Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

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

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.9 E141D kcat for D-glyceraldehyde 3-phosphate is 2.1fold lower than wild-type value Sulfurisphaera tokodaii
1.2.1.9 K137E kcat for D-glyceraldehyde 3-phosphate is 1.1fold lower than wild-type value Sulfurisphaera tokodaii
1.2.1.9 L138T kcat for D-glyceraldehyde 3-phosphate is 1.3fold lower than wild-type value Sulfurisphaera tokodaii
1.2.1.9 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
1.2.1.9 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
1.2.1.9 R136K kcat for D-glyceraldehyde 3-phosphate is 2.8fold lower than wild-type value Sulfurisphaera tokodaii
1.2.1.9 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.9 55000
-
 4 * 55000, SDS-PAGE Sulfurisphaera tokodaii
1.2.1.9 57000
-
 4 * 57000, SDS-PAGE Saccharolobus solfataricus
1.2.1.9 223000
-
 gel filtration Sulfurisphaera tokodaii
1.2.1.9 230000
-
 gel filtration Saccharolobus solfataricus

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.9
-
 Saccharolobus solfataricus
1.2.1.9
-
 Sulfurisphaera tokodaii

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.9 60
-
 assay at Saccharolobus solfataricus
1.2.1.9 60
-
 assay at Sulfurisphaera tokodaii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.9 1.13
-
 D-glyceraldehyde 3-phosphate pH 8.0, 60°C, mutant enzyme Y139R Sulfurisphaera tokodaii
1.2.1.9 15
-
 D-glyceraldehyde 3-phosphate pH 8.0, 60°C Saccharolobus solfataricus
1.2.1.9 117
-
 D-glyceraldehyde 3-phosphate pH 8.0, 60°C, mutant enzyme R136K Sulfurisphaera tokodaii
1.2.1.9 161
-
 D-glyceraldehyde 3-phosphate pH 8.0, 60°C, mutant enzyme E141D Sulfurisphaera tokodaii
1.2.1.9 257
-
 D-glyceraldehyde 3-phosphate pH 8.0, 60°C, mutant enzyme L138T Sulfurisphaera tokodaii
1.2.1.9 297
-
 D-glyceraldehyde 3-phosphate pH 8.0, 60°C, mutant enzyme K137E Sulfurisphaera tokodaii
1.2.1.9 341
-
 D-glyceraldehyde 3-phosphate pH 8.0, 60°C, wild-type enzyme Sulfurisphaera tokodaii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.9 8
-
 assay at Saccharolobus solfataricus
1.2.1.9 8
-
 assay at Sulfurisphaera tokodaii