Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.1 extracted from

  • Plapp, B.; Subramanian, R.
    Alternative binding modes in abortive NADH-alcohol complexes of horse liver alcohol dehydrogenase (2021), Arch. Biochem. Biophys., 701, 108825 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

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 (Commentary)

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

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 [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

Organism UniProt Comment Textmining
Equus caballus P00327
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Equus caballus
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
ADH
-
Equus caballus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Equus caballus
NADH
-
Equus caballus

General Information

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