Information on EC 2.5.1.54 - 3-deoxy-7-phosphoheptulonate synthase and Organism(s) Escherichia coli and UniProt Accession P0AB91

a mononuclear iron enzyme, the enzyme required divalent metal cations, Fe2+ activates best, iron is the prosthetic metal in vivo

Mn2+

can substitute for Fe2+, activates DAHP synthase to about 70% of the iron-activated sample

Zn2+

cannot well substitute for Fe2+, activates DAHP synthase to about 20% of the iron-activated sample

Cd2+

-

activates, Tyr-sensitive isozyme

Co2+

Cu2+

Fe2+

Mg2+

-

activates, Tyr-sensitive isozyme

Mn2+

7 entries

Zn2+

5 entries

additional information

D-erythrose 4-phosphate

Phe-sensitive isozyme: in absence of phosphoenolpyruvate the enzyme is inhibited via formation of a covalent binding to Lys186 via a slow Schiff base reaction, mechanism

H2O2

DAHP synthase enzymes are inactivated by H2O2 in vitro and in vivo, H2O2 displaces the iron atom from the enzyme, only the Fe2+-metalloform of the enzyme can be inactivated by hydrogen peroxide or superoxide

L-tyrosine

feedback inhibition

Phe

Phe-sensitive isozyme

superoxide

displaces the iron atom from the enzyme, only the Fe2+-metalloform of the enzyme can be inactivated by hydrogen peroxide or superoxide. Superoxide stress promotes the mismetallation of DAHP synthase

(2R)-2-(phosphonooxy)propanoic acid

-

mimicking phosphohemiketal 2 (instable), competitive to substrate phosphoenolpyruvate

(2S)-2-(phosphonooxy)propanoic acid

-

mimicking phosphohemiketal 2 (instable), competitive to substrate phosphoenolpyruvate

(2Z)-3-phosphono-2-(trifluoromethyl)prop-2-enoic acid

-

trifluorinated phosphonate

(E)-2-methyl-3-phosphonoacrylic acid

-

most potent of the tested inhibitors mimicking intermediates in the reaction, vinyl phosphonate 4

1,10-phenanthroline

-

activity is restored by Fe2+ or Zn2+

2,3-bisphosphoglycerate

-

2-(phosphonomethyl)prop-2-enoic acid

-

mimics substrate phosphoenolpyruvate, and should be inert due to alkene structure but lacking an electron-donor, acts as competitive inhibitor

2-phosphoglycerate

-

competitive with respect to phosphoenolpyruvate

3-deoxy-D-arabino-heptonic acid 7-phosphate

-

3-deoxy-D-arabinoheptulosonate-7-phosphate oxime

3 entries

3-Methylphosphoenolpyruvate

-

3-Propylphosphoenolpyruvate

-

5,5'-dithiobis(2-nitrobenzoate)

-

alpha-Methylphenylalanine

-

beta-2-Thienyl-D,L-Ala

-

beta-phenylserine

-

beta-Thienylalanine

-

CN-

-

Tyr-sensitive isozyme, strong inhibition, reactivation by divalent cations only to a small extent

Cu2+

3 entries

D-fructose 1,6-diphosphate

-

D-sedoheptulose 1,7-diphosphate

-

D-sedoheptulose 7-phosphate

-

diethyl dicarbonate

-

Phe-sensitive isozyme, pH-dependent, phosphoenolpyruvate protects wild-type and mutants H64G, H207G, H304G

dihydroxyphenylalanine

-

EDTA

Fe2+

fosmidomycin

-

uncompetitive inhibitor, maximum level of inhibition after 10 min incubation, extent of inhibition dependent on the type of the metal cofactor, competitive inhibitor with respect to phosphoenolpyruvate

L-tyrosine

-

m-Chlorophenylalanine

-

m-Fluorophenylalanine

-

m-hydroxyphenylalanine

-

N-bromosuccinimide

-

N-ethylmaleimide

-

o-chlorophenylalanine

-

o-Fluorophenylalanine

-

o-hydroxyphenylalanine

-

p-aminophenylalanine

-

p-chloromercuribenzoate

-

complete inhibition at 0.02 mM, reversible by cysteine

p-Fluorophenylalanine

-

Phe

phenylalanine

-

1 Mn, wild-type 8.2% residual activity

phosphate

-

non-competitive with respect to both phosphoenolpyruvate and D-erythrose 4-phosphate

tetraammonium (((carboxymethyl)[(2S,3R,4S)-2,3,4-trihydroxy-5-(phosphonatooxy)pentyl]amino)methyl)phosphonate

