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Information on EC 1.2.1.90 - glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+]
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1.2.1.90 glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+]IUBMB Comments
The enzyme is part of the modified Embden-Meyerhof-Parnas pathway of the archaeon Thermoproteus tenax. cf. EC 1.2.1.9 [glyceraldehyde-3-phosphate dehydrogenase (NADP+)].
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
non-phosphorylating ga3pdhase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NAD+-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
non-phosphorylating Ga3PDHase
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glyceraldehyde 3-phosphate + NAD(P)+ + H2O = 3-phospho-D-glycerate + NAD(P)H + 2 H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-
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SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate:NAD(P)+ oxidoreductase
The enzyme is part of the modified Embden-Meyerhof-Parnas pathway of the archaeon Thermoproteus tenax. cf. EC 1.2.1.9 [glyceraldehyde-3-phosphate dehydrogenase (NADP+)].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate + NAD(P)+ + H2O
3-phospho-D-glycerate + NAD(P)H + 2 H+
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
-
-
ir
L-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-L-glycerate + NADH + 2 H+
-
-
-
ir
L-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-L-glycerate + NADPH + 2 H+
-
-
-
ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
-
-
-
ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
-
-
-
ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
part of the modified Emden-Meyerhof-Parnas pathway in Thermoproteus tenax
-
-
ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
the enzyme is part of the modified EmbdenÂMeyerhofÂParnas pathway, the main route for carbohydrate metabolism in Thermoproteus tenax
-
-
ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
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
-
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
-
-
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
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
-
-
ir
additional information
?
-
the enzyme is also active with succinate semialdehyde (SSA), cf. EC 1.2.1.16. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. When D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed. In addition, recombinant GabD is able to oxidize both D- and L-Ga3P isomers with either NADP+ or NAD+ as cofactors with similar apparent Km values for D- or L-Ga3P and twice the kcat with D-Ga3P with both cofactors. No activity with formaldehyde, glutaraldehyde, ethanol, and glycerol as substrates
-
-
-
additional information
?
-
-
the enzyme is also active with succinate semialdehyde (SSA), cf. EC 1.2.1.16. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. When D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed. In addition, recombinant GabD is able to oxidize both D- and L-Ga3P isomers with either NADP+ or NAD+ as cofactors with similar apparent Km values for D- or L-Ga3P and twice the kcat with D-Ga3P with both cofactors. No activity with formaldehyde, glutaraldehyde, ethanol, and glycerol as substrates
-
-
-
additional information
?
-
the enzyme is also active with succinate semialdehyde (SSA), cf. EC 1.2.1.16. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. When D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed. In addition, recombinant GabD is able to oxidize both D- and L-Ga3P isomers with either NADP+ or NAD+ as cofactors with similar apparent Km values for D- or L-Ga3P and twice the kcat with D-Ga3P with both cofactors. No activity with formaldehyde, glutaraldehyde, ethanol, and glycerol as substrates
-
-
-
additional information
?
-
the enzyme is also active with succinate semialdehyde (SSA), cf. EC 1.2.1.16. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. When D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed. In addition, recombinant GabD is able to oxidize both D- and L-Ga3P isomers with either NADP+ or NAD+ as cofactors with similar apparent Km values for D- or L-Ga3P and twice the kcat with D-Ga3P with both cofactors. No activity with formaldehyde, glutaraldehyde, ethanol, and glycerol as substrates
-
-
-
additional information
?
-
the enzyme is also active with succinate semialdehyde (SSA), cf. EC 1.2.1.16. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. When D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed. In addition, recombinant GabD is able to oxidize both D- and L-Ga3P isomers with either NADP+ or NAD+ as cofactors with similar apparent Km values for D- or L-Ga3P and twice the kcat with D-Ga3P with both cofactors. No activity with formaldehyde, glutaraldehyde, ethanol, and glycerol as substrates
-
-
-
additional information
?
