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Literature summary for 1.1.1.245 extracted from

  • Secundo, F.; Russo, C.; Giordano, A.; Carrea, G.; Rossi, M.; Raia, C.A.
    Temperature-induced conformational change at the catalytic site of Sulfolobus solfataricus alcohol dehydrogenase highlighted by Asn249Tyr substitution. A hydrogen/deuterium exchange, kinetic, and fluorescence quenching study (2005), Biochemistry, 44, 11040-11048.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Saccharolobus solfataricus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37500
-
4 * 37500, SDS-PAGE Saccharolobus solfataricus
150000
-
SDS-PAGE Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-propanol + NAD+
-
Saccharolobus solfataricus propionaldehyde + NADH
-
?
benzyl alcohol + NAD+
-
Saccharolobus solfataricus benzylaldehyde + NADH
-
?
cyclohexanol + NAD+
-
Saccharolobus solfataricus cyclohexanone + NADH + H+
-
?
cyclohexanol + NAD+ temperature-induced conformational change is associated with the flexible loops directly involved in the substrate and coenzyme binding Saccharolobus solfataricus cyclohexanone + NADH + H+
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 37500, SDS-PAGE Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
alcohol dehydrogenase
-
Saccharolobus solfataricus
SSADH
-
Saccharolobus solfataricus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 65
-
Saccharolobus solfataricus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Saccharolobus solfataricus
NAD+ temperature-induced conformational change is associated with the flexible loops directly involved in the substrate and coenzyme binding Saccharolobus solfataricus