-

IC50: 0.0066 mM

672596

Tetranitromethane

-

Trinitrobenzene sulfonate

-

Trp

-

Trp-sensitive isozyme

639767

Tyr

6 entries

[(1E)-7-bromo-2-carboxyhept-1-en-1-yl]phosphonate

-

inhibitor based on vinyl phosphonate, designed to fit into the binding sites of both phosphoenolpyruvate and D-erythrose 4-phosphate substrates simultaneously. Competitive with respect to phosphoenolpyruvate

[2-carboxy-7-(phosphonatooxy)hept-1-en-1-yl]phosphonate

-

inhibitor based on vinyl phosphonate ratio Z:E enantiomer 1:1. Inhibitor is designed to fit into the binding sites of both phosphoenolpyruvate and D-erythrose 4-phosphate substrates simultaneously. Competitive with respect to phosphoenolpyruvate

[2-carboxy-7-(phosphonatooxy)hept-2-en-1-yl]phosphonate

-

inhibitor based on allyl phosphonate, ratio Z:E enantiomer 7:3. Inhibitor is designed to fit into the binding sites of both phosphoenolpyruvate and D-erythrose 4-phosphate substrates simultaneously. Competitive with respect to phosphoenolpyruvate

additional information

6 entries

-

2-mercaptoethanol

-

activates

additional information

-

2 - 21

phosphoenolpyruvate

3 entries

0.65

(3S)-2-deoxyerythrose 4-phosphate

-

pH 6.8

672576

6.8

2-deoxyribose 5-phosphate

-

recombinant enzyme, pH 7.5, 25°C

0.03

D-arabinose 5-phosphate

-

recombinant enzyme, pH 7.5, 25°C

0.015 - 52.36

D-erythrose 4-phosphate

12 entries

0.005 - 12.25

phosphoenolpyruvate

15 entries

6

ribose 5-phosphate

-

recombinant enzyme, pH 7.5, 25°C

additional information

6 entries

-

71

D-erythrose 4-phosphate

Phe-sensitive isozyme, pH 6.8, 25°C

71

phosphoenolpyruvate

Phe-sensitive isozyme, pH 6.8, 25°C

0.233

(3S)-2-deoxyerythrose 4-phosphate

-

pH 6.8

672576

1.183 - 122

D-erythrose 4-phosphate

5 entries

4.2 - 122

phosphoenolpyruvate

10 entries

0.049

(2R)-2-(phosphonooxy)propanoic acid

-

buffer bis-tris-propane, 50 mM, pH 6.8, Mn2+, UV-visible spectroscopy at 232 nm, substrates phosphoenolpyruvate and D-erythrose 4-phosphate

0.67

(2S)-2-(phosphonooxy)propanoic acid

-

buffer bis-tris-propane, 50 mM, pH 6.8, Mn2+, UV-visible spectroscopy at 232 nm, substrates phosphoenolpyruvate and D-erythrose 4-phosphate

0.0088

(2Z)-3-phosphono-2-(trifluoromethyl)prop-2-enoic acid

-

buffer bis-tris-propane, 50 mM, pH 6.8, Mn2+, UV-visible spectroscopy at 232 nm, substrates phosphoenolpyruvate and D-erythrose 4-phosphate

0.0047

(E)-2-methyl-3-phosphonoacrylic acid

-

buffer bis-tris-propane, 50 mM, pH 6.8, Mn2+, UV-visible spectroscopy at 232 nm, substrates phosphoenolpyruvate and D-erythrose 4-phosphate

0.27

2-(phosphonomethyl)prop-2-enoic acid

-

buffer bis-tris-propane, 50 mM, pH 6.8, Mn2+, UV-visible spectroscopy at 232 nm, substrates phosphoenolpyruvate and D-erythrose 4-phosphate