-
the enzyme is also active with succinate semialdehyde (SSA), cf. EC 1.2.1.16. Values obtained reflect a 3500 and 87fold higher catalytic efficiency when SSA/NADP+ or SSA/NAD+ pairs, respectively, are used instead of Ga3P/NADP+ or Ga3P/NAD+. When D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed. In addition, recombinant GabD is able to oxidize both D- and L-Ga3P isomers with either NADP+ or NAD+ as cofactors with similar apparent Km values for D- or L-Ga3P and twice the kcat with D-Ga3P with both cofactors. No activity with formaldehyde, glutaraldehyde, ethanol, and glycerol as substrates
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate + NAD(P)+ + H2O
3-phospho-D-glycerate + NAD(P)H + 2 H+
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
-
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
-
-
-
ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
-
-
-
ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
-
-
-
ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
part of the modified Emden-Meyerhof-Parnas pathway in Thermoproteus tenax
-
-
ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
the enzyme is part of the modified EmbdenÂMeyerhofÂParnas pathway, the main route for carbohydrate metabolism in Thermoproteus tenax
-
-
ir
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
NADP(H), NADH, and ATP reduce the affinity for the cosubstrate, AMP, ADP, D-glucose 1-phosphate, and D-fructose 6-phosphate increase the affinity for NAD+. Additionally, most of the effectors investigated induce cooperativity of NAD+ binding. NADP+ cannot replace NAD+
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
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
additional information
when D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed
-
additional information
-
when D-Ga3P is the substrate, no significant differences for NADP+ or NAD+ are observed
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Mg2+ does not affect the enzymatic properties
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-Glyceraldehyde 3-phosphate
strong competitive inhibitor with respect to D-glyceraldehyde 3-phosphate
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3
L-Glyceraldehyde 3-phosphate
about, pH 8.5, 30°C, recombinant enzyme, with NADP+
0.23
NADP+
pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde
additional information
D-glyceraldehyde 3-phosphate
the saturation with D-glyceraldehyde 3-phosphate follows classical Michaelis-Menten kinetics, showing half-maximal saturation at 50 mM. A definite Km for the free aldehyde, the presumed substrate of the enzyme, cannot be given because the portion of the free aldehyde in aqueous solution could not be determined at 70 °C
1.9
D-glyceraldehyde 3-phosphate
pH 8.5, 30°C, recombinant enzyme, with NADP+
2.2
D-glyceraldehyde 3-phosphate
pH 8.5, 30°C, recombinant enzyme, with NAD+
0.4
NAD+
pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.007
L-Glyceraldehyde 3-phosphate
about, pH 8.5, 30°C, recombinant enzyme
0.0167
NAD+
pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde
0.0133
NADP+
pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde
0.0133
D-glyceraldehyde 3-phosphate
pH 8.5, 30°C, recombinant enzyme, with NADP+
0.0167
D-glyceraldehyde 3-phosphate
pH 8.5, 30°C, recombinant enzyme, with NAD+
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0023
L-Glyceraldehyde 3-phosphate
about, pH 8.5, 30°C, recombinant enzyme, with NADP+
0.0418
NAD+
pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde
0.0578
NADP+
pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde
0.007
D-glyceraldehyde 3-phosphate
pH 8.5, 30°C, recombinant enzyme, with NADP+
0.0076
D-glyceraldehyde 3-phosphate
pH 8.5, 30°C, recombinant enzyme, with NAD+
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
specific activity of remains constant in autotrophically and heterotrophically grown cells
brenda
specific activity of remains constant in autotrophically and heterotrophically grown cells
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
the enzyme is part of the modified EmbdenÂMeyerhofÂParnas pathway, the main route for carbohydrate metabolism in Thermoproteus tenax
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
physiological function
