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Literature summary for 1.1.1.1 extracted from
- Arabidopsis thaliana alcohol dehydrogenase is differently affected by several redox modifications (2018), PLoS ONE, 13, e0204530 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| single gene ADH1, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli | Arabidopsis thaliana |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C243S | site-directed mutagenesis, the mutant shows increased specific activity, the mutation at Cys243 does not significantly affect ADH kinetic efficiency | Arabidopsis thaliana |
| C47S | site-directed mutagenesis, the mutation Ser causes an almost complete loss of the enzyme activity | Arabidopsis thaliana |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Diethylamine NONOate | - |
Arabidopsis thaliana |  |
| H2O2 | fomation of a disulfide bridge between residues Cys47 and Cys243. Cys residues responsible for ADH inhibition by H2O2 are oxidized to irreversible forms. ADH inhibition by H2O2 is not reversible by DTT | Arabidopsis thaliana | |
| additional information | ADH activity is not significantly affected by diamide + GSH treatment. NAD+ and NADH binding to ADH reduce enzyme sensitivity to H2O2 and diethylamine NONOate | Arabidopsis thaliana |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.166 | - |
ethanol | recombinant His-tagged wild-type enzyme, pH 7.5, temperature not specified in the publication | Arabidopsis thaliana | |
| 0.251 | - |
ethanol | recombinant His-tagged mutant C243S, pH 7.5, temperature not specified in the publication | Arabidopsis thaliana | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | required, ADH is a Zn-binding enzyme | Arabidopsis thaliana | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ethanol + NAD+ | Arabidopsis thaliana | - |
acetaldehyde + NADH + H+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | P06525 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| side-chain modification | S-glutathionylation, recombinant ADH activity does not decrease upon incubation with GSSG. In contrast, ADH activity is more stable over time when incubated with GSSG. This increase in the enzyme stability leads to an increase (about 20%) in activity compared to the control. Treatment with GSSG does not significantly promote the release of Zn from recombinant ADH | Arabidopsis thaliana |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by affinity chromatography and dialysis | Arabidopsis thaliana |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| cell suspension culture | - |
Arabidopsis thaliana | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 42.7 | - |
purified recombinant His-tagged wild-type enzyme, pH 7.5, temperature not specified in the publication, aldehyde formation | Arabidopsis thaliana |
| 70.8 | - |
purified recombinant His-tagged mutant C243S, pH 7.5, temperature not specified in the publication, aldehyde formation | Arabidopsis thaliana |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ethanol + NAD+ | - |
Arabidopsis thaliana | acetaldehyde + NADH + H+ | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 45000, recombinant His-tagged enzyme, SDS-PAGE, x * 50750, His-tagged enzyme, sequence calculation | Arabidopsis thaliana |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ADH | - |
Arabidopsis thaliana |
| ADH1 | - |
Arabidopsis thaliana |
| alcohol dehydrogenase class-P | UniProt | Arabidopsis thaliana |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 31.5 | - |
ethanol | recombinant His-tagged wild-type enzyme, pH 7.5, temperature not specified in the publication | Arabidopsis thaliana | |
| 52.1 | - |
ethanol | recombinant His-tagged mutant C243S, pH 7.5, temperature not specified in the publication | Arabidopsis thaliana | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Arabidopsis thaliana |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | LC-MS/MS analysis shows that Cys47 and Cys243 can make a stable disulfide bond with glutathione, suggesting redox sensitivity of these residues. Binding of ADH with its cofactors may limit availability of Cys residues to redox modifications | Arabidopsis thaliana | |
| NAD+ | - |
Arabidopsis thaliana | |
| NADH | - |
Arabidopsis thaliana | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | Arabidopsis suspension cell cultures show decreased ADH activity upon exposure to H2O2, but not to the thiol oxidizing agent diamide. Purified recombinant ADH shows a significant decrease in the enzyme activity by treatments with H2O2 and diethylamine NONOate (DEA/NO). Treatments leading to the formation of a disulfide bond between ADH and glutathione (protein S-glutathionylation) have no negative effect on the enzyme activity. LC-MS/MS analysis shows that Cys47 and Cys243 can make a stable disulfide bond with glutathione, suggesting redox sensitivity of these residues. Mutation of ADH Cys47 to Ser causes an almost complete loss of the enzyme activity while the Cys243 to Ser mutant have increased specific activity. Incubation of ADH with NAD+ or NADH prevents inhibition of the enzyme by H2O2 or DEA/NO. Binding of ADH with its cofactors may limit availability of Cys residues to redox modifications | Arabidopsis thaliana |
| additional information | six Cys residues are found to be involved in the intrachain disulfide bond formation Cys99, Cys102, Cys105, Cys 113, Cys173, and Cys177. Among the six Cys residues, Cys99, Cys102, Cys105, and Cys 113 are bound to the same structural Zn atom, and Cys 177 is bound to the Zn atom at the catalytic center | Arabidopsis thaliana |
| physiological function | alcohol dehydrogenase (ADH) catalyzes the reversible conversion of acetaldehyde to ethanol while oxidizing NADH to NAD+. During hypoxia, it ensures the maintenance of the glycolytic flux by recycling NAD+ and controls toxic acetaldehyde produced by the decarboxylation of pyruvate. ADH catalyzes the last step of the ethanol fermentation pathway used by plants to cope with energy deficiency during hypoxic stress | Arabidopsis thaliana |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 189.76 | - |
ethanol | recombinant His-tagged wild-type enzyme, pH 7.5, temperature not specified in the publication | Arabidopsis thaliana | |
| 207.57 | - |
ethanol | recombinant His-tagged mutant C243S, pH 7.5, temperature not specified in the publication | Arabidopsis thaliana | |
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