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Literature summary for 1.1.1.1 extracted from

  • Trincone, A.; Lama, L.; Rella, R.; D'Auria, S.; Raia, C.A.; Nicolaus, B.
    Determination of hydride transfer stereospecificity of NADH-dependent alcohol-aldehyde/ketone oxidoreductase from Sulfolobus solfataricus (1990), Biochim. Biophys. Acta, 1041, 94-96.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ contains a zinc ion which is directly involved in the structural stabilization of enzyme molecule Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-methylbutan-2-one + NADH + H+
-
Saccharolobus solfataricus 3-methylbutan-2-ol + NAD+
-
?
anisaldehyde + NADH + H+
-
Saccharolobus solfataricus anisic alcohol + NAD+
-
?

Synonyms

Synonyms Comment Organism
ADH
-
Saccharolobus solfataricus
alcohol-aldehyde/ketone oxidoreductase, NAD+-dependent the enzyme transfers the pro-R hydrogen from coenzyme to substrate and is therefore an A-specific dehydrogenase Saccharolobus solfataricus

Cofactor

Cofactor Comment Organism Structure
NADH dependent Saccharolobus solfataricus