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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

Giordano, A.; Febbraio, F.; Russo, C.; Rossi, M.; Raia, C.A.; Biochem. J. 388, 657-667 (2005)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
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°)
Sulfolobus solfataricus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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
Sulfolobus solfataricus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sulfolobus solfataricus
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
cyclohexanol + NAD+
-
667502
Sulfolobus solfataricus
cyclohexanone + NADH + H+
-
-
-
?
Cofactor
Cofactor
Commentary
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
Sulfolobus solfataricus
Cofactor (protein specific)
Cofactor
Commentary
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
Sulfolobus solfataricus
Engineering (protein specific)
Amino acid exchange
Commentary
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°)
Sulfolobus solfataricus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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
Sulfolobus solfataricus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
cyclohexanol + NAD+
-
667502
Sulfolobus solfataricus
cyclohexanone + NADH + H+
-
-
-
?
Other publictions for EC 1.1.1.245
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
667502
Giordano
Evidence for co-operativity in ...
Sulfolobus solfataricus
Biochem. J.
388
657-667
2005
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667621
Secundo
Temperature-induced conformati ...
Sulfolobus solfataricus
Biochemistry
44
11040-11048
2005
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286383
Tae-Kang
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Purification and characterizat ...
Rhodococcus sp., Rhodococcus sp. TK6
J. Microbiol. Biotechnol.
12
39-45
2002
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30
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12556
Dangel
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Enzyme reactions involved in a ...
Pseudomonas sp.
Arch. Microbiol.
152
273-279
1989
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14
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286378
Trower
Isolation and characterization ...
Xanthobacter sp.
Appl. Environ. Microbiol.
49
1282-1289
1985
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4
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286381
Stirling
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Purification and properties of ...
Nocardia sp.
Curr. Microbiol.
4
37-40
1980
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286382
Anderson M.A.; Hall
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Microbial metabolism of alicyc ...
Pseudomonas sp.
J. Gen. Microbiol.
120
89-94
1980
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246371
Donoghue
The metabolism of cyclohexanol ...
Acinetobacter sp., Acinetobacter sp. NCIB
Eur. J. Biochem.
60
1-7
1975
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