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Ligand L-arogenate

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for L-arogenate

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (9 results)

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Show Natural Substrate (9 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.43

L-arogenate + NAD+ = L-tyrosine + NADH + CO2

390791, 390803, 390802, 390512, 390519, 390785, 390783, 390804, 390797, 390782, 390548, 390798, 390784

-

1.3.1.78

L-arogenate + NAD+ = L-tyrosine + NADH + CO2

390781, 390801, 390793, 390560, 390531, 390557, 390796, 390805, 390794, 390788

-

1.3.1.78

L-arogenate + NADP+ = L-tyrosine + NADPH + CO2

745837, 654548

-

1.3.1.79

L-arogenate + NAD(P)+ = L-tyrosine + NAD(P)H + CO2

746040

-

1.3.1.79

L-arogenate + NAD+ = L-tyrosine + NADH + CO2

390795, 390525

-

1.3.1.78

2 entries

1.3.1.79

2 entries

2.6.1.78

L-arogenate + oxaloacetate = L-aspartate + prephenate

759178, 759965

-

2.6.1.79

L-arogenate + 2-oxoglutarate = L-glutamate + prephenate

759178, 759965

-

4.2.1.91

L-arogenate = L-phenylalanine + CO2 + H2O

648475, 648473, 33892, 648474, 648479, 648476

-

4.2.1.91

L-arogenate = L-phenylalanine + H2O + CO2

729977, 730568, 648479, 665896, 666899, 716582, 748332, 748705, 748982, 748993

-

4.2.1.91

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.6.1.78

prephenate + L-aspartate = L-arogenate + oxaloacetate

0

-

2.6.1.79

prephenate + L-glutamate = L-arogenate + 2-oxoglutarate

0

-

Substrate in Enzyme-catalyzed Reactions (18 results)

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Show Substrate (18 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.12

L-arogenate + NAD+ = L-tyrosine + NADH + CO2

390518, 677010

-

1.3.1.13

L-arogenate + NADP+ = L-tyrosine + NADPH + H+ + CO2

763088

-

1.3.1.43

L-arogenate + NAD(P)+ = L-tyrosine + NAD(P)H + CO2

390791, 390803, 390802, 390512, 390798, 390519, 390783, 390804, 390797, 390782, 390548, 390785, 390784

-

1.3.1.43

L-arogenate + NAD+ = L-tyrosine + NADH + CO2

390791, 390803, 390802, 390512, 390519, 390785, 390783, 390804, 390797, 390782, 390548, 390798, 390784

-

1.3.1.78

L-arogenate + NAD(P)+ = L-tyrosine + NAD(P)H + CO2

390781, 390801, 390793, 390560, 390531, 390557, 390788, 390796, 390794, 390805

-

1.3.1.78

L-arogenate + NAD+ = L-tyrosine + NADH + CO2

390781, 390801, 390793, 390560, 390531, 390557, 390796, 390805, 390794, 390788

-

1.3.1.78

L-arogenate + NADP+ = L-tyrosine + NADPH + CO2

677163, 745837, 654548, 655440

-

1.3.1.79

L-arogenate + NAD(P)+ = L-tyrosine + NAD(P)H + CO2

390525, 684578, 390795, 746040

-

1.3.1.79

L-arogenate + NAD(P)+ = L-tyrosine + NAD(P)H + H+ + CO2

763088

-

1.3.1.79

L-arogenate + NAD+ = L-tyrosine + NADH + CO2

390795, 390525

-

1.3.1.43

2 entries

1.3.1.78

3 entries

1.3.1.79

3 entries

2.6.1.57

L-arogenate + indolepyruvate = L-tryptophan + 3-(1-carboxy-4-hydroxycyclohexa-2,5-dienyl)2-oxopropanoate