0.0015

3-deoxy-D-arabinoheptulosonate-7-phosphate oxime

pH 7., 25°C

758795

0.035

fosmidomycin

-

buffer bis-tris-propane, 50 mM, pH 6.8, Mn2+, UV-visible spectroscopy at 232 nm, substrates phosphoenolpyruvate and D-erythrose 4-phosphate

0.02

Tyr

-

pH 7.0, 24°C

additional information

-

-

0.0066

tetraammonium (((carboxymethyl)[(2S,3R,4S)-2,3,4-trihydroxy-5-(phosphonatooxy)pentyl]amino)methyl)phosphonate

Escherichia coli

-

IC50: 0.0066 mM

672596

0.0036

[(1E)-7-bromo-2-carboxyhept-1-en-1-yl]phosphonate

Escherichia coli

-

pH not specified in the publication, temperature not specified in the publication

0.0053

[2-carboxy-7-(phosphonatooxy)hept-1-en-1-yl]phosphonate

Escherichia coli

-

pH not specified in the publication, temperature not specified in the publication

0.154

[2-carboxy-7-(phosphonatooxy)hept-2-en-1-yl]phosphonate

Escherichia coli

-

pH not specified in the publication, temperature not specified in the publication

0.29

-

N-terminal deletion mutant, 37°C, pH 6.4

0.4

-

partially purified enzyme

0.81

-

mutant W215A, 37°C, pH 6.4

0.92

-

mutant I10A, 37°C, pH 6.4

1.97

-

mutant N5K, 37°C, pH 6.4

13.1

-

2.1

-

purified enzyme

2.37

-

mutant V221A, 37°C, pH 6.4

2.7

-

wild-type, 37°C, pH 6.4

2.81

22

-

purified recombinant Tyr-sensitive isozyme, with Cd2+

3.07

-

mutant F144A, 37°C, pH 6.4

3.25

-

mutant F209A, 37°C, pH 6.4

3.6

-

mutant L175Q, 37°C, pH 6.4

30 - 40

-

purified Tyr-sensitive isozyme, wild-type and mutant N8K

4.25

-

mutant L175A, 37°C, pH 6.4

4.46

-

mutant L175D, 37°C, pH 6.4

56

-

purified enzyme

67

-

purified enzyme

82.6

-

purified enzyme

additional information

6.4

assay at

6.8

assay at

6.4

-

6.5 - 7

-

6.8

7

-

639746, 639747, 639749

7 - 7.5

-

recombinant Tyr-sensitive isozyme

8

-

above, Phe-sensitive iaozyme mutant C61G

additional information

-

Tyr-sensitive isozyme, pIs: 6.1 and 8.9

5.7 - 8.5

-

pH 5.7: about 25% of maximal activity, pH 8.5: about 30% of maximal activity

6 - 8.5

-

pH 6.0: about 65% of maximal activity, pH 8.5: about 50% of maximal activity

25

assay at

37

assay at

24

-

assay at

25

-

assay at

639768, 639771, 639789

30

-

assay at

37

-

assay at

639741, 639747, 639749

evolution

DAHP synthase belongs to a family of mononuclear iron-containing enzymes that are disabled by oxidative stress

metabolism

physiological function

expression of wild-type enzyme and phenylalanine-feedback insensitive mutant L175Q in Arabidopsis thaliana. Transgenic plants have comparable phenotypes and are fully fertile. The levels of shikimate, prephenate and Phe are higher in the different lines expressing the mutant enzyme than in the lines expressing the natural feedback-sensitive bacterial enzyme, and the control plants. Results imply that the bacterial enzyme is active in the transgenic plants and, similar to its operation in bacteria, the feedback insensitivity trait of the mutant enzyme is fundamental for enhancement of the flow of primary carbon metabolites via the shikimate pathway into the production of aromatic amino acids also in the plant

metabolism

105000

-

strain JP401, gel filtration

110000

136000

-

equilibrium sedimentation

140000

-

gel filtration and sedimentation equilibrium analysis

33000

-

x * 33000, SDS-PAGE

35000

-

4 * 35000, Phe-sensitive isozyme, SDS-PAGE

39000

66000

-

gel filtration

69000

-

gel filtration

71000

-

Tyr-sensitive isozyme, mutant N8K, gel filtration

75000

-

Tyr-sensitive isozyme, wild-type, gel filtration

77000

sedimentation velocity data, apo protein

78000

sedimentation velocity data, in complex with tyrosine

?

