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show all sequences of 1.2.1.90

Structural basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase from Thermoproteus tenax

Lorentzen, E.; Hensel, R.; Knura, T.; Ahmed, H.; Pohl, E.; J. Mol. Biol. 341, 815-828 (2004)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
ADP
in contrast to other members of the ALDH superfamily, the enzyme from Thermoproteus tenax is regulated by a number of intermediates and metabolites. In the NAD+-dependent oxidation of D-glyceraldehyde 3-phosphate, D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP increase the affinity for the cosubstrate. In the NADP+-dependent reaction the presence of activators increases Vmax by a factor of 3. The crystal structure of the enzyme with the activating molecules reveal a common regulatory site able to accommodate the different activators
Thermoproteus tenax
AMP
in contrast to other members of the ALDH superfamily, the enzyme from Thermoproteus tenax is regulated by a number of intermediates and metabolites. In the NAD+-dependent oxidation of D-glyceraldehyde 3-phosphate, D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP increase the affinity for the cosubstrate. In the NADP+-dependent reaction the presence of activators increases Vmax by a factor of 3. The crystal structure of the enzyme with the activating molecules reveal a common regulatory site able to accommodate the different activators
Thermoproteus tenax
D-fructose 6-phosphate
in contrast to other members of the ALDH superfamily, the enzyme from Thermoproteus tenax is regulated by a number of intermediates and metabolites. In the NAD+-dependent oxidation of D-glyceraldehyde 3-phosphate, D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP increase the affinity for the cosubstrate. In the NADP+-dependent reaction the presence of activators increases Vmax by a factor of 3. The crystal structure of the enzyme with the activating molecules reveal a common regulatory site able to accommodate the different activators
Thermoproteus tenax
D-glucose 1-phosphate
in contrast to other members of the ALDH superfamily, the enzyme from Thermoproteus tenax is regulated by a number of intermediates and metabolites. In the NAD+-dependent oxidation of D-glyceraldehyde 3-phosphate, D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP increase the affinity for the cosubstrate. In the NADP+-dependent reaction the presence of activators increases Vmax by a factor of 3. The crystal structure of the enzyme with the activating molecules reveal a common regulatory site able to accommodate the different activators
Thermoproteus tenax
Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Thermoproteus tenax
Crystallization (Commentary)
Crystallization
Organism
hanging-drop vapour-diffusion method, crystal structure of the enzyme in complex with the substrate D-glyceraldehyde 3-phosphate at 2.3 A resolution, crystal structure of the enzyme in complex with NAD+ at 2.2 A resolution, co-crystal structures with the activating molecules glucose 1-phosphate, fructose 6-phosphate, AMP and ADP determined at resolutions ranging from 2.3 A to 2.6 A
Thermoproteus tenax
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
in contrast to other members of the ALDH superfamily, the enzyme from Thermoproteus tenax is regulated by a number of intermediates and metabolites. In the NAD+-dependent oxidation of D-glyceraldehyde 3-phosphate, ATP, NADP, NADPH and NADH decrease the affinity for the cosubstrate leaving, however, the catalytic rate virtually unaltered
Thermoproteus tenax
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glyceraldehyde 3-phosphate + NAD(P)+ + H2O
Thermoproteus tenax
the enzyme is part of the modified glycolytic pathway of Thermoproteus tenax. In the classical Embden–Meyerhof–Parnas glycolysis, as found in Eucarya and Bacteria, the oxidation of D-glyceraldehyde 3-phosphate is coupled to phosphorylation to yield 1,3-diphosphoglycerate, which in turn is utilized by phosphoglycerate kinase giving 3-phosphoglycerate and ATP. These steps are reversible and non-regulated in the common Embden–Meyerhof–Parnas pathway. In contrast, the direct and irreversible oxidation of D-glyceraldehyde 3-phosphate to 3-phospho-D-glycerate without production of ATP is catalysed either by non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase or by glyceraldehyde-3-phosphate ferredoxin oxidoreductase (EC 1.2.7.6). The non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase/glyceraldehyde-3-phosphate ferredoxin oxidoreductase substitution in the catabolic Embden–Meyerhof–Parnas pathway avoids the production of the highly thermolabile compound 1,3-diphosphoglycerate and could minimize the pools of the thermolabile intermediates D-glyceraldehyde 3-phosphate and dihydroxyacetonphosphate by driving the carbon flow down the pathway and thus reducing the velocity of their heat destruction
3-phospho-D-glycerate + NAD(P)H + 2 H+
-
-
ir
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermoproteus tenax
O57693
-
-
Purification (Commentary)
Commentary
Organism
-
Thermoproteus tenax
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glyceraldehyde 3-phosphate + NAD(P)+ + H2O
