Literature summary 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.

Metals/Ions

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

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.1.1.1	Saccharolobus solfataricus	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.1.1.1	3-methylbutan-2-one + NADH + H+	-	Saccharolobus solfataricus	3-methylbutan-2-ol + NAD+	-	?
1.1.1.1	anisaldehyde + NADH + H+	-	Saccharolobus solfataricus	anisic alcohol + NAD+	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
1.1.1.1	ADH	-	Saccharolobus solfataricus
1.1.1.1	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

EC Number	Cofactor	Comment	Organism	Structure
1.1.1.1	NADH	dependent	Saccharolobus solfataricus

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Release 2023.1 (January 2023)