x * 38009-38014, Phe-sensitive isozyme, electron mass spectroscopy and amino acid sequence determination

dimer

mutant E24Q, crystallization data

tetramer

wild-type, crystallization data

?

dimer

tetramer

-

4 * 35000, Phe-sensitive isozyme, SDS-PAGE

additional information

5 entries

native and selenomethionine-substituted protein, in complex with phosphoenolpyruvate and Mn2+, mutant E24Q in complex with phosphoenolpyruvate and Mn2+

Phe-sensitive isozyme, enzyme-Mn2+-2-phosphoglycolate-complexes, hanging drop vapour diffusion method, room temperature, all solutions, except the MnSO4 and the enzyme solution, are treated with Chelex-100 to remove metals, 0.2 mM enzyme subunit solution: 0.37 MnSO4, 4.2 mM 2-phosphoglycolate, 0.1 M Li2SO4, 12% PEG 100 w/v, 20% ethanol v/v, 50 mM 1,3-bis[tris(hydroxy-methyl)methylamino]propane buffer, pH 8.7, reservoir solution: 19% PEG 1000, 0.1 M Li2SO4, 20% ethanol v/v, 50 mM 1,3-bis[tris(hydroxy-methyl)methylamino]propane buffer, X-ray diffraction structure determination and analysis

639788

in complex with inhibitor 3-deoxy-D-arabinoheptulosonate-7-phosphate oxime

758795

Phe-sensitive isozyme, hanging drop vapour diffusion method, 22°C, with or without inhibitor phenylalanine, at pH 6.3-9.4, 0.1-0.2 M monovalent cations, PEG 1000-4000, 0.01 ml protein solution + 0.3 ml precipitant solution, X-ray diffraction structure determination and analysis

-

639776

structures of apo form and complex with the inhibitor tyrosine at 2.5 and 2.0 A resolutions, respectively. DAHPS(Tyr) has a typical (beta/alpha)8 TIM barrel, which is decorated with an N-terminal extension and an antiparallel beta sheet. Inhibitor tyrosine binds at a cavity formed by residues of helices alpha3, alpha4, strands beta6a, beta6b and the adjacent loops, and directly interacts with residues P148, Q152, S181, I213 and N8*. Conformational changes of residues P148, Q152 and I213 initiate a transmission pathway to propagate the allosteric signal from the tyrosine-binding site to the active site

E24Q

unlike tetrameric enzyme, mutant is dimeric in solution

L175Q

phenylalanine-feedback-insensitive mutant

C328V

-

oligo-nucleotide mutagenesis, expression in Escherichia coli strains, 20% reduction in the catalytic constant, 2-3fold increase in Km for the substrates, completely resistant to both spontaneous and Cu2+-catalysed inactivation

C61A

DAHP oxime binding is noncompetitive with respect to Mn2+

C61G

-

site-directed mutagenesis, highly reduced activity, highly increased Km for phosphoenolpyruvate, higher pH-optimum than the wild-type

C61V

-

oligo-nucleotide mutagenesis, expression in Escherichia coli strains, inactive, does not bind metal ions, resistant to metal attack, no subunit dissociation upon Cu2+ treatment

D326A

DAHP oxime binding is noncompetitive with respect to Mn2+

DELTA1-15

-

N-terminal deletion of amino acids 1-15, no formation of dimeric form

659072

F144A

-

inhibition by phenylalanine, 30% residual activity

F209A

-

inhibition by phenylalanine, 79% residual activity

H172G

-

site-directed mutagenesis, inactive

H207G

-

site-directed mutagenesis, reduced activity, increased Km values for the substrates, reduced kcat

H268A

DAHP oxime binding is competitive with respect to Mn2+

H268G

-

site-directed mutagenesis, inactive

H304G

-

site-directed mutagenesis, reduced activity, increased Km values for the substrates, increased kcat

H64G

-

site-directed mutagenesis, reduced activity, increased Km values for the substrates, increased kcat

H64L

-

oligo-nucleotide mutagenesis, expression in Escherichia coli strains, unstable to treatment with phosphoenolpyruvate, half-life of about 24 h at 0.4 mM compared to 6 days for the wild-type