the enzyme is part of the modified glycolytic pathway of Thermoproteus tenax. In the classical Embden–Meyerhof–Parnas glycolysis, as found in Eucarya and Bacteria, the oxidation of D-glyceraldehyde 3-phosphate is coupled to phosphorylation to yield 1,3-diphosphoglycerate, which in turn is utilized by phosphoglycerate kinase giving 3-phosphoglycerate and ATP. These steps are reversible and non-regulated in the common Embden–Meyerhof–Parnas pathway. In contrast, the direct and irreversible oxidation of D-glyceraldehyde 3-phosphate to 3-phospho-D-glycerate without production of ATP is catalysed either by non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase or by glyceraldehyde-3-phosphate ferredoxin oxidoreductase (EC 1.2.7.6). The non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase/glyceraldehyde-3-phosphate ferredoxin oxidoreductase substitution in the catabolic Embden–Meyerhof–Parnas pathway avoids the production of the highly thermolabile compound 1,3-diphosphoglycerate and could minimize the pools of the thermolabile intermediates D-glyceraldehyde 3-phosphate and dihydroxyacetonphosphate by driving the carbon flow down the pathway and thus reducing the velocity of their heat destruction
728132
Thermoproteus tenax
3-phospho-D-glycerate + NAD(P)H + 2 H+
-
-
-
ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
the enzyme is able to utilize NAD+ and NADP+ as cofactor. Without activator Vmax of the NADP-dependent reaction is 40% compared to the NAD+-dependent reaction. In presence of activators (D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP) Vmax of the NADP+-dependent reaction increases by a factor of 3
728132
Thermoproteus tenax
3-phospho-D-glycerate + NADH + 2 H+
-
-
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
the enzyme is able to utilize NAD+ and NADP+ as cofactor. Without activator Vmax of the NADP-dependent reaction is 40% compared to the NAD+-dependent reaction. In presence of activators (D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP) Vmax of the NADP+-dependent reaction increases by a factor of 3
728132
Thermoproteus tenax
3-phospho-D-glycerate + NADPH + 2 H+
-
-
-
ir
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
70
-
assay at
Thermoproteus tenax
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Thermoproteus tenax
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
the enzyme is able to utilize NAD+ and NADP+ as cofactor. Without activator Vmax of the NADP-dependent reaction is 40% compared to the NAD+-dependent reaction. In presence of activators (D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP) Vmax of the NADP+-dependent reaction increases by a factor of 3
Thermoproteus tenax
NADP+
the enzyme is able to utilize NAD+ and NADP+ as cofactor. Without activator Vmax of the NADP-dependent reaction is 40% compared to the NAD+-dependent reaction. In presence of activators (D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP) Vmax of the NADP+-dependent reaction increases by a factor of 3
Thermoproteus tenax
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
ADP
in contrast to other members of the ALDH superfamily, the enzyme from Thermoproteus tenax is regulated by a number of intermediates and metabolites. In the NAD+-dependent oxidation of D-glyceraldehyde 3-phosphate, D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP increase the affinity for the cosubstrate. In the NADP+-dependent reaction the presence of activators increases Vmax by a factor of 3. The crystal structure of the enzyme with the activating molecules reveal a common regulatory site able to accommodate the different activators
Thermoproteus tenax
AMP
in contrast to other members of the ALDH superfamily, the enzyme from Thermoproteus tenax is regulated by a number of intermediates and metabolites. In the NAD+-dependent oxidation of D-glyceraldehyde 3-phosphate, D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP increase the affinity for the cosubstrate. In the NADP+-dependent reaction the presence of activators increases Vmax by a factor of 3. The crystal structure of the enzyme with the activating molecules reveal a common regulatory site able to accommodate the different activators
Thermoproteus tenax
D-fructose 6-phosphate
in contrast to other members of the ALDH superfamily, the enzyme from Thermoproteus tenax is regulated by a number of intermediates and metabolites. In the NAD+-dependent oxidation of D-glyceraldehyde 3-phosphate, D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP increase the affinity for the cosubstrate. In the NADP+-dependent reaction the presence of activators increases Vmax by a factor of 3. The crystal structure of the enzyme with the activating molecules reveal a common regulatory site able to accommodate the different activators
Thermoproteus tenax
D-glucose 1-phosphate
in contrast to other members of the ALDH superfamily, the enzyme from Thermoproteus tenax is regulated by a number of intermediates and metabolites. In the NAD+-dependent oxidation of D-glyceraldehyde 3-phosphate, D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP increase the affinity for the cosubstrate. In the NADP+-dependent reaction the presence of activators increases Vmax by a factor of 3. The crystal structure of the enzyme with the activating molecules reveal a common regulatory site able to accommodate the different activators
Thermoproteus tenax
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Thermoproteus tenax
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
the enzyme is able to utilize NAD+ and NADP+ as cofactor. Without activator Vmax of the NADP-dependent reaction is 40% compared to the NAD+-dependent reaction. In presence of activators (D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP) Vmax of the NADP+-dependent reaction increases by a factor of 3
Thermoproteus tenax
NADP+
the enzyme is able to utilize NAD+ and NADP+ as cofactor. Without activator Vmax of the NADP-dependent reaction is 40% compared to the NAD+-dependent reaction. In presence of activators (D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP) Vmax of the NADP+-dependent reaction increases by a factor of 3
Thermoproteus tenax
Crystallization (Commentary) (protein specific)
Crystallization
Organism
