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Literature summary extracted from

  • Bchini, R.; Vasiliou, V.; Branlant, G.; Talfournier, F.; Rahuel-Clermont, S.
    Retinoic acid biosynthesis catalyzed by retinal dehydrogenases relies on a rate-limiting conformational transition associated with substrate recognition (2013), Chem. Biol. Interact., 202, 78-84 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.36 gene ALDH1A1, recombinant expression of N-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain C41(DE3) Homo sapiens
1.2.1.36 gene ALDH1A2, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain C41(DE3) Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.36 K127A site-directed mutagenesis, the mutant shows reduced activity with retinoic acid compared to the wild-type enzyme Homo sapiens
1.2.1.36 N120A site-directed mutagenesis, the mutant shows reduced activity with retinoic acid compared to the wild-type enzyme Homo sapiens
1.2.1.36 Y296A site-directed mutagenesis, the mutant shows reduced activity with retinoic acid compared to the wild-type enzyme Homo sapiens
1.2.1.36 Y296V site-directed mutagenesis, the mutant shows reduced activity with retinoic acid compared to the wild-type enzyme Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.36 additional information
-
 additional information Michaelis-Menten kinetics and pre-steady-state kinetics Rattus norvegicus
1.2.1.36 additional information
-
 additional information Michaelis-Menten kinetics and pre-steady-state kinetics Homo sapiens
1.2.1.36 0.002
-
 all-trans-retinal pH 8.5, 25°C, recombinant enzyme Rattus norvegicus
1.2.1.36 0.0029
-
 citral pH 8.5, 25°C, recombinant enzyme Rattus norvegicus
1.2.1.36 0.0063
-
 2,4-decadienal pH 8.5, 25°C, recombinant enzyme Rattus norvegicus
1.2.1.36 0.0064
-
 decanal pH 8.5, 25°C, recombinant enzyme Rattus norvegicus
1.2.1.36 0.0081
-
 all-trans-retinal pH 8.5, 25°C, recombinant wild-type ALDH1A1 enzyme Homo sapiens
1.2.1.36 0.0086
-
 all-trans-retinal pH 8.5, 25°C, recombinant mutant K127A Homo sapiens
1.2.1.36 0.0089
-
 all-trans-retinal pH 8.5, 25°C, recombinant mutant Y296A Homo sapiens
1.2.1.36 0.01
-
 decanal pH 8.5, 25°C, recombinant wild-type ALDH1A1 enzyme Homo sapiens
1.2.1.36 0.011
-
 all-trans-retinal pH 8.5, 25°C, recombinant mutant N120A Homo sapiens
1.2.1.36 0.015
-
 all-trans-retinal pH 8.5, 25°C, recombinant mutant Y296V Homo sapiens
1.2.1.36 0.023
-
 hexanal pH 8.5, 25°C, recombinant enzyme Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.36 all-trans-retinal + NAD+ + H2O Rattus norvegicus
-
 all-trans-retinoate + NADH + 2 H+
-
 ?
1.2.1.36 all-trans-retinal + NAD+ + H2O Homo sapiens
-
 all-trans-retinoate + NADH + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.36 Homo sapiens P00352
-
-
1.2.1.36 Rattus norvegicus Q63639
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.36 recombinant N-terminally His-tagged enzyme from Escherichia coli strain C41(DE3) by nickel affinity chromatography Rattus norvegicus
1.2.1.36 recombinant N-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain C41(DE3) by nickel affinityy chromatography Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.1.36 liver
-
 Rattus norvegicus
-
1.2.1.36 liver
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.36 2,4-decadienal + NAD+ + H2O
-
 Rattus norvegicus 2,4-decadienoate + NADH + 2 H+
-
 ?
1.2.1.36 all-trans-retinal + NAD+ + H2O
-
 Rattus norvegicus all-trans-retinoate + NADH + 2 H+
-
 ?
1.2.1.36 all-trans-retinal + NAD+ + H2O
-
 Homo sapiens all-trans-retinoate + NADH + 2 H+
-
 ?
1.2.1.36 citral + NAD+ + H2O
-
 Rattus norvegicus 3,7-dimethyl-2,6-octadienoate + NADH + 2 H+
-
 ?