636657

-

2.6.1.78

L-arogenate + oxaloacetate = L-aspartate + prephenate

759178, 759965

-

2.6.1.78

L-arogenate + oxaloacetate = prephenate + L-aspartate

722267

-

2.6.1.79

L-arogenate + 2-oxoglutarate = L-glutamate + prephenate

759178, 759965

-

2.6.1.79

L-arogenate + 2-oxoglutarate = prephenate + L-glutamate

722267

-

2.6.1.78

2 entries

2.6.1.79

2 entries

4.2.1.51

L-arogenate = L-phenylalanine + CO2 + H2O

694629

-

4.2.1.91

L-arogenate = L-phenylalanine + CO2 + H2O

648475, 648473, 33892, 648474, 648476, 680833, 706229, 648479, 706157

-

4.2.1.91

L-arogenate = L-phenylalanine + H2O + CO2

729977, 730568, 648479, 665896, 666899, 716582, 748332, 748705, 748982, 748993, 694629

-

4.2.1.91

2 entries

Product in Enzyme-catalyzed Reactions (12 results)

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Show Product (12 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.6.1.17

prephenate + N-succinyl-L-2,6-diaminoheptanedioate = L-arogenate + N-succinyl-2-amino-6-oxoheptanedioate

0

-

2.6.1.57

prephenate + Asp = arogenate + 2-oxosuccinate

0

-

2.6.1.57

prephenate + Glu = arogenate + 2-oxoglutarate

0

-

2.6.1.57

prephenate + Phe = arogenate + phenylpyruvate

0

-

2.6.1.57

prephenate + Tyr = arogenate + 4-hydroxyphenylpyruvate

0

-

2.6.1.78

L-aspartate + prephenate = L-arogenate + oxaloacetate

0

-

2.6.1.78

prephenate + L-aspartate = L-arogenate + oxaloacetate

0

-

2.6.1.78

prephenate + L-glutamate = L-arogenate + 2-oxoglutarate

0

-

2.6.1.79

L-glutamate + prephenate = L-arogenate + 2-oxoglutarate

0

-

2.6.1.79

prephenate + L-aspartate = L-arogenate + oxaloacetate

0

-

2.6.1.79

prephenate + L-glutamate = L-arogenate + 2-oxoglutarate

0

-

2.6.1.79

prephenate + N-succinyl-L-2,6-diaminoheptanedioate = L-arogenate + N-succinyl-2-amino-6-oxoheptanedioate

0

-

2.6.1.57

4 entries

2.6.1.78

3 entries

2.6.1.79

4 entries

Inhibitor in Enzyme-catalyzed Reactions (3 results)

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Show Inhibitors (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.54

isozyme DS-Mn, competitive against D-erythrose 4-phosphate, non-competitive against phosphoenolpyruvate

639782

-

4.2.1.91

competitive inhibition of prephenate dehydratase activity

33892

-

4.2.1.91

competitive inhibition of prephenate dehydratase activity; competitive to prephenate; reaction with prephenate is inhibited

648479

-

4.2.1.91

2 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (20 results)

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Show Turnover Number (20 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.3.1.12

1.3

-

at 30°C, wild-type

677010

1.3.1.12

2.2

-

at 30°C, delta19PD

677010

1.3.1.12

3

6

at 80°C, wild-type

677010

1.3.1.12

6.8

-

at 55°C, wild-type

677010

1.3.1.12

13

-

at 55°C, delta19PD

677010

1.3.1.12

68

-

at 80°C, delta19PD

677010

1.3.1.12

6 entries

1.3.1.13

0.7

-

mutant Q227E, pH 7.6, temperature not specified in the publication

763088

1.3.1.78

37.3

-

pH 7.5, 25°C, TyrAAT2

655440

1.3.1.78

84.2

-

pH 7.5, 25°C, TyrAAT1

655440

1.3.1.79

0.45

-

mutant D208N, pH 7.6, temperature not specified in the publication

763088

1.3.1.79

3.44

-

wild-type, pH 7.6, temperature not specified in the publication

763088

4.2.1.91

0.194

-

at 37°C, in 250 mM Na-phosphate buffer, pH 8.2, 1 mM EDTA

706229

4.2.1.91

0.267

-

at 37°C, in 250 mM Na-phosphate buffer, pH 8.2, 1 mM EDTA

706229

4.2.1.91

0.5

-

37°C

680833

4.2.1.91

1.1

-

37°C

680833

4.2.1.91

1.231

-

at 37°C, in 250 mM Na-phosphate buffer, pH 8.2, 1 mM EDTA

706229

4.2.1.91

3.2

-

37°C

680833

4.2.1.91

4

-

37°C

680833

4.2.1.91

4.9

-

37°C

680833

4.2.1.91

6.1

-

37°C

680833

1.3.1.78

2 entries

1.3.1.79

2 entries

4.2.1.91

9 entries

K_M Value (54 results)

