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Literature summary extracted from

  • Giordano, A.; Febbraio, F.; Russo, C.; Rossi, M.; Raia, C.A.
    Evidence for co-operativity in coenzyme binding to tetrameric Sulfolobus solfataricus alcohol dehydrogenase and its structural basis: fluorescence, kinetic and structural studies of the wild-type enzyme and non-co-operative N249Y mutant (2005), Biochem. J., 388, 657-667.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.245 N249Y mutant N249Y displays non-cooperative behavious in coenzyme binding under the same experimental conditions used for the wild-type enzyme (that exhibits linearity of NAD(H) binding at pH 9.8 and at moderate ionic strength, in addition to positive cooperativity at pH 7.8 and 6.8, and at pH 9.8 in the presence of salt. NADH binding is positively cooperative below 20°C and negatively cooperative at 40–50°) Saccharolobus solfataricus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.245 additional information
-
 additional information steady-state kinetic measurements show that SsADH displays standard Michaelis–Menten kinetics between 35°C and 45°C, but exhibits positive and negative cooperativity for NADH oxidation below and above this range of temperatures, respectively Saccharolobus solfataricus

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.245 cyclohexanol + NAD+
-
 Saccharolobus solfataricus cyclohexanone + NADH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.245 SSADH
-
 Saccharolobus solfataricus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.245 NADH enzyme exhibits linearity of NAD(H) binding at pH 9.8 and at moderate ionic strength, in addition to positive cooperativity at pH 7.8 and 6.8, and at pH 9.8 in the presence of salt. NADH binding is positively cooperative below 20°C and negatively cooperative at 40–50°. Steady-state kinetic measurements show that SsADH displays standard Michaelis–Menten kinetics between 35°C and 45°C, but exhibits positive and negative cooperativity for NADH oxidation below and above this range of temperatures, respectively. Mutant N249Y displays non-cooperative behavious in coenzyme binding under the same experimental conditions used for the wild-type enzyme Saccharolobus solfataricus