I10A

I213P

overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type

L175A

-

inhibition by phenylalanine, 18% residual activity

L175D

-

inhibition by phenylalanine, 83% residual activity

L175Q

-

inhibition by phenylalanine, 44% residual activity

L179A

-

inhibition by phenylalanine, 82% residual activity

N5K

N8A

overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type

N8K

-

similar activity and substrate affinities like the wild-type, but insensitive against inhibition by tyrosine, decreased thermostability

P148A

overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type

P150L

-

inhibition by phenylalanine, no inhibition by phenylalanine

Q152A

overexpression of variant leads to higher accumulation of phenylalanine

S181A

overexpression of variant leads to higher accumulation of phenylalanine

V221A

-

inhibition by phenylalanine, 95% residual activity

W215A

-

inhibition by phenylalanine, 58% residual activity

additional information

4 entries

22

-

half-life: 1.2 days in absence of phosphoenolpyruvate, half-life: 4 days in presence of 1 mM phosphoenolpyruvate

25

37

-

Tyr-sensitive isozyme, wild-type: 50% loss of activity in 80 min in presence of phosphoenolpyruvate, mutant N8K: 50% loss of activity in 20 min in presence of phosphoenolpyruvate

37°C, 65 min, 50% residual activity

-

Co2+ stabilizes

-

Cu2+ and Fe2+ accelerates subunit dissociation

-

metal-catalysed oxidation of the enzyme, the apoenzyme shows an exponentially decrease in activity with a half-life of about 1 day at 22°C, Cu2+ and Fe2+ accelerated the rate of inactivation and subunit dissociation, phosphoenolpyruvate and EDTA stabilize, mutants are insensitive

-

phosphoenolpyruvate stabilizes

-

639747, 639771

spontaneous inactivation with a net loss of two of the seven thiol groups per subunit is restored by dithiothreitol

-

-15°C, ammonium sulfate and acetone fractions, stable for at least several weeks

-

-20°C, 0.1 M potassium phosphate, pH 6.5, 1 mM phosphoenolpyruvate, stable for at least 6 months

-

-20°C, in phosphate buffer containing phosphoenolpyruvate, stable for several months

-

639747, 639753

recombinant His10-tagged enzyme from Escherichia coli strain BL21 by affinity chromatography, followed by tag cleavage with factor Xa and again affinity chromatography and dialysis to remove the tag

-

-

105fold

-

2fold

-

5-6fold to homogeneity

-

683fold

-

partial

-

Phe-sensitive isozyme, recombinant wild-type from overexpressing strain and recombinant mutants

-

639771, 639789

recombinant from overexpressing strain

-

639768, 639774, 639775, 639777

strain JP1525

-

Tyr-sensitive isozyme, wild-type and mutants from strain AB3257

-

gene aroG, recombinant expression of a truncated coding DNA sequence of aroG in transgenic Solanum lycopersicum cv. 82 fruits under control of a fruit ripening-specific promoter, E8. Metabolic profiling of transgenic tomato plants expressing a bacterial feedback-insensitive AroG gene, overview

738761

gene aroG, recombinant expression of His10-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain DH5alpha

-

-

expressed in Escherichia coli strain NSTCSRA

-

684632

gene aroF, Tyr-sensitive isozyme, expression of wild-type and mutants in strain AB3257

-

gene aroF, Tyr-sensitive isozyme, overexpression in strain BL21(DE3)

-

gene aroG, Phe-sensitive isozyme, overexpression in strain gene aroH, Trp-sensitive isozyme, overexpression in deficient strain AB3248

-

overexpression in BL21(DE3)

-

overexpression of 3 isozymes

-

639775

Phe-sensitive isozyme, wild-type and mutants, expression in Escherichia coli strain BL21(DE3)

