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Literature summary extracted from

  • Nazmi, A.R.; Schofield, L.R.; Dobson, R.C.; Jameson, G.B.; Parker, E.J.
    Destabilization of the homotetrameric assembly of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from the hyperthermophile Pyrococcus furiosus enhances enzymatic activity (2014), J. Mol. Biol., 426, 656-673.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.54 hanging-drop vapor diffusion, ctystal structure of wild-type enzyme and mutant enzyme I181D Pyrococcus furiosus

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.54 I181D mutant enzyme is catalytically more active than the wild type enzyme from 20 to 80°C, the mutation disrupts the tetrameric structure of the enzyme, the melting temperatures of the wild-type protein are significantly higher than the melting temperatures of mutant enzyme I181D at pH values greater than 6.5 Pyrococcus furiosus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.54 0.066
-
 phosphoenolpyruvate pH 7.5, 60°C, mutant enzyme I181D Pyrococcus furiosus
2.5.1.54 0.071
-
 D-erythrose 4-phosphate pH 7.5, 60°C, mutant enzyme I181D Pyrococcus furiosus
2.5.1.54 0.092
-
 D-erythrose 4-phosphate pH 7.5, 60°C, wild-type enzyme Pyrococcus furiosus
2.5.1.54 0.112
-
 phosphoenolpyruvate pH 7.5, 60°C, wild-type enzyme Pyrococcus furiosus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.54 109000
-
 sedimentation equilibrium experiments, tetrameric enzyme Pyrococcus furiosus
2.5.1.54 111000
-
 gel filtration, tetrameric enzyme Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.54 Pyrococcus furiosus Q8U0A9
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.54 phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
-
 Pyrococcus furiosus 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.54 dimer although the enzyme crystallizes as a tetramer, equilibrium exists between tetrameric and dimeric forms with a dissociation constant of 0.022 mM Pyrococcus furiosus
2.5.1.54 tetramer at pH 7.5 and 20°C, the wild-type enzyme is present as a tetramer in solution. Although the enzyme crystallizes as a tetramer, equilibrium exists between tetrameric and dimeric forms with a dissociation constant of 0.022 mM Pyrococcus furiosus

Synonyms

EC Number Synonyms Comment Organism
2.5.1.54 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase
-
 Pyrococcus furiosus
2.5.1.54 DAH7PS
-
 Pyrococcus furiosus
2.5.1.54 PF1690 locus name Pyrococcus furiosus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.54 60
-
 assay at Pyrococcus furiosus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.5.1.54 98
-
 melting temperature of the wild-type enzyme by differential scanning calorimetry at a protein monomer concentration of 0.034 mM and a pH of 7.5 Pyrococcus furiosus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.54 5.5
-
 phosphoenolpyruvate pH 7.5, 60°C, wild-type enzyme Pyrococcus furiosus
2.5.1.54 5.5
-
 D-erythrose 4-phosphate pH 7.5, 60°C, wild-type enzyme Pyrococcus furiosus
2.5.1.54 14.9
-
 phosphoenolpyruvate pH 7.5, 60°C, mutant enzyme I181D Pyrococcus furiosus
2.5.1.54 14.9
-
 D-erythrose 4-phosphate pH 7.5, 60°C, mutant enzyme I181D Pyrococcus furiosus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.54 7.5
-
 assay at Pyrococcus furiosus
2.5.1.54 7.5
-
 mutant enzyme I181D Pyrococcus furiosus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.5.1.54 6 9 at pH 9.0 the activity is about 60% of the activity at pH 6.0, wid-type enzyme Pyrococcus furiosus
2.5.1.54 6 9 pH 6.0: about 55% of maximal activity, pH 9.0: about 35% of maximal activity, mutant enzyme I181D Pyrococcus furiosus

General Information

EC Number General Information Comment Organism
2.5.1.54 physiological function the enzyme is involved in shikimate biosynthesis pathway Pyrococcus furiosus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.5.1.54 0.21
-
 D-erythrose 4-phosphate pH 7.5, 60°C, mutant enzyme I181D Pyrococcus furiosus
2.5.1.54 0.22
-
 phosphoenolpyruvate pH 7.5, 60°C, mutant enzyme I181D Pyrococcus furiosus
2.5.1.54 49
-
 phosphoenolpyruvate pH 7.5, 60°C, wild-type enzyme Pyrococcus furiosus
2.5.1.54 60
-
 D-erythrose 4-phosphate pH 7.5, 60°C, wild-type enzyme Pyrococcus furiosus