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Literature summary for 2.5.1.54 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)

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

Protein Variants

Protein Variants Comment Organism
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]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus Q8U0A9
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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
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

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

Temperature Optimum [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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]

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

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
6 9 at pH 9.0 the activity is about 60% of the activity at pH 6.0, wid-type enzyme Pyrococcus furiosus
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

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

kcat/KM [mM/s]

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