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Literature summary for 1.1.1.245 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
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Protein Variants

Protein Variants Comment Organism
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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

Organism UniProt Comment Textmining
Saccharolobus solfataricus
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-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
SSADH
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 Saccharolobus solfataricus

Cofactor

Cofactor Comment Organism Structure
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