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Literature summary for 1.2.1.36 extracted from
- 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 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene ALDH1A1, recombinant expression of N-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain C41(DE3) | Homo sapiens |
| gene ALDH1A2, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain C41(DE3) | Rattus norvegicus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K127A | site-directed mutagenesis, the mutant shows reduced activity with retinoic acid compared to the wild-type enzyme | Homo sapiens |
| N120A | site-directed mutagenesis, the mutant shows reduced activity with retinoic acid compared to the wild-type enzyme | Homo sapiens |
| Y296A | site-directed mutagenesis, the mutant shows reduced activity with retinoic acid compared to the wild-type enzyme | Homo sapiens |
| Y296V | site-directed mutagenesis, the mutant shows reduced activity with retinoic acid compared to the wild-type enzyme | Homo sapiens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics and pre-steady-state kinetics | Rattus norvegicus | |
| additional information | - |
additional information | Michaelis-Menten kinetics and pre-steady-state kinetics | Homo sapiens | |
| 0.002 | - |
all-trans-retinal | pH 8.5, 25°C, recombinant enzyme | Rattus norvegicus |  |
| 0.0029 | - |
citral | pH 8.5, 25°C, recombinant enzyme | Rattus norvegicus | |
| 0.0063 | - |
2,4-decadienal | pH 8.5, 25°C, recombinant enzyme | Rattus norvegicus | |
| 0.0064 | - |
decanal | pH 8.5, 25°C, recombinant enzyme | Rattus norvegicus | |
| 0.0081 | - |
all-trans-retinal | pH 8.5, 25°C, recombinant wild-type ALDH1A1 enzyme | Homo sapiens | |
| 0.0086 | - |
all-trans-retinal | pH 8.5, 25°C, recombinant mutant K127A | Homo sapiens | |
| 0.0089 | - |
all-trans-retinal | pH 8.5, 25°C, recombinant mutant Y296A | Homo sapiens | |
| 0.01 | - |
decanal | pH 8.5, 25°C, recombinant wild-type ALDH1A1 enzyme | Homo sapiens | |
| 0.011 | - |
all-trans-retinal | pH 8.5, 25°C, recombinant mutant N120A | Homo sapiens | |
| 0.015 | - |
all-trans-retinal | pH 8.5, 25°C, recombinant mutant Y296V | Homo sapiens | |
| 0.023 | - |
hexanal | pH 8.5, 25°C, recombinant enzyme | Rattus norvegicus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| all-trans-retinal + NAD+ + H2O | Rattus norvegicus | - |
all-trans-retinoate + NADH + 2 H+ | - |
? | |
| all-trans-retinal + NAD+ + H2O | Homo sapiens | - |
all-trans-retinoate + NADH + 2 H+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P00352 | - |
- |
| Rattus norvegicus | Q63639 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant N-terminally His-tagged enzyme from Escherichia coli strain C41(DE3) by nickel affinity chromatography | Rattus norvegicus |
| recombinant N-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain C41(DE3) by nickel affinityy chromatography | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Rattus norvegicus | - |
| liver | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2,4-decadienal + NAD+ + H2O | - |
Rattus norvegicus | 2,4-decadienoate + NADH + 2 H+ | - |
? | |
| all-trans-retinal + NAD+ + H2O | - |
Rattus norvegicus | all-trans-retinoate + NADH + 2 H+ | - |
? | |
| all-trans-retinal + NAD+ + H2O | - |
Homo sapiens | all-trans-retinoate + NADH + 2 H+ | - |
? | |
| citral + NAD+ + H2O | - |
Rattus norvegicus | 3,7-dimethyl-2,6-octadienoate + NADH + 2 H+ | - |
? | |
| decanal + NAD+ + H2O | - |
Rattus norvegicus | decanoate + NADH + 2 H+ | - |
? | |
| decanal + NAD+ + H2O | - |
Homo sapiens | decanoate + NADH + 2 H+ | - |
? | |
| hexanal + NAD+ + H2O | - |
Rattus norvegicus | hexanoate + NADH + 2 H+ | - |
? | |
| 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 | ? | - |
? | |
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| ALDH1A1 | - |
Homo sapiens |
| Aldh1a2 | - |
Rattus norvegicus |
| NAD-dependent retinal dehydrogenases | - |
Rattus norvegicus |
| NAD-dependent retinal dehydrogenases | - |
Homo sapiens |
| RALDH | - |
Rattus norvegicus |
| RALDH | - |
Homo sapiens |
| RalDH1 | - |
Homo sapiens |
| RALDH2 | - |
Rattus norvegicus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Rattus norvegicus |
| 25 | - |
assay at | Homo sapiens |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.008 | - |
all-trans-retinal | pH 8.5, 25°C, recombinant mutant Y296V | Homo sapiens | |
| 0.017 | - |
all-trans-retinal | pH 8.5, 25°C, recombinant mutant Y296A | Homo sapiens | |
| 0.03 | - |
all-trans-retinal | pH 8.5, 25°C, recombinant mutant K127A | Homo sapiens | |
| 0.03 | - |
all-trans-retinal | pH 8.5, 25°C, recombinant mutant N120A | Homo sapiens | |
| 0.07 | - |
all-trans-retinal | pH 8.5, 25°C, recombinant enzyme | Homo sapiens | |
| 0.1 | - |
all-trans-retinal | pH 8.5, 25°C, recombinant enzyme | Rattus norvegicus | |
| 0.1 | - |
citral | pH 8.5, 25°C, recombinant enzyme | Rattus norvegicus | |
| 0.15 | - |
2,4-decadienal | pH 8.5, 25°C, recombinant enzyme | Rattus norvegicus | |
| 1 | - |
decanal | pH 8.5, 25°C, recombinant enzyme | Homo sapiens | |
| 2 | - |
hexanal | pH 8.5, 25°C, recombinant enzyme | Rattus norvegicus | |
| 2.2 | - |
decanal | pH 8.5, 25°C, recombinant enzyme | Rattus norvegicus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
assay at | Rattus norvegicus |
| 8.5 | - |
assay at | Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Rattus norvegicus | |
| NAD+ | - |
Homo sapiens | |
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Release 2023.1 (January 2023)
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