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Literature summary extracted from

  • Ito, F.; Chishiki, H.; Fushinobu, S.; Wakagi, T.
    Comparative analysis of two glyceraldehyde-3-phosphate dehydrogenases from a thermoacidophilic archaeon, Sulfolobus tokodaii (2012), FEBS Lett., 586, 3097-3103.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.2.1.9 D-fructose 6-phosphate a slight increase in enzyme activity is observed in the presence of D-fructose 6-phosphate and coenzyme A (1.1fold) Sulfurisphaera tokodaii
1.2.1.9 D-glucose 1-phosphate activity increases by 1.4fold with increasing D-glucose 1-phosphate concentration from 0 to 0.1 mM. The enzyme shows K-type allosterism in which the positive cooperativity is abolished with concomitant activation by glucose 1-phosphate Sulfurisphaera tokodaii
1.2.1.9 D-glucose 1-phosphate D-glucose 1-phosphate does not influence the affinity for DL-glyceraldehyde-3-phosphate; but increases the turnover severalfold Sulfurisphaera tokodaii
1.2.1.9 additional information ATP, ADP, AMP, D-glucose 6-phosphate and galactose 1-phosphate exhibit no effect on enzyme activity Sulfurisphaera tokodaii
1.2.1.13 additional information no influence on activity is observed on assaying of the enzyme with 5 mM substrate and 0.5 mM co-substrate with 1 mM ATP, ADP, AMP, D-glucose 6-phosphate, D-fructose 6-phosphate, galactose 1-phosphate, D-glucose 1-phosphate or coenzyme A in either the glycolytic or gluconeogenic reaction Sulfurisphaera tokodaii
1.2.1.59 additional information no influence on activity is observed on assaying of the enzyme with 5 mM substrate and 0.5 mM co-substrate with 1 mM ATP, ADP, AMP, glucose 6-phosphate, fructose 6-phosphate, galactose 1-phosphate, glucose 1-phosphate or coenzyme A in either the glycolytic or gluconeogenic reaction Sulfurisphaera tokodaii

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.9 expressed in Escherichia coli C43 (DE3) cells Sulfurisphaera tokodaii
1.2.1.9 expression in Escherichia coli Sulfurisphaera tokodaii
1.2.1.13 expressed in Escherichia coli C43 (DE3) cells Sulfurisphaera tokodaii
1.2.1.59 expression in Escherichia coli Sulfurisphaera tokodaii

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.9 A198S/S199I the catalytic efficiency with NADP+ decreases while that with NAD+ increases by 2.5fold. Substitutions reduces the NADP/NAD preference ratio by more than 50% Sulfurisphaera tokodaii
1.2.1.9 A198S/S199I the mutant shows reduced catalytic efficiency with NADP+ and increased catalytic efficiency with NAD+ as compared to the wild type enzyme Sulfurisphaera tokodaii
1.2.1.9 S199I the catalytic efficiency (kcat/Km) with NADP+ decreases by 0.5fold while that with NAD+ remains unchanged. Substitution reduces the NADP/NAD preference ratio by more than 50% Sulfurisphaera tokodaii
1.2.1.9 S199I the mutant shows reduced catalytic efficiency with NADP+ and increased catalytic efficiency with NAD+ as compared to the wild type enzyme Sulfurisphaera tokodaii

