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EC Tree
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae 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, dah7p, 3-deoxy-d-arabinoheptulosonate 7-phosphate synthase,
more
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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 synthase
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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 (phe)
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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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deoxy-D-arabino-heptulosonate-7-phosphate 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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DAHP synthase
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
simultaneous presence of a metal ion and phosphoenolpyruvate result in an ordering of the protein into a conformation that is prepared for binding the second substrate erythrose 4-phosphate. Initial step of reaction is a nucleophilic attack of the double bond of phosphoenolpyruvate on the metal-activated carbonyl group of erythrose 4-phosphate
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
sequential mechanism
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phosphoenolpyruvate:D-erythrose-4-phosphate C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming)
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
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Fe2+
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contains 0.6 mol of iron per mol of enzyme
additional information
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Tyr-sensitive isozyme, metal factor required
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additional information
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not inhibited by tryptophan
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EDTA
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Co2+, Mn2+, Zn2+ and Fe2+ restore activity
EDTA
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phosphoenolpyruvate, 2 mM, partially protects from inactivation, does not restore activity
EDTA
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Co2+, Zn2+, Cu2+, and Fe3+ restore activity
L-tyrosine
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L-tyrosine
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almost complete inhibition at 0.5 mM
Phe
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Phe-sensitive isozyme
Phe
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Tyr-sensitive isozyme is less inhibited than the Phe-sensitive isozyme
Phe
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competitive with respect to D-erythrose 4-phosphate and non-competitive to phosphoenolpyruvate
Tyr
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Tyr-sensitive isozyme
Tyr
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noncompetitive with respect to D-erythrose 4-phosphate, competitive with respect to phosphoenolpyruvate
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0.13 - 0.5
D-erythrose 4-phosphate
0.018 - 0.125
phosphoenolpyruvate
0.13
D-erythrose 4-phosphate
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Phe-sensitive isozyme, pH 6.8, 30°C
0.5
D-erythrose 4-phosphate
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Tyr-sensitive isozyme, pH 6.8
0.018
phosphoenolpyruvate
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Phe-sensitive isozyme, pH 6.8, 30°C
0.125
phosphoenolpyruvate
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Tyr-sensitive isozyme, pH 6.8
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0.0009
Tyr
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Tyr-sensitive isozyme, pH 6.8
0.01
Phe
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Phe-sensitive isozyme, pH 6.8, 30°C
0.27
Phe
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Tyr-sensitive isozyme, pH 6.8
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8.24
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purified recombinant Tyr-sensitive isozyme
additional information
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Uniprot
brenda
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42000
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x * 42000, Tyr-sensitive isozyme, SDS-PAGE
42130
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1 * 42130, calculation from nucleotide sequence
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?
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x * 42000, Tyr-sensitive isozyme, SDS-PAGE
monomer
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1 * 42130, calculation from nucleotide sequence
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Tyr-sensitive isozyme, hanging drop vapour diffusion method, protein solution in 1:1 mixture with precipitant, 0.004 ml, + 1 ml precipitant solution: 1. 50 mM KH2PO4, 20% polyethylene glycol 8000 w/v or 2. 0.1 M Tris, pH 9.0, 10 mM NiCl2, 20% polyethylene glycol monomethylester 2000 w/v, room temperature for 3 days, X-ray diffraction structure analysis, usage of cryoprotectant glycerol for investigations
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K229L
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the mutation eliminates the L-tyrosine sensitivity
P165G
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inhibited by tryptophan
Q302R
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inhibited by tryptophan
S195A
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inhibited by tryptophan
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-20°C, 50% glycerol, stable for at least 4 weeks
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Phe-sensitive isozyme, 11fold to homogeneity from overproducing strain
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recombinantly overexpresed Tyr-sensitive isozyme, 7.5fold
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ARO3 gene, expression in deficient strain and in Escherichia coli strain JA196
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ARO4 gene, tyrosine-sensitive isozyme, overexpression from plasmid in strain RH1326
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Teshiba, S.; Furter, R.; Niederberger, P.; Braus, G.; Paravicini, G.; Htter, R.
Cloning of the ARO3 gene of Saccharomyces cerevisiae and its regulation
Mol. Gen. Genet.
205
353-357
1986
Saccharomyces cerevisiae
brenda
Schnappauf, G.; Hartmann, M.; Knzler, M.; Braus, G.H.
The two 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase isoenzymes from Saccharomyces cerevisiae show different kinetic modes of inhibition
Arch. Microbiol.
169
517-524
1998
Saccharomyces cerevisiae
brenda
Paravicini, G.; Schmidheini, T.; Braus, G.
Purification and properties of the 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (phenylalanine-inhibitable) of Saccharomyces cerevisiae
Eur. J. Biochem.
186
361-366
1989
Saccharomyces cerevisiae
brenda
Schneider, T.R.; Hartmann, M.; Braus, G.H.
Crystallization and preliminary X-ray analysis of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (tyrosine inhibitable) from Saccharomyces cerevisiae
Acta Crystallogr. Sect. D
55
1586-1588
1999
Saccharomyces cerevisiae, Saccharomyces cerevisiae RH1326
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brenda
Konig, V.; Pfeil, A.; Braus, G.H.; Schneider, T.R.
Substrate and metal complexes of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Saccharomyces cerevisiae provide new insights into the catalytic mechanism
J. Mol. Biol.
337
675-690
2004
Saccharomyces cerevisiae (P32449), Saccharomyces cerevisiae
brenda
Helmstaedt, K.; Strittmatter, A.; Lipscomb, W.N.; Braus, G.H.
Evolution of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase-encoding genes in the yeast Saccharomyces cerevisiae
Proc. Natl. Acad. Sci. USA
102
9784-9789
2005
Saccharomyces cerevisiae
brenda
Luttik, M.A.; Vuralhan, Z.; Suir, E.; Braus, G.H.; Pronk, J.T.; Daran, J.M.
Alleviation of feedback inhibition in Saccharomyces cerevisiae aromatic amino acid biosynthesis: quantification of metabolic impact
Metab. Eng.
10
141-153
2008
Saccharomyces cerevisiae
brenda