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Information on EC 2.5.1.54 - 3-deoxy-7-phosphoheptulonate synthase and Organism(s) Pyrococcus furiosus and UniProt Accession Q8U0A9

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Pyrococcus furiosus
UNIPROT: Q8U0A9 not found.
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The taxonomic range for the selected organisms is: Pyrococcus furiosus
The enzyme appears in selected viruses and cellular organisms
Synonyms
dahp synthase, dahps, dah7ps, 3-deoxy-d-arabino-heptulosonate-7-phosphate synthase, ds-co, ds-mn, dah7p synthase, dahp synthase-phe, 3-deoxy-d-arabinoheptulosonate 7-phosphate synthase, dah7p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-deoxy-D-arabino-heptulosonate-7-phosphate synthase
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PF1690
locus name
2-dehydro-3-deoxy-D-arabino-heptonate-7-phosphate D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating)
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2-dehydro-3-deoxy-phosphoheptanoate aldolase
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2-dehydro-3-deoxy-phosphoheptonate aldolase
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2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase
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3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase
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3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase
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3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase
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3-deoxy-D-arabino-heptulosonate-7-phosphate synthase
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7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating)
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7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate lyase (pyruvate-phosphorylating)
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aldolase, phospho-2-keto-3-deoxyheptanoate
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D-erythrose-4-phosphate-lyase
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D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating)
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DAH7-P synthase
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DAH7-P synthase (phe)
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DAHP synthase
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DAHP synthase-phe
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DAHP synthase-trp
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DAHP synthase-tyr
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DAHP(Phe)
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deoxy-D-arabino-heptulosonate-7-phosphate synthetase
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KDPH synthase
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KDPH synthetase
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phospho-2-dehydro-3-deoxyheptonate aldolase
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phospho-2-keto-3-deoxyheptanoate aldolase
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Phospho-2-keto-3-deoxyheptonate aldolase
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phospho-2-keto-3-deoxyheptonic aldolase
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phospho-2-oxo-3-deoxyheptonate aldolase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
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-
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SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate:D-erythrose-4-phosphate C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9026-94-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + 2-deoxy-D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + 2-deoxy-D-ribose 5-phosphate + H2O
3,5-dideoxy-D-gluco-octulosonate 8-phosphate + 3,5-dideoxy-D-manno-octulosonate 8-phosphate + phosphate
show the reaction diagram
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-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
show the reaction diagram
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-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
phosphoenolpyruvate + D-ribose 5-phosphate + H2O
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
show the reaction diagram
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-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
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-
-
-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
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assay with 0.1 mM
additional information
-
EDTA-inactivated enzyme, restoration in decreasing order of effectiveness by Zn2+, Cd2+, Mn2+, Co2+, Ni2+, Ca2+, Hg2+, Cu2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
inactivation, restoration in decreasing order of effectiveness by Zn2+, Cd2+, Mn2+, Co2+, Ni2+, Ca2+, Hg2+, Cu2+
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
2-deoxy-D-erythrose 4-phosphate
pH 6.8, 60°C
2.5
2-deoxy-D-ribose 5-phosphate
pH 6.8, 60°C
2.7
D-arabinose 5-phosphate
pH 6.8, 60°C
0.009 - 0.092
D-erythrose 4-phosphate
1.58
D-ribose 5-phosphate
pH 6.8, 60°C
0.033 - 0.112
phosphoenolpyruvate
0.028
D-erythrose 4-phosphate
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60°C, pH 6.8
0.12
phosphoenolpyruvate
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60°C, pH 6.8
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.5 - 14.9
D-erythrose 4-phosphate
1.12 - 14.9
phosphoenolpyruvate
1.5
phosphoenolpyruvate
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60°C, pH 6.8
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21 - 60
D-erythrose 4-phosphate
0.22 - 49
phosphoenolpyruvate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved in shikimate biosynthesis pathway
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
109000
sedimentation equilibrium experiments, tetrameric enzyme
111000
gel filtration, tetrameric enzyme
29224
-
2 * 29226, ESI-MS, 2 * 29224, calculated
29226
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2 * 29226, ESI-MS, 2 * 29224, calculated
5700
-
gel filtration
58450
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ESI-MS
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
although the enzyme crystallizes as a tetramer, equilibrium exists between tetrameric and dimeric forms with a dissociation constant of 0.022 mM
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
dimer
-
2 * 29226, ESI-MS, 2 * 29224, calculated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion, ctystal structure of wild-type enzyme and mutant enzyme I181D
recombinant enzyme, in complex with phosphoenolpyruvate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
60
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30 min, presence of phosphoenolpyruvate, stable
70
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30 min, presence of phosphoenolpyruvate, stable
95
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presence of 0.1 mM Mn2+, 130 min, 50% residual activity, absence of Mn2+, 3 min, 50% residual activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
resistant to denaturation by sodium dodecyl sulfate
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
EDTA-inactivated enzyme, restoration in decreasing order of effectiveness by Zn2+, Cd2+, Mn2+, Co2+, Ni2+, Ca2+, Hg2+, Cu2+
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schofield, L.R.; Anderson, B.F.; Patchett, M.L.; Norris, G.E.; Jameson, G.B.; Parker, E.J.
Substrate ambiguity and crystal structure of Pyrococcus furiosus 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase: an ancestral 3-deoxyald-2-ulosonate-phosphate synthase?
Biochemistry
44
11950-11962
2005
Pyrococcus furiosus (Q8U0A9), Pyrococcus furiosus
Manually annotated by BRENDA team
Schofield, L.R.; Patchett, M.L.; Parker, E.J.
Expression, purification, and characterization of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Pyrococcus furiosus
Protein Expr. Purif.
34
17-27
2004
Pyrococcus furiosus
Manually annotated by BRENDA team
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
J. Mol. Biol.
426
656-673
2014
Pyrococcus furiosus (Q8U0A9), Pyrococcus furiosus
Manually annotated by BRENDA team