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Show KM Value (54 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.1.12

0.017

-

at 30°C, wild-type

677010

1.3.1.12

0.041

-

at 30°C, delta19PD

677010

1.3.1.12

0.097

-

at 55°C, wild-type

677010

1.3.1.12

0.135

-

at 55°C, delta19PD

677010

1.3.1.12

0.136

-

at 80°C, wild-type

677010

1.3.1.12

0.249

-

at 80°C, delta19PD

677010

1.3.1.12

6 entries

1.3.1.13

3.29

-

mutant Q227E, pH 7.6, temperature not specified in the publication

763088

1.3.1.43

0.09

-

-

390784

1.3.1.43

0.1

-

-

390783

1.3.1.43

0.15

-

-

390785

1.3.1.43

0.17

-

-

390803

1.3.1.43

0.18

-

-

390804

1.3.1.43

0.3

-

-

390791

1.3.1.43

0.56

-

-

390802

1.3.1.43

0.66

-

-

390548

1.3.1.43

0.91

-

-

390782

1.3.1.78

0.0001

-

-

390781

1.3.1.78

0.0002

-

-

390781

1.3.1.78

0.003

-

-

390781

1.3.1.78

0.045

-

recombinant from plasmids TyrA-AT2 and TyrA-ATlM36

390801

1.3.1.78

0.0526

-

pH 7.5, 25°C, TyrAAT1

655440

1.3.1.78

0.07

-

recombinant from plasmid TyrA-ATcM36

390801

1.3.1.78

0.0842

-

pH 7.5, 25°C, TyrAAT2

655440

1.3.1.78

0.093

-

-

677163

1.3.1.78

0.1

-

-

390794

1.3.1.78

0.313

-

ATCC 23055

390560

1.3.1.78

0.331

-

pH 8.6, 25°C

654548

1.3.1.78

0.34

-

-

390788

1.3.1.79

0.85

-

mutant D208N, pH 7.6, temperature not specified in the publication

763088

1.3.1.79

0.9

-

wild-type, pH 7.6, temperature not specified in the publication

763088

1.3.1.43

9 entries

1.3.1.78

12 entries

1.3.1.79

2 entries

2.6.1.57

0.45

-

pH 8.6, 37°C, AAT I

636657

2.6.1.79

0.8

-

pH 8.0

660563

4.2.1.51

0.12

-

wild-type, rice PDT is a bifunctional enzyme

694629

4.2.1.51

0.17

-

mutant S298I, rice PDT is a bifunctional enzyme

694629

4.2.1.91

0.0488

-

at 37°C, in 250 mM Na-phosphate buffer, pH 8.2, 1 mM EDTA

706229

4.2.1.91

0.0667

-

at 37°C, in 250 mM Na-phosphate buffer, pH 8.2, 1 mM EDTA

706229

4.2.1.91

0.09

-

pH 7.2, 37°C, 0.01 mM tyrosine

33892

4.2.1.91

0.1

-

pH 8.0, 22°C, 0.01 mM tyrosine

648476

4.2.1.91

0.12

-

wild-type, rice ADT is a bifunctional enzyme

694629

4.2.1.91

0.17

-

mutant S298I, rice ADT is a bifunctional enzyme

694629

4.2.1.91

0.179

-

at 37°C, in 250 mM Na-phosphate buffer, pH 8.2, 1 mM EDTA

706229

4.2.1.91

0.19

-

enzyme purified directly from Pseudomonas aeruginosa

648479

4.2.1.91

0.22

-

pH 7.5, 22°C

648479

4.2.1.91

0.22

-

pH 7.5, 37°C

648479

4.2.1.91

0.22

-

recombinant protein, purified from Escherichia coli

648479

4.2.1.91

0.32

-

pH 8.0, 22°C

648476

4.2.1.91

0.43

-

37°C

680833

4.2.1.91

0.63

-

-

648473

4.2.1.91

0.63

-

pH 7.5, 37°C, ATCC 13184

648475

4.2.1.91

0.8

-

37°C

680833

4.2.1.91

1.58

-

37°C

680833

4.2.1.91

1.72

-

37°C

680833

4.2.1.91

3.05

-

37°C

680833

4.2.1.91

10.08

-

37°C

680833

4.2.1.51

2 entries

4.2.1.91

20 entries

K_i Value (3 results)

