Literature summary extracted from
Lorentzen, E.; Hensel, R.; Knura, T.; Ahmed, H.; Pohl, E.
Structural basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase from Thermoproteus tenax (2004), J. Mol. Biol., 341, 815-828.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
1.2.1.90 |
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 |
|
1.2.1.90 |
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 |
|
1.2.1.90 |
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 |
|
1.2.1.90 |
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)
EC Number |
Cloned (Comment) |
Organism |
---|
1.2.1.90 |
expression in Escherichia coli |
Thermoproteus tenax |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.2.1.90 |
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
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.2.1.90 |
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)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
1.2.1.90 |
D-glyceraldehyde 3-phosphate + NAD(P)+ + H2O |
Thermoproteus tenax |
the enzyme is part of the modified glycolytic pathway of Thermoproteus tenax. In the classical EmbdenÂMeyerhofÂParnas 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 EmbdenÂMeyerhofÂParnas 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 EmbdenÂMeyerhofÂParnas 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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.2.1.90 |
Thermoproteus tenax |
O57693 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.2.1.90 |
- |
Thermoproteus tenax |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.2.1.90 |
D-glyceraldehyde 3-phosphate + NAD(P)+ + H2O |
the enzyme is part of the modified glycolytic pathway of Thermoproteus tenax. In the classical EmbdenÂMeyerhofÂParnas 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 EmbdenÂMeyerhofÂParnas 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 EmbdenÂMeyerhofÂParnas 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 |
3-phospho-D-glycerate + NAD(P)H + 2 H+ |
- |
ir |
|
1.2.1.90 |
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 |
Thermoproteus tenax |
3-phospho-D-glycerate + NADH + 2 H+ |
- |
ir |
|
1.2.1.90 |
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 |
Thermoproteus tenax |
3-phospho-D-glycerate + NADPH + 2 H+ |
- |
ir |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.2.1.90 |
GAPN |
- |
Thermoproteus tenax |
1.2.1.90 |
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase |
- |
Thermoproteus tenax |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
1.2.1.90 |
70 |
- |
assay at |
Thermoproteus tenax |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
1.2.1.90 |
7 |
- |
assay at |
Thermoproteus tenax |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.2.1.90 |
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 |
|
1.2.1.90 |
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 |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
1.2.1.90 |
metabolism |
the enzyme is part of the modified glycolytic pathway of Thermoproteus tenax. In the classical EmbdenÂMeyerhofÂParnas 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 EmbdenÂMeyerhofÂParnas 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 EmbdenÂMeyerhofÂParnas 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 |