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.9 additional information no effect: ADP, AMP, D-glucose 6-phosphate and D-galactose 1-phosphate Sulfurisphaera tokodaii
1.2.1.13 3-phospho-D-glyceroyl phosphate
-
 Sulfurisphaera tokodaii
1.2.1.13 DL-glyceraldehyde 3-phosphate
-
 Sulfurisphaera tokodaii
1.2.1.13 NAD+
-
 Sulfurisphaera tokodaii
1.2.1.13 NADH strong inhibition with excess co-substrate s observed and no activity is observed with over 2 mM NADH Sulfurisphaera tokodaii
1.2.1.13 NADP+
-
 Sulfurisphaera tokodaii
1.2.1.13 NADPH strong inhibition with excess co-substrate s observed and no activity is observed with over 2 mM NADPH Sulfurisphaera tokodaii
1.2.1.59 3-phospho-D-glyceroyl phosphate
-
 Sulfurisphaera tokodaii
1.2.1.59 D-glyceraldehyde 3-phosphate
-
 Sulfurisphaera tokodaii
1.2.1.59 additional information no influence on activity is observed on assaying of the enzyme with 5 mM substrate and 0.5 mM co-substrate with 1 mM ATP, ADP, AMP, glucose 6-phosphate, fructose 6-phosphate, galactose 1-phosphate, glucose 1-phosphate or coenzyme A in either the glycolytic or gluconeogenic reaction Sulfurisphaera tokodaii
1.2.1.59 NAD+
-
 Sulfurisphaera tokodaii
1.2.1.59 NADH
-
 Sulfurisphaera tokodaii
1.2.1.59 NADP+
-
 Sulfurisphaera tokodaii
1.2.1.59 NADPH
-
 Sulfurisphaera tokodaii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.9 0.022
-
 NADP+ pH 8.0, 60°C, mutant enzyme A198S/S199I Sulfurisphaera tokodaii
1.2.1.9 0.0222
-
 NADP+ mutant enzyme A198S/S199I, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 0.023
-
 NADP+ pH 8.0, 60°C, wild-type enzyme Sulfurisphaera tokodaii
1.2.1.9 0.0231
-
 NADP+ wild type enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 0.026
-
 NADP+ pH 8.0, 60°C, mutant enzyme S199I Sulfurisphaera tokodaii
1.2.1.9 0.0263
-
 NADP+ mutant enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 0.0901
-
 NADP+ wild type enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 0.0979
-
 NADP+ mutant enzyme A198S/S199I, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 0.187
-
 NADP+ mutant enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 17.2
-
 NAD+ mutant enzyme A198S/S199I, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 17.2
-
 NAD+ pH 8.0, 60°C, mutant enzyme A198S/S199I Sulfurisphaera tokodaii
1.2.1.9 18.9
-
 NAD+ wild type enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 19.4
-
 NAD+ mutant enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 25.8
-
 NAD+ mutant enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 25.8
-
 NAD+ pH 8.0, 60°C, mutant enzyme S199I Sulfurisphaera tokodaii
1.2.1.9 26.4
-
 NAD+ pH 8.0, 60°C, wild-type enzyme Sulfurisphaera tokodaii
1.2.1.9 26.4
-
 NAD+ wild type enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 29.3
-
 NAD+ mutant enzyme A198S/S199I, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.13 0.18
-
 NADPH wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 50°C Sulfurisphaera tokodaii
1.2.1.13 0.21
-
 DL-glyceraldehyde 3-phosphate wild type enzyme, with NADP+ as cosubstrate, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C Sulfurisphaera tokodaii
1.2.1.13 0.28
-
 NADP+ wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C Sulfurisphaera tokodaii
1.2.1.13 0.61
-
 NADH wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 50°C Sulfurisphaera tokodaii
1.2.1.13 0.77
-
 DL-glyceraldehyde 3-phosphate wild type enzyme, with NAD+ as cosubstrate, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C Sulfurisphaera tokodaii
1.2.1.13 5.8
-
 3-phospho-D-glyceroyl phosphate wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 50°C Sulfurisphaera tokodaii
1.2.1.13 10.7
-
 phosphate wild type enzyme, with NADP+ as cosubstrate, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C Sulfurisphaera tokodaii
1.2.1.13 16.8
-
 NAD+ wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C Sulfurisphaera tokodaii
1.2.1.59 0.18
-