hanging-drop vapour-diffusion method, crystal structure of the enzyme in complex with the substrate D-glyceraldehyde 3-phosphate at 2.3 A resolution, crystal structure of the enzyme in complex with NAD+ at 2.2 A resolution, co-crystal structures with the activating molecules glucose 1-phosphate, fructose 6-phosphate, AMP and ADP determined at resolutions ranging from 2.3 A to 2.6 A
Thermoproteus tenax
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
in contrast to other members of the ALDH superfamily, the enzyme from Thermoproteus tenax is regulated by a number of intermediates and metabolites. In the NAD+-dependent oxidation of D-glyceraldehyde 3-phosphate, ATP, NADP, NADPH and NADH decrease the affinity for the cosubstrate leaving, however, the catalytic rate virtually unaltered
Thermoproteus tenax
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glyceraldehyde 3-phosphate + NAD(P)+ + H2O
Thermoproteus tenax
the enzyme is part of the modified glycolytic pathway of Thermoproteus tenax. In the classical Embden–Meyerhof–Parnas glycolysis, as found in Eucarya and Bacteria, the oxidation of D-glyceraldehyde 3-phosphate is coupled to phosphorylation to yield 1,3-diphosphoglycerate, which in turn is utilized by phosphoglycerate kinase giving 3-phosphoglycerate and ATP. These steps are reversible and non-regulated in the common Embden–Meyerhof–Parnas pathway. In contrast, the direct and irreversible oxidation of D-glyceraldehyde 3-phosphate to 3-phospho-D-glycerate without production of ATP is catalysed either by non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase or by glyceraldehyde-3-phosphate ferredoxin oxidoreductase (EC 1.2.7.6). The non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase/glyceraldehyde-3-phosphate ferredoxin oxidoreductase substitution in the catabolic Embden–Meyerhof–Parnas pathway avoids the production of the highly thermolabile compound 1,3-diphosphoglycerate and could minimize the pools of the thermolabile intermediates D-glyceraldehyde 3-phosphate and dihydroxyacetonphosphate by driving the carbon flow down the pathway and thus reducing the velocity of their heat destruction
3-phospho-D-glycerate + NAD(P)H + 2 H+
-
-
ir
Purification (Commentary) (protein specific)
Commentary
Organism
-
Thermoproteus tenax
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glyceraldehyde 3-phosphate + NAD(P)+ + H2O
the enzyme is part of the modified glycolytic pathway of Thermoproteus tenax. In the classical Embden–Meyerhof–Parnas glycolysis, as found in Eucarya and Bacteria, the oxidation of D-glyceraldehyde 3-phosphate is coupled to phosphorylation to yield 1,3-diphosphoglycerate, which in turn is utilized by phosphoglycerate kinase giving 3-phosphoglycerate and ATP. These steps are reversible and non-regulated in the common Embden–Meyerhof–Parnas pathway. In contrast, the direct and irreversible oxidation of D-glyceraldehyde 3-phosphate to 3-phospho-D-glycerate without production of ATP is catalysed either by non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase or by glyceraldehyde-3-phosphate ferredoxin oxidoreductase (EC 1.2.7.6). The non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase/glyceraldehyde-3-phosphate ferredoxin oxidoreductase substitution in the catabolic Embden–Meyerhof–Parnas pathway avoids the production of the highly thermolabile compound 1,3-diphosphoglycerate and could minimize the pools of the thermolabile intermediates D-glyceraldehyde 3-phosphate and dihydroxyacetonphosphate by driving the carbon flow down the pathway and thus reducing the velocity of their heat destruction
728132
Thermoproteus tenax
3-phospho-D-glycerate + NAD(P)H + 2 H+
-
-
-
ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
the enzyme is able to utilize NAD+ and NADP+ as cofactor. Without activator Vmax of the NADP-dependent reaction is 40% compared to the NAD+-dependent reaction. In presence of activators (D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP) Vmax of the NADP+-dependent reaction increases by a factor of 3
728132
Thermoproteus tenax
3-phospho-D-glycerate + NADH + 2 H+
-
-
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
the enzyme is able to utilize NAD+ and NADP+ as cofactor. Without activator Vmax of the NADP-dependent reaction is 40% compared to the NAD+-dependent reaction. In presence of activators (D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP) Vmax of the NADP+-dependent reaction increases by a factor of 3
728132
Thermoproteus tenax
3-phospho-D-glycerate + NADPH + 2 H+
-
-
-
ir
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
70
-
assay at
Thermoproteus tenax
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Thermoproteus tenax
General Information
General Information
Commentary
Organism
metabolism
the enzyme is part of the modified glycolytic pathway of Thermoproteus tenax. In the classical Embden–Meyerhof–Parnas glycolysis, as found in Eucarya and Bacteria, the oxidation of D-glyceraldehyde 3-phosphate is coupled to phosphorylation to yield 1,3-diphosphoglycerate, which in turn is utilized by phosphoglycerate kinase giving 3-phosphoglycerate and ATP. These steps are reversible and non-regulated in the common Embden–Meyerhof–Parnas pathway. In contrast, the direct and irreversible oxidation of D-glyceraldehyde 3-phosphate to 3-phospho-D-glycerate without production of ATP is catalysed either by non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase or by glyceraldehyde-3-phosphate ferredoxin oxidoreductase (EC 1.2.1.59). The non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase/glyceraldehyde-3-phosphate ferredoxin oxidoreductase substitution in the catabolic Embden–Meyerhof–Parnas pathway avoids the production of the highly thermolabile compound 1,3-diphosphoglycerate and could minimize the pools of the thermolabile intermediates D-glyceraldehyde 3-phosphate and dihydroxyacetonphosphate by driving the carbon flow down the pathway and thus reducing the velocity of their heat destruction