-

enzyme damage by reactive oxidants, H2O2 and superoxide, induces the enzyme expression in Escherichia coli, which attempts to compensate for diminished DAHP synthase activity by increasing expression

agriculture

expression of wild-type enzyme and phenylalanine-feedback insensitive mutant L175Q in Arabidopsis thaliana. Transgenic plants have comparable phenotypes and are fully fertile. The levels of shikimate, prephenate and Phe are higher in the different lines expressing the mutant enzyme than in the lines expressing the natural feedback-sensitive bacterial enzyme, and the control plants. Results imply that the bacterial enzyme is active in the transgenic plants and, similar to its operation in bacteria, the feedback insensitivity trait of the mutant enzyme is fundamental for enhancement of the flow of primary carbon metabolites via the shikimate pathway into the production of aromatic amino acids also in the plant

biotechnology

fruit-specific manipulation of the conversion of primary to specialized metabolism, e.g. by expressing 3-deoxy-7-phosphoheptulonate synthase in tomato fruits, is an attractive approach for improving fruit aroma and flavour qualities as well as discovering novel fruit-specialized metabolites. Metabolic profiling of transgenic tomato plants expressing a bacterial feedback-insensitive AroG gene, overview

biotechnology

synthesis

synthesis of L-phenylalanine (an important amino acid that is widely used in the production of food flavors and pharmaceuticals) by engineered Escherichia coli. Coexpression of Vitreoscilla hemoglobin gene, driven by a tac promoter, with the genes encoding 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (aroF) and feedback-resistant chorismate mutase/prephenate dehydratase (pheAfbr), leads to increased productivity of L-phenylalanine and decreased demand for aeration by Escherichia coli CICC10245

747338

637413

Radaev, S.; Dastidar, P.; Patel, M.; Woodard, R.W.; Gatti, D.L.

Structure and mechanism of 3-deoxy-D-manno-octulosonate 8-phosphate synthase

J. Biol. Chem.

275

9476-9484

2000

Escherichia coli

10734095

637421

Howe, D.L.; Sundaram, A.K.; Wu, J.; Gatti, D.L.; Woodard, R.W.

Mechanistic insight into 3-deoxy-D-manno-octulosonate-8-phosphate synthase and 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase utilizing phosphorylated monosaccharide analogues

Biochemistry

42

4843-4854

2003

Escherichia coli

12718525

Srinivasan, P.R.; Sprinson, D.B.

2-Keto-3-deoxy-D-arabo-heptonic acid 7-phosphate synthetase

J. Biol. Chem.

234

716-722

1954

Escherichia coli

13654249

Dusha, I.; D�nes, G.

Purification and properties of tyrosine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthetase of Escherichia coli K12

Biochim. Biophys. Acta

438

563-573

1976

Escherichia coli

821531

Schoner, R.; Herrmann, K.M.

3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification, properties, and kinetics of the tyrosine-sensitive isoenzyme from Escherichia coli

J. Biol. Chem.

251

5440-5447

1976

Escherichia coli

9387

Simpson, R.J.; Davidson, B.E.

Studies on 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase(phe) from Escherichia coli. Purification and subunit structure

Eur. J. Biochem.

70

493-500

1976

Escherichia coli

12951

Simpson, R.J.; Davidson, B.E.

Studies on 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase(phe) from Escherichia coli K12. 2. Kinetic properties

Eur. J. Biochem.

70

501-507

1976

Escherichia coli

12952

Simpson, R.J.; Davidson, B.E.

Studies on 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase(phe) from Escherichia coli K12. 3. Structural studies

Eur. J. Biochem.

70

509-516

1976

Escherichia coli

12953

McCandliss, R.J.; Poling, M.D.; Herrmann, K.M.

3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification and molecular characterization of the phenylalanine-sensitive isoenzyme from Escherichia coli

J. Biol. Chem.

253

4259-4265

1978

Escherichia coli, Escherichia coli HE 401

26682

639767

Akowski, J.P.; Bauerle, R.

Steady state kinetics and inhibitor binding of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (tryptophan sensitive) from Escherichia coli

Biochemistry

36

15817-15822

1997

Escherichia coli

9398312

Ray, J.M.; Bauerle, R.

Purification and properties of tryptophan-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli

J. Bacteriol.

173

1894-1901

1991

Escherichia coli

1672127

Park, O.K.; Bauerle, R.

Metal-catalyzed oxidation of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli: inactivation and destabilization by oxidation of active-site cysteine

J. Bacteriol.

181

1636-1642

1999

Escherichia coli

10049398

Sheflyan, G.Y.; Howe, D.L.; Wilson, T.L.; Woodard, R.W.

