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Literature summary for 1.1.1.1 extracted from
- Characterization of the two alcohol dehydrogenases of Zymomonas mobilis (1981), Arch. Biochem. Biophys., 210, 775-785.
General Stability
| General Stability | Organism |
|---|---|
| enzyme form ADH I is more stable during purification than enzyme form ADH-II | Zymomonas mobilis |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zinc | enzyme form ADH I and ADH II contain one zinc atom per subunit | Zymomonas mobilis |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 31100 | - |
2 * 31100, enzyme form ADH-II, SDS-PAGE | Zymomonas mobilis |
| 34700 | - |
2 * 34700, enzyme form ADH-I, SDS-PAGE | Zymomonas mobilis |
| 67000 | - |
enzyme form ADH-II, glycerol density gradient centrifugation | Zymomonas mobilis |
| 145000 | - |
enzyme form ADH-I, glycerol density gradient centrifugation | Zymomonas mobilis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Zymomonas mobilis | - |
enzyme form ADH-I and ADH-II | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Zymomonas mobilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| allyl alcohol + NAD+ | - |
Zymomonas mobilis | prop-2-en-1-al + NADH | - |
? | |
| butanol + NAD+ | oxidized by enzyme form ADH-I, no activity with enzyme form ADH-II | Zymomonas mobilis | butyraldehyde + NADH | - |
? | |
| ethanol + NAD+ | - |
Zymomonas mobilis | acetaldehyde + NADH | - |
? | |
| methanol + NAD+ | no activity | Zymomonas mobilis | formaldehyde + NADH + H+ | - |
? | |
| propan-2-ol + NAD+ | very low activity | Zymomonas mobilis | acetone + NADH | - |
? | |
| propanol + NAD+ | - |
Zymomonas mobilis | propionaldehyde + NADH + H+ | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 34700, enzyme form ADH-I, SDS-PAGE | Zymomonas mobilis |
| dimer | 2 * 31100, enzyme form ADH-II, SDS-PAGE | Zymomonas mobilis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9.5 | - |
enzyme form ADH-I, oxidation of ethanol | Zymomonas mobilis |
| 10 | - |
enzyme form ADH-II, oxidation of ethanol | Zymomonas mobilis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Zymomonas mobilis | |
| NADH | - |
Zymomonas mobilis | |
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Release 2023.1 (January 2023)
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