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Literature summary for 1.2.1.9 extracted from

  • Ito, F.; Miyake, M.; Fushinobu, S.; Nakamura, S.; Shimizu, K.; Wakagi, T.
    Engineering the allosteric properties of archaeal non-phosphorylating glyceraldehyde-3-phosphate dehydrogenases (2014), Biochim. Biophys. Acta, 1844, 759-766.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
D-glucose 1-phosphate activates. Activation follows an increase in affinity for glyceraldehyde-3-phosphate rather than an increase in maximum velocity Sulfurisphaera tokodaii
D-glucose 1-phosphate activates. Activation follows an increase in maximum velocity rather than in affinity glyceraldehyde-3-phosphate Saccharolobus solfataricus

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Saccharolobus solfataricus
expression in Escherichia coli Sulfurisphaera tokodaii

Protein Variants

Protein Variants Comment Organism
E141D kcat for D-glyceraldehyde 3-phosphate is 2.1fold lower than wild-type value Sulfurisphaera tokodaii
K137E kcat for D-glyceraldehyde 3-phosphate is 1.1fold lower than wild-type value Sulfurisphaera tokodaii
L138T kcat for D-glyceraldehyde 3-phosphate is 1.3fold lower than wild-type value Sulfurisphaera tokodaii
additional information in non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Sulfolobus tokodaii, D-glucose 1-phosphate-induced activation follows an increase in affinity for glyceraldehyde-3-phosphate rather than an increase in maximum velocity, whereas in the enzyme from Sulfolobus solfataricus, D-glucose 1-phosphate-induced activation follows an increase in maximum velocity rather than in affinity for glyceraldehyde-3-phosphate. To explore the molecular basis of this difference 14 mutants and 2 chimeras are generated. The analyses of chimeric enzymes generated from regions of the Sulfolobus tokodaii enzyme and the Sulfolobus solfataricus enzyme indicates that a 57-residue module located in the subunit interface is involved in their allosteric behavior Saccharolobus solfataricus
additional information in non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Sulfolobus tokodaii, D-glucose 1-phosphate-induced activation follows an increase in affinity for glyceraldehyde-3-phosphate rather than an increase in maximum velocity, whereas in the enzyme from Sulfolobus solfataricus, D-glucose 1-phosphate-induced activation follows an increase in maximum velocity rather than in affinity for glyceraldehyde-3-phosphate. To explore the molecular basis of this difference 14 mutants and 2 chimeras are generated. The analyses of chimeric enzymes generated from regions of the Sulfolobus tokodaii enzyme and the Sulfolobus solfataricus enzyme indicates that a 57-residue module located in the subunit interface is involved in their allosteric behavior Sulfurisphaera tokodaii
R136K kcat for D-glyceraldehyde 3-phosphate is 2.8fold lower than wild-type value Sulfurisphaera tokodaii
Y139R kcat for D-glyceraldehyde 3-phosphate is 302fold lower than wild-type value. The mutant enzyme no longer displays a sigmoidal K-type-like allostery but instead has apparent V-type allostery similar to that of the Sulfolobus solfataricus enzyme, suggesting that the residue located in the center of the homotetramer critically contributes to the allosteric behavior Sulfurisphaera tokodaii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55000
-
4 * 55000, SDS-PAGE Sulfurisphaera tokodaii
57000
-
4 * 57000, SDS-PAGE Saccharolobus solfataricus
223000
-
gel filtration Sulfurisphaera tokodaii
230000
-
gel filtration Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q97U30
-
-
Saccharolobus solfataricus P2 Q97U30
-
-
Sulfurisphaera tokodaii Q96XP0
-
-
Sulfurisphaera tokodaii 7 Q96XP0
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharolobus solfataricus
-
Sulfurisphaera tokodaii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + NADP+ + H2O
-
Saccharolobus solfataricus 3-phospho-D-glycerate + NADPH + 2 H+
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
-
Sulfurisphaera tokodaii 3-phospho-D-glycerate + NADPH + 2 H+
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
-
Saccharolobus solfataricus P2 3-phospho-D-glycerate + NADPH + 2 H+
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
-
Sulfurisphaera tokodaii 7 3-phospho-D-glycerate + NADPH + 2 H+
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 55000, SDS-PAGE Sulfurisphaera tokodaii
homotetramer 4 * 57000, SDS-PAGE Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
GAPN
-
Saccharolobus solfataricus
GAPN
-
Sulfurisphaera tokodaii
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
Saccharolobus solfataricus
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
Sulfurisphaera tokodaii
SSO3194 locus name Saccharolobus solfataricus
STK_24770 locus name Sulfurisphaera tokodaii

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
60
-
assay at Saccharolobus solfataricus
60
-
assay at Sulfurisphaera tokodaii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13
-
D-glyceraldehyde 3-phosphate pH 8.0, 60┬░C, mutant enzyme Y139R Sulfurisphaera tokodaii
15
-
D-glyceraldehyde 3-phosphate pH 8.0, 60┬░C Saccharolobus solfataricus
117
-
D-glyceraldehyde 3-phosphate pH 8.0, 60┬░C, mutant enzyme R136K Sulfurisphaera tokodaii
161
-
D-glyceraldehyde 3-phosphate pH 8.0, 60┬░C, mutant enzyme E141D Sulfurisphaera tokodaii
257
-
D-glyceraldehyde 3-phosphate pH 8.0, 60┬░C, mutant enzyme L138T Sulfurisphaera tokodaii
297
-
D-glyceraldehyde 3-phosphate pH 8.0, 60┬░C, mutant enzyme K137E Sulfurisphaera tokodaii
341
-
D-glyceraldehyde 3-phosphate pH 8.0, 60┬░C, wild-type enzyme Sulfurisphaera tokodaii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Saccharolobus solfataricus
8
-
assay at Sulfurisphaera tokodaii