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Show KI Value (3 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

4.2.1.91

0.2

-

-

648479

4.2.1.91

0.2

-

pH 7.5, 22°C

648479

4.2.1.91

0.2

-

pH 7.5, 37°C

648479

4.2.1.91

3 entries

References & Links

Literature References (59)

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Show Reference (59 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

33892

1897969

A single cyclohexadienyl dehydratase specifies the prephenate dehydratase and arogenate dehydratase components of one of two independent pathways to L-phenylalanine in Erwinia herbicola

1991

Xia, T.; Ahmad, S.; Zhao, G.; Jensen, R.A.

Arch. Biochem. Biophys.

286

461-465

390512

2894820

Enzymic arrangement and allosteric regulation of the aromatic amino acid pathway in Neisseria gonorrhoeae

1987

Berry, A.; Jensen, R.A.; Hendry, A.T.

Arch. Microbiol.

149

87-94

390518

3556217

The prephenate dehydrogenase component of the bifunctional T-protein in enteric bacteria can utilize L-arogenate

1987

Ahmad, S.; Jensen, R.A.

FEBS Lett.

216

133-139

390519

-

Phenylalanine and tyrosine biosynthesis in sporeforming members of the order Actinomycetales

1987

Hund, H.K.; Keller, B.; Lingens, F.

Z. Naturforsch. C

42

387-393

390525

6642432

Zur Biosynthese von Phenylalanin und Tyrosin bei Flavobakterien

1983

Waldner-Sander, S.; Keller, B.; Keller, E.; Lingens, F.

Hoppe-Seyler's Z. Physiol. Chem.

364

1467-1473

390531

457594

Obligatory biosynthesis of L-tyrosine via the pretyrosine branchlet in coryneform bacteria

1979

Fazel, A.M.; Jensen, R.A.

J. Bacteriol.

138

805-815

390548

-

Evolution of the biochemical pathway for aromatic amino acid biosynthesis in Serpens flexibilis in relationship to its phylogenetic position

1987

Ahmad, S.; Jensen, R.A.

Arch. Microbiol.

147

8-12

390557

16661043

Enzymology of L-tyrosine biosynthesis in mung bean (Vigna radiata [L.] Wilczek)

1979

Rubin, J.L.; Jensen, R.A.

Plant Physiol.

64

727-734

390560

4074072

Evolutionary implications of features of aromatic amino acid biosynthesis in the genus Acinetobacter

1985

Byng, G.S.; Berry, A.; Jensen, R.A.

Arch. Microbiol.

143

122-129

390781

3600376

Arogenate dehydrogenase

1987

Bonner, C.; Jensen, R.

Methods Enzymol.

142

488-494

390782

-

Arogenate dehydrogenase from Phenylobacterium immobile

1987

Lingens, F.; Keller, E.; Keller, B.

Methods Enzymol.

142

513-518

390783

4074498

Arogenate dehydrogenase from Streptomyces phaeochromogenes. Purification and properties

1985

Keller, B.; Keller, E.; Lingens, F.

Biol. Chem. Hoppe-Seyler

366

1063-1066

390784

3967752

Purification of arogenate dehydrogenase from Phenylobacterium immobile

1985

Mayer, E.; Waldner-Sander, S.; Keller, B.; Keller, E.; Lingens, F.

FEBS Lett.

179

208-212

390785

2590341

Purification and properties of arogenate dehydrogenase from Actinoplanes missouriensis

1989

Hund, H.K.; B. r, G.; Lingens, F.

