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Information on EC 2.5.1.54 - 3-deoxy-7-phosphoheptulonate synthase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P32449

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Saccharomyces cerevisiae
UNIPROT: P32449 not found.
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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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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DAH7-P synthase (phe)
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DAHP synthase
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
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
show the reaction diagram
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
show the reaction diagram
sequential mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
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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 + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-tyrosine
additional information
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not inhibited by tryptophan
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13 - 0.5
D-erythrose 4-phosphate
0.018 - 0.125
phosphoenolpyruvate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.27
Phe
0.0009
Tyr
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Tyr-sensitive isozyme, pH 6.8
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.24
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purified recombinant Tyr-sensitive isozyme
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
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x * 42000, Tyr-sensitive isozyme, SDS-PAGE
42130
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1 * 42130, calculation from nucleotide sequence
53000
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gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 42000, Tyr-sensitive isozyme, SDS-PAGE
monomer
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1 * 42130, calculation from nucleotide sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% glycerol, stable for at least 4 weeks
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Phe-sensitive isozyme, 11fold to homogeneity from overproducing strain
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recombinantly overexpresed Tyr-sensitive isozyme, 7.5fold
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Tyr-sensitive isozyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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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Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team