1.2.1.36 decanal + NAD+ + H2O
-
 Rattus norvegicus decanoate + NADH + 2 H+
-
 ?
1.2.1.36 decanal + NAD+ + H2O
-
 Homo sapiens decanoate + NADH + 2 H+
-
 ?
1.2.1.36 hexanal + NAD+ + H2O
-
 Rattus norvegicus hexanoate + NADH + 2 H+
-
 ?
1.2.1.36 additional information molecular basis of retinal recognition, comparison of enzyme from Rattus and human, overview. In contrast to long chain unsaturated substrates, the rate-limiting step of retinal oxidation by RALDHs is associated with acylation. Retinal recognition occurs in two steps: binding into the substrate access channel, and a slower structural reorganization with a rate constant of the same magnitude. The conformational transition of the RALDH-retinal complex significantly contributes to the rate-limiting step that controls the kinetics of retinal oxidation, as a prerequisite for the formation of a catalytically competent Michaelis complex. The conclusion is consistent with the general notion that structural flexibility within the active site of ALDH enzymes has been shown to be an integral component of catalysis. No activity with 2,4-decadienal, citral, and hexanal Homo sapiens ?
-
 ?
1.2.1.36 additional information molecular basis of retinal recognition,comparison of enzyme from Rattus and human, overview. In contrast to long chain unsaturated substrates, the rate-limiting step of retinal oxidation by RALDHs is associated with acylation. Retinal recognition occurs in two steps: binding into the substrate access channel, and a slower structural reorganization with a rate constant of the same magnitude. The conformational transition of the RALDH-retinal complex significantly contributes to the rate-limiting step that controls the kinetics of retinal oxidation, as a prerequisite for the formation of a catalytically competent Michaelis complex. The conclusion is consistent with the general notion that structural flexibility within the active site of ALDH enzymes has been shown to be an integral component of catalysis Rattus norvegicus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.1.36 ALDH1A1
-
 Homo sapiens
1.2.1.36 Aldh1a2
-
 Rattus norvegicus
1.2.1.36 NAD-dependent retinal dehydrogenases
-
 Rattus norvegicus
1.2.1.36 NAD-dependent retinal dehydrogenases
-
 Homo sapiens
1.2.1.36 RALDH
-
 Rattus norvegicus
1.2.1.36 RALDH
-
 Homo sapiens
1.2.1.36 RalDH1
-
 Homo sapiens
1.2.1.36 RALDH2
-
 Rattus norvegicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.36 25
-
 assay at Rattus norvegicus
1.2.1.36 25
-
 assay at Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.36 0.008
-
 all-trans-retinal pH 8.5, 25°C, recombinant mutant Y296V Homo sapiens
1.2.1.36 0.017
-
 all-trans-retinal pH 8.5, 25°C, recombinant mutant Y296A Homo sapiens
1.2.1.36 0.03
-
 all-trans-retinal pH 8.5, 25°C, recombinant mutant K127A Homo sapiens
1.2.1.36 0.03
-
 all-trans-retinal pH 8.5, 25°C, recombinant mutant N120A Homo sapiens
1.2.1.36 0.07
-
 all-trans-retinal pH 8.5, 25°C, recombinant enzyme Homo sapiens
1.2.1.36 0.1
-
 all-trans-retinal pH 8.5, 25°C, recombinant enzyme Rattus norvegicus
1.2.1.36 0.1
-
 citral pH 8.5, 25°C, recombinant enzyme Rattus norvegicus
1.2.1.36 0.15
-
 2,4-decadienal pH 8.5, 25°C, recombinant enzyme Rattus norvegicus
1.2.1.36 1
-
 decanal pH 8.5, 25°C, recombinant enzyme Homo sapiens
1.2.1.36 2
-
 hexanal pH 8.5, 25°C, recombinant enzyme Rattus norvegicus
1.2.1.36 2.2
-
 decanal pH 8.5, 25°C, recombinant enzyme Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.36 8.5
-
 assay at Rattus norvegicus
1.2.1.36 8.5
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.36 NAD+
-
 Rattus norvegicus
1.2.1.36 NAD+
-
 Homo sapiens