Z. Naturforsch. C

44

797-801

390788

2939643

Tyrosine biosynthesis in Sorghum bicolor: isolation and regulatory properties of arogenate dehydrogenase

1986

Connelly, J.A.; Conn, E.E.

Z. Naturforsch. C

41

69-78

390791

-

Enzymology of L-tyrosine biosynthesis in corn (Zea mays)

1981

Byng, G.; Whitaker, R.; Flick, C.; Jensen, R.A.

Phytochemistry

20

1289-1292

390793

23196297

Aromatic amino acid biosynthesis in a 4-chlorobenzoic acid degrading Pseudomonas species; phenylalanine and tyrosine synthesis via arogenate

1983

Keller, B.; Keller, E.; Klages, U.; Lingens, F.

Syst. Appl. Microbiol.

4

27-33

390794

24272471

L-tyrosine regulation and biosynthesis via arogenate dehydrogenase in suspension-cultured cells of Nicotiana silvestris Speg. et Comes

1982

Gaines, C.G.; Byng, G.S.; Whitaker, R.J.; Jensen, R.A.

Planta

156

233-240

390795

7119734

Arogenate (pretyrosine) pathway of tyrosine and phenylalanine biosynthesis in Pseudomonas aureofaciens ATCC 15926

1982

Keller, B.; Keller, E.; Salcher, O.; Lingens, F.

J. Gen. Microbiol.

128

1199-1202

390796

-

Arogenate (pretyrosine) as an obligatory precursor of L-tyrosine biosynthesis in Flavobacterium devorans

1982

Keller, B.; Keller, E.; Sussmuth, R.; Lingens, F.

FEMS Microbiol. Lett.

13

3-4

390797

6108316

Enzymological basis for growth inhibition by L-phenylalanine in the cyanobacterium Synechocystis sp. 29108

1980

Hall, G.C.; Jensen, R.A.

J. Bacteriol.

144

1034-1042

390798

6929482

Arogenate (pretyrosine) is an obligatory intermediate of L-tyrosine biosynthesis: confirmation in a microbial mutant

1980

Fazel, A.M.; Bowen, J.R.; Jensen, R.A.

Proc. Natl. Acad. Sci. USA

77

1270-1273

390801

11905963

Molecular and biochemical characterization of an Arabidopsis thaliana arogenate dehydrogenase with two highly similar and active protein domains

2002

Rippert, P.; Matringe, M.

Plant Mol. Biol.

48

361-368

390802

11790331

Cyclohexadienyl dehydrogenase from Pseudomonas stutzeri exemplifies a widespread type of tyrosine-pathway dehydrogenase in the TyrA protein family

2000

Xie, G.; Bonner, C.A.; Jensen, R.A.

Comp. Biochem. Physiol. C

125

65-83

390803

2123197

A single cyclohexadienyl dehydrogenase specifies the prephenate dehydrogenase and arogenate dehydrogenase components of the dual pathways to L-tyrosine in Pseudomonas aeruginosa

1990

Xia, T.; Jensen, R.A.

J. Biol. Chem.

265

20033-20036

390804

7916685

An allosterically insensitive class of cyclohexadienyl dehydrogenase from Zymomonas mobilis

1993

Zhao, G.; Xia, T.; Ingram, L.O.; Jensen, R.A.

Eur. J. Biochem.

212

157-165

390805

-

Distinctive enzymes of aromatic amino acid biosynthesis that are highly conserved in land plants are also present in the chlorophyte alga Chlorella sorokiniana

1995

Bonner, C.A.; Fischer, R.S.; Schmidt, R.R.; Miller, P.W.; Jensen, R.A.

Plant Cell Physiol.

36

1013-1022

636657

-

Charakterisierung von drei aromatischen Aminotransferasen aus Candida maltosa

1984

Bode, R.; Birnbaum, D.

Z. Allg. Mikrobiol.

24

67-75

639782

16664478

Differentially regulated isoenzymes of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from seedlings of Vigna radiata

1985

Rubin, J.L.; Jensen, R.A.

Plant Physiol.

79

711-718

648473

3924095

Enzymatic and nonenzymatic dehydration reactions of L-arogenate

1985

Zamir, L.O.; Tiberio, R.; Fiske, M.; Berry, A.; Jensen, R.A.

