Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | high concentrations of alcohols can bind to the enzyme-NADH complex and activate or inhibit the enzyme | Equus caballus |
Crystallization (Comment) | Organism |
---|---|
enzyme in complex with substrates NADH or NAD+, and 4-methylbenzyl alcohol, or with NAD+ and 4-bromobenzyl alcohol or 1H,1H-heptafluorobutanol, X-ray diffraction structure determination and analysis | Equus caballus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
1H,1H-heptafluorobutanol | strong inhibitor | Equus caballus | |
4-bromobenzyl alcohol-NAD+ | - |
Equus caballus | |
4-methylbenzyl alcohol-NAD+ | - |
Equus caballus | |
additional information | high concentrations of alcohols can bind to the enzyme-NADH complex and activate or inhibit the enzyme | Equus caballus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | models for the Michaelis complexes with NAD+-alcohol and NADH-aldehyde are proposed | Equus caballus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Equus caballus | P00327 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Equus caballus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2,2,2-trifluoroethanol + NAD+ | - |
Equus caballus | 2,2,2-trifluoroethanone + NADH + H+ | - |
? | |
2,3,4,5,6-pentafluorobenzyl alcohol + NAD+ | - |
Equus caballus | 2,3,4,5,6-pentafluorobenzaldehyde + NADH + H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ADH | - |
Equus caballus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Equus caballus | |
NADH | - |
Equus caballus |
General Information | Comment | Organism |
---|---|---|
malfunction | alternative binding modes in abortive NADH-alcohol complexes of horse liver alcohol dehydrogenase | Equus caballus |
additional information | high resolution X-ray crystallography of complexes with NADH and alcohols show alternative modes of binding in the active site. Enzyme crystallized with the good substrates NAD+ and 4-methylbenzyl alcohol is found to be an abortive complex of NADH with 4-methylbenzyl alcohol rotated to a non-productive mode as compared to the structures that resemble reactive Michaelis complexes with NAD+ and 2,2,2-trifluoroethanol or 2,3,4,5,6-pentafluorobenzyl alcohol. Crystals prepared with NAD+ and 4-bromobenzyl alcohol also form the abortive complex with NADH. Crystals prepared with NAD+ and the strong inhibitor 1H,1H-heptafluorobutanol also have NADH, and the alcohol is bound in two different conformations that illustrate binding flexibility. Oxidation of 2-methyl-2,4-pentanediol during the crystallization apparently leads to reduction of the NAD+. Kinetic studies show that high concentrations of alcohols can bind to the enzyme-NADH complex and activate or inhibit the enzyme. Models for the Michaelis complexes with NAD+-alcohol and NADH-aldehyde are proposed | Equus caballus |