Activating Compound | Comment | 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 (Comment) | Organism |
---|---|
expression in Escherichia coli | Thermoproteus tenax |
Crystallization (Comment) | 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 | Comment | 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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Thermoproteus tenax | O57693 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Thermoproteus tenax |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | |
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 | |
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 | Comment | Organism |
---|---|---|
GAPN | - |
Thermoproteus tenax |
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase | - |
Thermoproteus tenax |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
70 | - |
assay at | Thermoproteus tenax |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Thermoproteus tenax |
Cofactor | Comment | 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 |
General Information | Comment | Organism |
---|---|---|
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 |