Thermoproteus tenax
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme is part of the modified glycolytic pathway of Thermoproteus tenax. In the classical Embden–Meyerhof–Parnas glycolysis, as found in Eucarya and Bacteria, the oxidation of D-glyceraldehyde 3-phosphate is coupled to phosphorylation to yield 1,3-diphosphoglycerate, which in turn is utilized by phosphoglycerate kinase giving 3-phosphoglycerate and ATP. These steps are reversible and non-regulated in the common Embden–Meyerhof–Parnas pathway. In contrast, the direct and irreversible oxidation of D-glyceraldehyde 3-phosphate to 3-phospho-D-glycerate without production of ATP is catalysed either by non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase or by glyceraldehyde-3-phosphate ferredoxin oxidoreductase (EC 1.2.1.59). The non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase/glyceraldehyde-3-phosphate ferredoxin oxidoreductase substitution in the catabolic Embden–Meyerhof–Parnas pathway avoids the production of the highly thermolabile compound 1,3-diphosphoglycerate and could minimize the pools of the thermolabile intermediates D-glyceraldehyde 3-phosphate and dihydroxyacetonphosphate by driving the carbon flow down the pathway and thus reducing the velocity of their heat destruction
Thermoproteus tenax
Other publictions for EC 1.2.1.90
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)
728132
Lorentzen
Structural basis of allosteric ...
Thermoproteus tenax
J. Mol. Biol.
341
815-828
2004
4
-
1
1
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1
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-
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1
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1
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1
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-
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3
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1
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1
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2
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4
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1
2
1
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1
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1
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-
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1
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-
-
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3
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1
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1
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-
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1
1
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288349
Pohl
The crystal structure of the a ...
Thermoproteus tenax
J. Biol. Chem.
277
19938-19945
2002
-
-
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1
-
-
-
-
-
-
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1
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1
-
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1
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-
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-
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1
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-
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1
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-
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-
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1
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-
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1
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1
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-
-
-
-
-
-
-
-
-
-
-
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727454
Brunner
Role of two different glyceral ...
Thermoproteus tenax
Extremophiles
5
101-109
2001
-
-
-
-
-
-
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3
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-
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1
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1
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2
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2
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3
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1
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2
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1
1
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727825
Brunner
NAD+-dependent glyceraldehyde- ...
Thermoproteus tenax
J. Biol. Chem.
273
6149-6156
1998
7
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1
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5
3
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1
2
1
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1
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1
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2
1
1
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1
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1
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1
1
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7
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1
1
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-
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5
1
3
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1
2
1
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1
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2
1
1
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1
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1
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