.3 R84Q KM-value for propionaldehyde is 5.8fold higher than the Km-value of the wild-type enzyme, KM-value for NAD+ is 36% of the KM-value of the wild-type enzyme Homo sapiens
1.2.1.3 S82A KM-value for propionaldehyde is 36% of the KM-value of the wild-type enzyme, KM-value for NAD+ is 15% of the KM-value of the wild-type enzyme Homo sapiens

General Stability

EC Number General Stability Organism
1.2.1.3 half-life of wild-type enzyme and mutant enzyme R84Q in 7 M urea is 10 min, the half-life of the double-mutant enzyme S82A is less than 2 min. At 2 M urea all of the proteins are present as a mixture of native and altered state Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.3 0.0017
-
 NAD+ pH 7.5, 25°C, mutant enzyme S82A Homo sapiens
1.2.1.3 0.0028
-
 propionaldehyde pH 7.5, 25°C, mutant enzyme D80G Homo sapiens
1.2.1.3 0.0035
-
 NAD+ pH 7.5, 25°C, mutant enzyme D80G Homo sapiens
1.2.1.3 0.004
-
 NAD+ pH 7.5, 25°C, mutant enzyme R84Q Homo sapiens
1.2.1.3 0.0044
-
 propionaldehyde pH 7.5, 25°C, mutant enzyme S82A Homo sapiens
1.2.1.3 0.008
-
 NAD+ pH 7.5, 25°C, mutant enzyme ALDH1-5AA Homo sapiens
1.2.1.3 0.008
-
 propionaldehyde pH 7.5, 25°C, mutant enzyme ALDH1-5AA Homo sapiens
1.2.1.3 0.011
-
 NAD+ pH 7.5, 25°C, wild-type enzyme Homo sapiens
1.2.1.3 0.012
-
 propionaldehyde pH 7.5, 25°C, wild-type enzyme Homo sapiens
1.2.1.3 0.022
-
 NAD+ pH 7.5, 25°C, mutant enzyme ALDH1-H3tail Homo sapiens
1.2.1.3 0.031
-
 propionaldehyde pH 7.5, 25°C, mutant enzyme ALDH1-H3tail Homo sapiens
1.2.1.3 0.07
-
 propionaldehyde pH 7.5, 25°C, mutant enzyme R84Q Homo sapiens

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.3
-
 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.3 propionaldehyde + NAD+ + H2O
-
 Homo sapiens propionate + NADH
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.1.3 aldehyde dehydrogenase class 1
-
 Homo sapiens
1.2.1.3 ALDH1
-
 Homo sapiens

Cofactor

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