enzyme GabD irreversibly oxidizes D-glyceraldehyde 3-phosphate (Ga3P) to 3-phospho-D-glycerate (3Pglycerate) using NAD+ or NADP+, thus resembling a non-phosphorylating Ga3PDHase. But the enzyme shows about 6fold higher Km value and three orders of magnitude higher catalytic efficiency with succinate semialdehyde (SSA) and NADP+. Indeed, the GabD protein identity corresponds to an SSA dehydrogenase (SSADHase, EC 1.2.1.16)
physiological function
-
enzyme GabD irreversibly oxidizes D-glyceraldehyde 3-phosphate (Ga3P) to 3-phospho-D-glycerate (3Pglycerate) using NAD+ or NADP+, thus resembling a non-phosphorylating Ga3PDHase. But the enzyme shows about 6fold higher Km value and three orders of magnitude higher catalytic efficiency with succinate semialdehyde (SSA) and NADP+. Indeed, the GabD protein identity corresponds to an SSA dehydrogenase (SSADHase, EC 1.2.1.16)
-
physiological function
-
enzyme GabD irreversibly oxidizes D-glyceraldehyde 3-phosphate (Ga3P) to 3-phospho-D-glycerate (3Pglycerate) using NAD+ or NADP+, thus resembling a non-phosphorylating Ga3PDHase. But the enzyme shows about 6fold higher Km value and three orders of magnitude higher catalytic efficiency with succinate semialdehyde (SSA) and NADP+. Indeed, the GabD protein identity corresponds to an SSA dehydrogenase (SSADHase, EC 1.2.1.16)
-
physiological function
-
enzyme GabD irreversibly oxidizes D-glyceraldehyde 3-phosphate (Ga3P) to 3-phospho-D-glycerate (3Pglycerate) using NAD+ or NADP+, thus resembling a non-phosphorylating Ga3PDHase. But the enzyme shows about 6fold higher Km value and three orders of magnitude higher catalytic efficiency with succinate semialdehyde (SSA) and NADP+. Indeed, the GabD protein identity corresponds to an SSA dehydrogenase (SSADHase, EC 1.2.1.16)
-
physiological function
-
enzyme GabD irreversibly oxidizes D-glyceraldehyde 3-phosphate (Ga3P) to 3-phospho-D-glycerate (3Pglycerate) using NAD+ or NADP+, thus resembling a non-phosphorylating Ga3PDHase. But the enzyme shows about 6fold higher Km value and three orders of magnitude higher catalytic efficiency with succinate semialdehyde (SSA) and NADP+. Indeed, the GabD protein identity corresponds to an SSA dehydrogenase (SSADHase, EC 1.2.1.16)
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GAPN_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
509
0
56927
Swiss-Prot
-
Q82TA7_NITEU
Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298)
443
0
47643
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method. Crystal structure of of the complex of the enzyme with its natural inhibitor NADP+. The structure is solved by multiple anomalous diffraction and refined to a resolution of 2.4 A with a crystallographic R-factor of 0.21
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
100 min, recombinant enzyme loses 90% of its activity, the enzyme isolated from Thermoproteus tenax loses 70% of its activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene gapD, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pohl, E.; Brunner, N.; Wilmanns, M.; Hensel, R.
The crystal structure of the allosteric non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeum Thermoproteus tenax
J. Biol. Chem.
277
19938-19945
2002
Thermoproteus tenax (O57693)
brenda
Brunner, N.A.; Siebers, B.; Hensel R.
Role of two different glyceraldehyde-3-phosphate dehydrogenases in controlling the reversible Embden-Meyerhof-Parnas pathway in Thermoproteus tenax: regulation on protein and transcript level
Extremophiles
5
101-109
2001
Thermoproteus tenax (O57693)
brenda
Brunner, N.A.; Brinkmann, H.; Siebers, B., Hensel, R.
NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax. The first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties
J. Biol. Chem.
273
6149-6156
1998
Thermoproteus tenax (O57693)
brenda
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
J. Mol. Biol.
341
815-828
2004
Thermoproteus tenax (O57693)
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Corregido, M.; Asencion Diez, M.; Iglesias, A.; Piattoni, C.
New pieces to the carbon metabolism puzzle of Nitrosomonas europaea kinetic characterization of glyceraldehyde-3 phosphate and succinate semialdehyde dehydrogenases
Biochimie
158
238-245
2019
Nitrosomonas europaea (Q82TA7), Nitrosomonas europaea, Nitrosomonas europaea NBRC 14298 (Q82TA7), Nitrosomonas europaea ATCC 19718 (Q82TA7), Nitrosomonas europaea KCTC 2705 (Q82TA7), Nitrosomonas europaea CIP 103999 (Q82TA7)
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