 NADPH pH 8.0, 60°C Sulfurisphaera tokodaii
1.2.1.59 0.21
-
 D-glyceraldehyde 3-phosphate pH 8.0, 60°C, cosubstrate: NADP+ Sulfurisphaera tokodaii
1.2.1.59 0.28
-
 NADP+ pH 8.0, 60°C Sulfurisphaera tokodaii
1.2.1.59 0.77
-
 D-glyceraldehyde 3-phosphate pH 8.0, 60°C, cosubstrate: NAD+ Sulfurisphaera tokodaii
1.2.1.59 5.8
-
 3-phospho-D-glyceroyl phosphate pH 8.0, 60°C Sulfurisphaera tokodaii
1.2.1.59 16.8
-
 NAD+ pH 8.0, 60°C Sulfurisphaera tokodaii
1.2.1.59 107
-
 phosphate pH 8.0, 60°C Sulfurisphaera tokodaii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.9 56000
-
 4 * 56000, SDS-PAGE Sulfurisphaera tokodaii
1.2.1.9 56400
-
 4 * 56400, calculated from amino acid sequence Sulfurisphaera tokodaii
1.2.1.9 56400
-
 4 * 56400, calculated from sequence Sulfurisphaera tokodaii
1.2.1.9 227000
-
 gel filtration Sulfurisphaera tokodaii
1.2.1.13 37500
-
 4 * 37500, calculated from amino acid sequence Sulfurisphaera tokodaii
1.2.1.13 38000
-
 4 * 38000, SDS-PAGE Sulfurisphaera tokodaii
1.2.1.13 148000
-
 gel filtration Sulfurisphaera tokodaii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.9 D-glyceraldehyde 3-phosphate + NAD+ + H2O Sulfurisphaera tokodaii NAD+ is a poor co-substrate 3-phospho-D-glycerate + NADH + H+
-
 ?
1.2.1.9 D-glyceraldehyde 3-phosphate + NADP+ + H2O Sulfurisphaera tokodaii
-
 3-phospho-D-glycerate + NADPH + H+
-
 ir
1.2.1.9 D-glyceraldehyde 3-phosphate + NADP+ + H2O Sulfurisphaera tokodaii
-
 3-phospho-D-glycerate + NADPH + 2 H+
-
 ir
1.2.1.9 D-glyceraldehyde 3-phosphate + NADP+ + H2O Sulfurisphaera tokodaii 7
-
 3-phospho-D-glycerate + NADPH + 2 H+
-
 ir
1.2.1.13 3-phospho-D-glyceroyl phosphate + NADPH + H+ Sulfurisphaera tokodaii
-
 DL-glyceraldehyde 3-phosphate + phosphate + NADP+
-
 r
1.2.1.13 DL-glyceraldehyde 3-phosphate + phosphate + NAD+ Sulfurisphaera tokodaii
-
 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 r
1.2.1.13 DL-glyceraldehyde 3-phosphate + phosphate + NADP+ Sulfurisphaera tokodaii
-
 3-phospho-D-glyceroyl phosphate + NADPH + H+
-
 r
1.2.1.59 3-phospho-D-glyceroyl phosphate + NADPH + H+ Sulfurisphaera tokodaii in the gluconeogenic direction the enzyme is specific for NADPH D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
 r
1.2.1.59 3-phospho-D-glyceroyl phosphate + NADPH + H+ Sulfurisphaera tokodaii 7 in the gluconeogenic direction the enzyme is specific for NADPH D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
 r
1.2.1.59 D-glyceraldehyde 3-phosphate + phosphate + NAD+ Sulfurisphaera tokodaii both NAD+ and NADP+ are utilized in the glycolytic direction 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 r
1.2.1.59 D-glyceraldehyde 3-phosphate + phosphate + NAD+ Sulfurisphaera tokodaii 7 both NAD+ and NADP+ are utilized in the glycolytic direction 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 r
1.2.1.59 D-glyceraldehyde 3-phosphate + phosphate + NADP+ Sulfurisphaera tokodaii both NAD+ and NADP+ are utilized in the glycolytic direction 3-phospho-D-glyceroyl phosphate + NADPH + H+
-
 r
1.2.1.59 D-glyceraldehyde 3-phosphate + phosphate + NADP+ Sulfurisphaera tokodaii 7 both NAD+ and NADP+ are utilized in the glycolytic direction 3-phospho-D-glyceroyl phosphate + NADPH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.9 Sulfurisphaera tokodaii
-
-
-
1.2.1.9 Sulfurisphaera tokodaii Q96XP0
-
-
1.2.1.9 Sulfurisphaera tokodaii 7 Q96XP0
-
-
1.2.1.13 Sulfurisphaera tokodaii
-
-
-
1.2.1.59 Sulfurisphaera tokodaii Q971K2
-
-
1.2.1.59 Sulfurisphaera tokodaii 7 Q971K2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.9
-
 Sulfurisphaera tokodaii
1.2.1.9 HisTrap column chromatography and Superdex 200 gel filtration Sulfurisphaera tokodaii
1.2.1.13 HisTrap column chromatography and Superdex 200 gel filtration Sulfurisphaera tokodaii
1.2.1.59
-
 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 + NAD+ + H2O NAD+ is a poor co-substrate Sulfurisphaera tokodaii 3-phospho-D-glycerate + NADH + H+
-