Biochemistry

24

1607-1612

648474

3619011

A simple spectrophotometric assay for arogenate dehydratase

1987

Ahmad, S.; Jensen, R.A.

Anal. Biochem.

163

107-111

648475

3600377

Arogenate dehydratase

1987

Fischer, R.; Jensen, R.

Methods Enzymol.

142

495-502

648476

3124763

Kinetic and regulatory properties of arogenate dehydratase in seedlings of Sorghum bicolor (L.) Moench

1988

Siehl, D.L.; Conn, E.E.

Arch. Biochem. Biophys.

260

822-829

648479

1733946

Cyclohexadienyl dehydratase from Pseudomonas aeruginosa. Molecular cloning of the gene and characterization of the gene product

1992

Zhao, G.; Xia, T.; Fischer, R.S.; Jensen, R.A.

J. Biol. Chem.

267

2487-2493

654548

15171683

A core catalytic domain of the TyrA protein family: arogenate dehydrogenase from Synechocystis

2004

Bonner, C.A.; Jensen, R.A.; Gander, J.E.; Keyhani, N.O.

Biochem. J.

382

279-291

655440

12354106

Purification and kinetic analysis of the two recombinant arogenate dehydrogenase isoforms of Arabidopsis thaliana

2002

Rippert, P.; Matringe, M.

Eur. J. Biochem.

269

4753-4761

660563

2939644

Tyrosine biosynthesis in Sorghum bicolor: characteristics of prephenate aminotransferase

1986

Siehl, D.L.; Connelly, J.A.; Conn, E.E.

Z. Naturforsch. C

41

79-86

665896

8515238

Cyclohexadienyl dehydratase from Pseudomonas aeruginosa is a periplasmic protein

1993

Zhao, G.; Xia, T.; Aldrich, H.; Jensen, R.A.

J. Gen. Microbiol.

139

807-813

666899

8210673

A bacterial periplasmic receptor homologue with catalytic activity: cyclohexadienyl dehydratase of Pseudomonas aeruginosa is homologous to receptors specific for polar amino acids

1993

Tam, R.; Saier, M.H., Jr.

Res. Microbiol.

144

165-169

677010

16731976

Biochemical characterization of prephenate dehydrogenase from the hyperthermophilic bacterium Aquifex aeolicus

2006

Bonvin, J.; Aponte, R.A.; Marcantonio, M.; Singh, S.; Christendat, D.; Turnbull, J.L.

Protein Sci.

15

1417-1432

677163

16615917

Biochemical characterization and crystal structure of Synechocystis arogenate dehydrogenase provide insights into catalytic reaction

2006

Legrand, P.; Dumas, R.; Seux, M.; Rippert, P.; Ravelli, R.; Ferrer, J.L.; Matringe, M.

Structure

14

767-776

680833

17726025

Phenylalanine biosynthesis in Arabidopsis thaliana. Identification and characterization of arogenate dehydratases

2007

Cho, M.H.; Corea, O.R.; Yang, H.; Bedgar, D.L.; Laskar, D.D.; Anterola, A.M.; Moog-Anterola, F.A.; Hood, R.L.; Kohalmi, S.E.; Bernards, M.A.; Kang, C.; Davin, L.B.; Lewis, N.G.

J. Biol. Chem.

282

30827-30835

684578

18344329

Metabolic engineering of Escherichia coli for L-tyrosine production by expression of genes coding for the chorismate mutase domain of the native chorismate mutase-prephenate dehydratase and a cyclohexadienyl dehydrogenase from Zymomonas mobilis

2008

Chavez-Bejar, M.I.; Lara, A.R.; Lopez, H.; Hernandez-Chavez, G.; Martinez, A.; Ramirez, O.T.; Bolivar, F.; Gosset, G.

Appl. Environ. Microbiol.

74

3284-3290

694629

18487352

Mutation of a rice gene encoding a phenylalanine biosynthetic enzyme results in accumulation of phenylalanine and tryptophan

2008

Yamada, T.; Matsuda, F.; Kasai, K.; Fukuoka, S.; Kitamura, K.; Tozawa, Y.; Miyagawa, H.; Wakasa, K.