Enzymatic synthesis of 3-deoxy-D-manno-octulosonate 8-phosphate 3-deoxy-D-altro-octulosonate 8-phosphate, 3,5-dideoxy-D-gluco(manno)-octulosonate 8-phosphate by 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase

J. Am. Chem. Soc.

120

11027-11032

1998

Escherichia coli

-

639775

Stephens, C.M.; Bauerle, R.

Analysis of the metal requirement of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli

J. Biol. Chem.

266

20810-20817

1991

Escherichia coli

1682314

639776

Shumilin, I.A.; Kretsinger, R.H.; Bauerle, R.

Purification, crystallization, and preliminary crystallographic analysis of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli

Proteins Struct. Funct. Genet.

24

404-406

1996

Escherichia coli

8778789

Ramilo, C.A.; Evans, J.N.S.

Overexpression, purification, and characterization of tyrosine-sensitive 3-deoxy-D-arabino-heptulosonic acid 7-phosphate synthase from Escherichia coli

Protein Expr. Purif.

9

253-261

1997

Escherichia coli

9056491

639783

Flores, N.; Xiao, J.; Berry, A.; Bolivar, F.; Valle, F.

Pathway engineering for the production of aromatic compouds in Escherichia coli

Nat. Biotechnol.

14

620-623

1996

Escherichia coli

9630954

639788

Wagner, T.; Shumilin, I.A.; Bauerle, R.; Kretsinger, R.H.

Structure of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli: Comparison of the Mn2+*2-phosphoglycolate and the Pb2+*2-phosphoenolpyruvate complexes and Implications for catalysis

J. Mol. Biol.

301

389-399

2000

Escherichia coli (P0AB91), Escherichia coli

10926516

Howe, D.L.; Duewel, H.S.; Woodard, R.W.

Histidine 268 in 3-deoxy-D-arabino-heptulosonic acid 7-phosphate synthase plays the same role as histidine 202 in 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase

J. Biol. Chem.

275

40258-40265

2000

Escherichia coli

10988284

Jossek, R.; Bongaerts, J.; Sprenger, G.A.

Characterization of a new feedback-resistant 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase AroF of Escherichia coli

FEMS Microbiol. Lett.

202

145-148

2001

Escherichia coli, Escherichia coli W3110 / ATCC 27325

11506923

Parker, E.J.; Bulloch, E.M.M.; Jameson, G.B.; Abell, C.

Substrate deactivation of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase by erythrose 4-phosphate

Biochemistry

40

14821-14828

2001

Escherichia coli (P0AB91), Escherichia coli

11732901

Shumilin, I.A.; Bauerle, R.; Kretsinger, R.H.

The high-resolution structure of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase reveals a twist in the plane of bound phosphoenolpyruvate

Biochemistry

42

3766-3776

2003

Escherichia coli (P0AB91), Escherichia coli

12667068

658128

Furdui, C.M.; Sau, A.K.; Yaniv, O.; Belakhov, V.; Woodard, R.W.; Baasov, T.; Anderson, K.S.

The use of (E)- and (Z)-phosphoenol-3-fluoropyruvate as mechanistic probes reveals significant differences between the active sites of KDO8P and DAHP synthases

Biochemistry

44

7326-7335

2005

Escherichia coli

15882071

Hu, C.; Jiang, P.; Xu, J.; Wu, Y.; Huang, W.

Mutation analysis of the feedback inhibition site of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of Escherichia coli

J. Basic Microbiol.

43

399-406

2003

Escherichia coli

12964183

659072

Xu, J.; Hu, C.; Shen, S.; Wang, W.; Jiang, P.; Huang, W.

Requirement of the N-terminus for dimer formation of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate synthase AroG of Escherichia coli

J. Basic Microbiol.

44

400-406

2004

Escherichia coli

15378531

659406

Furdui, C.; Zhou, L.; Woodard, R.W.; Anderson, K.S.

Insights into the mechanism of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (Phe) from Escherichia coli using a transient kinetic analysis

J. Biol. Chem.

279

45618-45625

2004

Escherichia coli

15326172

672576

Williamson, R.M.; Pietersma, A.L.; Jameson, G.B.; Parker, E.J.