 ?
1.2.1.9 D-glyceraldehyde 3-phosphate + NAD+ + H2O the enzyme prefers NADP+ to NAD+. NAD+ is a poor cosubstrate. The NAD+-dependent reaction of St-GAPN shows no saturation up to 20 mM Sulfurisphaera tokodaii 3-phospho-D-glycerate + NADH + 2 H+
-
 ir
1.2.1.9 D-glyceraldehyde 3-phosphate + NAD+ + H2O the enzyme prefers NADP+ to NAD+. NAD+ is a poor cosubstrate. The NAD+-dependent reaction of St-GAPN shows no saturation up to 20 mM Sulfurisphaera tokodaii 7 3-phospho-D-glycerate + NADH + 2 H+
-
 ir
1.2.1.9 D-glyceraldehyde 3-phosphate + NADP+ + H2O
-
 Sulfurisphaera tokodaii 3-phospho-D-glycerate + NADPH + H+
-
 ir
1.2.1.9 D-glyceraldehyde 3-phosphate + NADP+ + H2O
-
 Sulfurisphaera tokodaii 3-phospho-D-glycerate + NADPH + 2 H+
-
 ir
1.2.1.9 D-glyceraldehyde 3-phosphate + NADP+ + H2O the enzyme prefers NADP+ to NAD+. NAD+ is a poor cosubstrate. The NAD+-dependent reaction of St-GAPN shows no saturation up to 20 mM. K-type allosterism in which the positive cooperativity is abolished with concomitant activation by D-glucose 1-phosphate Sulfurisphaera tokodaii 3-phospho-D-glycerate + NADPH + 2 H+
-
 ir
1.2.1.9 D-glyceraldehyde 3-phosphate + NADP+ + H2O
-
 Sulfurisphaera tokodaii 7 3-phospho-D-glycerate + NADPH + 2 H+
-
 ir
1.2.1.9 D-glyceraldehyde 3-phosphate + NADP+ + H2O the enzyme prefers NADP+ to NAD+. NAD+ is a poor cosubstrate. The NAD+-dependent reaction of St-GAPN shows no saturation up to 20 mM. K-type allosterism in which the positive cooperativity is abolished with concomitant activation by D-glucose 1-phosphate Sulfurisphaera tokodaii 7 3-phospho-D-glycerate + NADPH + 2 H+
-
 ir
1.2.1.13 3-phospho-D-glyceroyl phosphate + NADPH + H+
-
 Sulfurisphaera tokodaii DL-glyceraldehyde 3-phosphate + phosphate + NADP+
-
 r
1.2.1.13 DL-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Sulfurisphaera tokodaii 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 r
1.2.1.13 DL-glyceraldehyde 3-phosphate + phosphate + NADP+
-
 Sulfurisphaera tokodaii 3-phospho-D-glyceroyl phosphate + NADPH + H+
-
 r
1.2.1.59 3-phospho-D-glyceroyl phosphate + NADPH + H+ in the gluconeogenic direction the enzyme is specific for NADPH Sulfurisphaera tokodaii D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
 r
1.2.1.59 3-phospho-D-glyceroyl phosphate + NADPH + H+ in the gluconeogenic direction the enzyme is specific for NADPH Sulfurisphaera tokodaii 7 D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
 r
1.2.1.59 D-glyceraldehyde 3-phosphate + phosphate + NAD+ both NAD+ and NADP+ are utilized in the glycolytic direction Sulfurisphaera tokodaii 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 r
1.2.1.59 D-glyceraldehyde 3-phosphate + phosphate + NAD+ comparable activity with NADP+ and NAD+ Sulfurisphaera tokodaii 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 r
1.2.1.59 D-glyceraldehyde 3-phosphate + phosphate + NAD+ both NAD+ and NADP+ are utilized in the glycolytic direction Sulfurisphaera tokodaii 7 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 r
1.2.1.59 D-glyceraldehyde 3-phosphate + phosphate + NAD+ comparable activity with NADP+ and NAD+ Sulfurisphaera tokodaii 7 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 r
1.2.1.59 D-glyceraldehyde 3-phosphate + phosphate + NADP+ both NAD+ and NADP+ are utilized in the glycolytic direction Sulfurisphaera tokodaii 3-phospho-D-glyceroyl phosphate + NADPH + H+
-
 r
1.2.1.59 D-glyceraldehyde 3-phosphate + phosphate + NADP+ comparable activity with NADP+ and NAD+ Sulfurisphaera tokodaii 3-phospho-D-glyceroyl phosphate + NADPH + H+
-
 r
1.2.1.59 D-glyceraldehyde 3-phosphate + phosphate + NADP+ both NAD+ and NADP+ are utilized in the glycolytic direction Sulfurisphaera tokodaii 7 3-phospho-D-glyceroyl phosphate + NADPH + H+
-
 r
1.2.1.59 D-glyceraldehyde 3-phosphate + phosphate + NADP+ comparable activity with NADP+ and NAD+ Sulfurisphaera tokodaii 7 3-phospho-D-glyceroyl phosphate + NADPH + H+
-
 r

