EC Number   |
Cofactor |
Reference |
|---|
    1.1.1.1 | 3-benzoylpyridine-adenine dinucleotide |
can be used as coenzyme |
285588 |
| 1.1.1.1 | acycloNAD+ |
NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety. The chemical properties are comparable to those of beta-NAD+ with a redox potential of -324 mV and a 341 nm lambdamax for the reduced form. The stereochemistry of the hydride transfer in the oxidation of n-butanol is identical to that for the reaction with beta-NAD+. There is no detectable reduction of acycloNAD+ by secondary alcohols although these alcohols serve as competitive inhibitors. AcycloNAD+ converts horse liver ADH from a broad spectrum alcohol dehydrogenase, capable of utilizing either primary or secondary alcohols, into an exclusively primary alcohol dehydrogenase |
738096 |
| 1.1.1.1 | glutathione |
dependent on |
762739 |
| 1.1.1.1 | more |
cofactor docking to the enzyme. The affinity for NADH coenzyme attachment is higher than the values provided for NADPH |
760374 |
| 1.1.1.1 | more |
crystallographic study of the coenzyme binding mode |
285593 |
| 1.1.1.1 | more |
in presence of propan-2-ol at 10% v/v, reduction of fluorinated ketones is catalyzed without addition of NADH |
738908 |
| 1.1.1.1 | more |
kinetic study on the binding of monomeric and polymeric derivatives of NAD+ |
285643 |
| 1.1.1.1 | more |
kinetics of native and modified enzyme with coenzyme analogues |
285609 |
| 1.1.1.1 | more |
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 |
762242 |
| 1.1.1.1 | more |
NADP+ shows less than 0.1% of the activity with NAD+ |
669540 |
