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BRENDA support

Literature summary for 1.1.1.1 extracted from

  • Plapp, B.V.
    Conformational changes and catalysis by alcohol dehydrogenase (2010), Arch. Biochem. Biophys., 493, 3-12.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Equus caballus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Equus caballus
-

Cofactor

Cofactor Comment Organism Structure
NAD+ the binding of NAD+ is kinetically limited by a unimolecular isomerization (corresponding to the conformational change) that is controlled by deprotonation of the catalytic zinc-water to produce a negatively-charged zinc-hydroxide, which can attract the positively-charged nicotinamide ring Equus caballus