Subunits

EC Number Subunits Comment Organism
1.2.1.9 homotetramer 4 * 56000, SDS-PAGE Sulfurisphaera tokodaii
1.2.1.9 homotetramer 4 * 56400, calculated from amino acid sequence Sulfurisphaera tokodaii
1.2.1.9 tetramer 4 * 56000, SDS-PAGE Sulfurisphaera tokodaii
1.2.1.9 tetramer 4 * 56400, calculated from sequence Sulfurisphaera tokodaii
1.2.1.13 homotetramer 4 * 38000, SDS-PAGE Sulfurisphaera tokodaii
1.2.1.13 homotetramer 4 * 37500, calculated from amino acid sequence Sulfurisphaera tokodaii

Synonyms

EC Number Synonyms Comment Organism
1.2.1.9 GAP dehydrogenase
-
 Sulfurisphaera tokodaii
1.2.1.9 GAPN
-
 Sulfurisphaera tokodaii
1.2.1.9 non-phosphorylating GAP dehydrogenase
-
 Sulfurisphaera tokodaii
1.2.1.9 St-GAPN
-
 Sulfurisphaera tokodaii
1.2.1.9 STK_24770 locus name Sulfurisphaera tokodaii
1.2.1.13 GAPDH
-
 Sulfurisphaera tokodaii
1.2.1.13 phosphorylating GAP dehydrogenase
-
 Sulfurisphaera tokodaii
1.2.1.59 GAPDH
-
 Sulfurisphaera tokodaii
1.2.1.59 STK_13560 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 Sulfurisphaera tokodaii
1.2.1.9 85
-
-
 Sulfurisphaera tokodaii
1.2.1.13 95
-
-
 Sulfurisphaera tokodaii
1.2.1.59 60
-
 assay at Sulfurisphaera tokodaii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.9 7.5
-
 at 60°C Sulfurisphaera tokodaii
1.2.1.9 8
-
 assay at Sulfurisphaera tokodaii
1.2.1.13 10.5
-
 at 60°C Sulfurisphaera tokodaii
1.2.1.59 8
-
 assay at Sulfurisphaera tokodaii

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.9 NAD+ poor cofactor Sulfurisphaera tokodaii
1.2.1.9 NADP+ preferred cofactor Sulfurisphaera tokodaii
1.2.1.9 NADP+ the enzyme prefers NADP+ to NAD+. NAD+ is a poor co-substrate Sulfurisphaera tokodaii
1.2.1.13 NAD+ the highest activity is almost equal for NADP+ and NAD+, whereas the affinity for NADP+ is higher than that for NAD+ Sulfurisphaera tokodaii
1.2.1.13 NADP+ the highest activity is almost equal for NADP+ and NAD+, whereas the affinity for NADP+ is higher than that for NAD+ Sulfurisphaera tokodaii
1.2.1.13 NADPH in the gluconeogenic direction, the enzyme shows a strong preference for NADPH, and only negligible activity is detected with NADH Sulfurisphaera tokodaii
1.2.1.59 NAD+ comparable activity with NADP+ and NAD+ Sulfurisphaera tokodaii
1.2.1.59 NADP+ comparable activity with NADP+ and NAD+ Sulfurisphaera tokodaii