Stereospecific deuteration of 2-deoxyerythrose 4-phosphate using 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase

Bioorg. Med. Chem. Lett.

15

2339-2342

2005

Escherichia coli

15837321

672596

Walker, S.R.; Parker, E.J.

Synthesis and evaluation of a mechanism-based inhibitor of a 3-deoxy-D-arabino heptulosonate 7-phosphate synthase

Bioorg. Med. Chem. Lett.

16

2951-2954

2006

Escherichia coli

16563755

680370

Ran, N.; Frost, J.W.

Directed evolution of 2-keto-3-deoxy-6-phosphogalactonate aldolase to replace 3-deoxy-D-arabino-heptulosonic acid 7-phosphate synthase

J. Am. Chem. Soc.

129

6130-6139

2007

Escherichia coli

17451239

684632

Yakandawala, N.; Romeo, T.; Friesen, A.D.; Madhyastha, S.

Metabolic engineering of Escherichia coli to enhance phenylalanine production

Appl. Microbiol. Biotechnol.

78

283-291

2008

Escherichia coli, Escherichia coli NST 37 / ATCC 31882

18080813

Walker, S.; Cumming, H.; Parker, E.

Substrate and reaction intermediate mimics as inhibitors of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase

Org. Biomol. Chem.

7

3031-3035

2009

Escherichia coli

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Walker, S.R.; Jiao, W.; Parker, E.J.

Synthesis and evaluation of dual site inhibitors of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase

Bioorg. Med. Chem. Lett.

21

5092-5097

2011

Escherichia coli

21493065

Tzin, V.; Malitsky, S.; Ben Zvi, M.M.; Bedair, M.; Sumner, L.; Aharoni, A.; Galili, G.

Expression of a bacterial feedback-insensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of the shikimate pathway in Arabidopsis elucidates potential metabolic bottlenecks between primary and secondary metabolism

New Phytol.

194

430-439

2012

Escherichia coli (P0AB91)

22296303

Sobota, J.M.; Gu, M.; Imlay, J.A.

Intracellular hydrogen peroxide and superoxide poison 3-deoxy-D-arabinoheptulosonate 7-phosphate synthase, the first committed enzyme in the aromatic biosynthetic pathway of Escherichia coli

J. Bacteriol.

196

1980-1991

2014

Escherichia coli (P0AB91), Escherichia coli

24659765

738761

Tzin, V.; Rogachev, I.; Meir, S.; Moyal Ben Zvi, M.; Masci, T.; Vainstein, A.; Aharoni, A.; Galili, G.

Tomato fruits expressing a bacterial feedback-insensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of the shikimate pathway possess enhanced levels of multiple specialized metabolites and upgraded aroma

J. Exp. Bot.

64

4441-4452

2013

Escherichia coli (P0AB91)

24006429

747338

Wu, W.B.; Guo, X.L.; Zhang, M.L.; Huang, Q.G.; Qi, F.; Huang, J.Z.

Enhancement of L-phenylalanine production in Escherichia coli by heterologous expression of Vitreoscilla hemoglobin

Biotechnol. Appl. Biochem.

65

476-483

2018

Escherichia coli (P00888), Escherichia coli, Escherichia coli K12 (P00888)

28872702

758795

Balachandran, N.; Heimhalt, M.; Liuni, P.; To, F.; Wilson, D.J.; Junop, M.S.; Berti, P.J.

Potent inhibition of 3-deoxy-D-arabinoheptulosonate-7-phosphate (DAHP) synthase by DAHP oxime, a phosphate group mimic

Biochemistry

55

6617-6629

2016

Escherichia coli (C3TIE2)

27933795

758801

Balachandran, N.; To, F.; Berti, P.J.

Linear free energy relationship analysis of transition state mimicry by 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) oxime, a DAHP synthase inhibitor and phosphate mimic

Biochemistry

56

592-601

2017

Escherichia coli (C3TIE2)

28045507

Heimhalt, M.; Jiang, S.; Berti, P.J.

Eliminating competition Characterizing and eliminating competitive binding at separate sites between DAHP synthases essential metal ion and the inhibitor DAHP oxime

Biochemistry

57

6679-6687

2018

Escherichia coli (C3TIE2)

30398055