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.2.1.13 0.035
-
 NADPH wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 50°C Sulfurisphaera tokodaii
1.2.1.13 0.081
-
 NADH wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 50°C Sulfurisphaera tokodaii
1.2.1.13 0.75
-
 NADP+ wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C Sulfurisphaera tokodaii
1.2.1.13 2.8
-
 DL-glyceraldehyde 3-phosphate wild type enzyme, with NAD+ as cosubstrate, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C Sulfurisphaera tokodaii
1.2.1.13 10.7
-
 NAD+ wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C Sulfurisphaera tokodaii
1.2.1.13 13.1
-
 DL-glyceraldehyde 3-phosphate wild type enzyme, with NADP+ as cosubstrate, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C Sulfurisphaera tokodaii
1.2.1.13 49.1
-
 3-phospho-D-glyceroyl phosphate wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 50°C Sulfurisphaera tokodaii
1.2.1.59 0.035
-
 NADPH pH 8.0, 60°C Sulfurisphaera tokodaii
1.2.1.59 0.081
-
 NADPH pH 8.0, 60°C Sulfurisphaera tokodaii
1.2.1.59 0.75
-
 NADP+ pH 8.0, 60°C Sulfurisphaera tokodaii
1.2.1.59 2.8
-
 D-glyceraldehyde 3-phosphate pH 8.0, 60°C, cosubstrate: NAD+ Sulfurisphaera tokodaii
1.2.1.59 10.7
-
 NAD+ pH 8.0, 60°C Sulfurisphaera tokodaii
1.2.1.59 13.1
-
 D-glyceraldehyde 3-phosphate pH 8.0, 60°C, cosubstrate: NADP+ Sulfurisphaera tokodaii
1.2.1.59 49.1
-
 3-phospho-D-glyceroyl phosphate pH 8.0, 60°C Sulfurisphaera tokodaii

Expression

EC Number Organism Comment Expression
1.2.1.9 Sulfurisphaera tokodaii ATP, ADP, AMP, D-glucose 6-phosphate and galactose 1-phosphate exhibit no effect on enzyme activity additional information
1.2.1.9 Sulfurisphaera tokodaii a slight increase in enzyme activity is observed in the presence of D-fructose 6-phosphate and coenzyme A (1.1fold) up
1.2.1.13 Sulfurisphaera tokodaii ATP, ADP, AMP, D-glucose 6-phosphate and galactose 1-phosphate exhibit no effect on enzyme activity additional information
1.2.1.13 Sulfurisphaera tokodaii a slight increase in enzyme activity is observed in the presence of D-fructose 6-phosphate and coenzyme A (1.1fold) up

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.2.1.9 0.378
-
 NAD+ pH 8.0, 60°C, wild-type enzyme Sulfurisphaera tokodaii
1.2.1.9 0.378
-
 NAD+ wild type enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 0.434
-
 NAD+ mutant enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 0.434
-
 NAD+ pH 8.0, 60°C, mutant enzyme S199I Sulfurisphaera tokodaii
1.2.1.9 0.637
-
 NAD+ wild type enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 0.639
-
 NAD+ mutant enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 1
-
 NAD+ mutant enzyme A198S/S199I, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 1
-
 NAD+ pH 8.0, 60°C, mutant enzyme A198S/S199I Sulfurisphaera tokodaii
1.2.1.9 1.63
-
 NAD+ mutant enzyme A198S/S199I, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 48.1
-
 NADP+ mutant enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 48.1
-
 NADP+ pH 8.0, 60°C, mutant enzyme S199I Sulfurisphaera tokodaii
1.2.1.9 61.5
-
 NADP+ mutant enzyme A198S/S199I, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 61.5
-
 NADP+ pH 8.0, 60°C, mutant enzyme A198S/S199I Sulfurisphaera tokodaii
1.2.1.9 71.4
-
 NADP+ mutant enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 96.6
-
 NADP+ pH 8.0, 60°C, wild-type enzyme Sulfurisphaera tokodaii
1.2.1.9 96.6
-
 NADP+ wild type enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 188
-
 NADP+ mutant enzyme A198S/S199I, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii
1.2.1.9 203
-
 NADP+ wild type enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C Sulfurisphaera tokodaii