Plant Cell

20

1316-1329

706157

-

Metabolic engineering of the tryptophan and phenylalanine biosynthetic pathways in rice

2009

Wakasa, K.; Ishihara, A.

Plant Biotechnol.

26

523-533

706229

20215586

RNAi suppression of arogenate dehydratase1 reveals that phenylalanine is synthesized predominantly via the arogenate pathway in petunia petals

2010

Maeda, H.; Shasany, A.K.; Schnepp, J.; Orlova, I.; Taguchi, G.; Cooper, B.R.; Rhodes, D.; Pichersky, E.; Dudareva, N.

Plant Cell

22

832-849

716582

21388819

Complementation of the pha2 yeast mutant suggests functional differences for arogenate dehydratases from Arabidopsis thaliana

2011

Bross, C.D.; Corea, O.R.; Kaldis, A.; Menassa, R.; Bernards, M.A.; Kohalmi, S.E.

Plant Physiol. Biochem.

49

882-890

722267

20883697

Identification of a plant gene encoding glutamate/aspartate-prephenate aminotransferase: the last homeless enzyme of aromatic amino acids biosynthesis

2010

Graindorge, M.; Giustini, C.; Jacomin, A.C.; Kraut, A.; Curien, G.; Matringe, M.

FEBS Lett.

584

4357-4360

729977

22311980

Arogenate dehydratase isoenzymes profoundly and differentially modulate carbon flux into lignins

2012

Corea, O.R.; Ki, C.; Cardenas, C.L.; Kim, S.J.; Brewer, S.E.; Patten, A.M.; Davin, L.B.; Lewis, N.G.

J. Biol. Chem.

287

11446-11459

730568

22818526

The arogenate dehydratase gene family: towards understanding differential regulation of carbon flux through phenylalanine into primary versus secondary metabolic pathways

2012

Corea, O.R.; Bedgar, D.L.; Davin, L.B.; Lewis, N.G.

Phytochemistry

82

22-37

745837

25402771

Non-plastidic, tyrosine-insensitive prephenate dehydrogenases from legumes

2015

Schenck, C.A.; Chen, S.; Siehl, D.L.; Maeda, H.A.

Nat. Chem. Biol.

11

52-57

746040

25524070

Transcriptomic analysis highlights reciprocal interactions of urea and nitrate for nitrogen acquisition by maize roots

2015

Zanin, L.; Zamboni, A.; Monte, R.; Tomasi, N.; Varanini, Z.; Cesco, S.; Pinton, R.

Plant Cell Physiol.

56

532-548

748332

28338876

Subcellular localization of Arabidopsis arogenate dehydratases suggests novel and non-enzymatic roles

2017

Bross, C.D.; Howes, T.R.; Abolhassani Rad, S.; Kljakic, O.; Kohalmi, S.E.

J. Exp. Bot.

68

1425-1440

748705

27720844

Arogenate dehydratase isoforms differentially regulate anthocyanin biosynthesis in Arabidopsis thaliana

2016

Chen, Q.; Man, C.; Li, D.; Tan, H.; Xie, Y.; Huang, J.

Mol. Plant

9

1609-1619

748982

27540109

The dehydratase ADT3 affects ROS homeostasis and cotyledon development

2016

Para, A.; Muhammad, D.; Orozco-Nunnelly, D.A.; Memishi, R.; Alvarez, S.; Naldrett, M.J.; Warpeha, K.M.

Plant Physiol.

172

1045-1060

748993

29523714

Reduced arogenate dehydratase expression ramifications for photosynthesis and metabolism

2018

Hoehner, R.; Marques, J.V.; Ito, T.; Amakura, Y.; Budgeon, A.D.; Weitz, K.; Hixson, K.K.; Davin, L.B.; Kirchhoff, H.; Lewis, N.G.

Plant Physiol.

177

115-131

759178

30771275

Tyrosine metabolism identification of a key residue in the acquisition of prephenate aminotransferase activity by 1beta aspartate aminotransferase

2019

Giustini, C.; Graindorge, M.; Cobessi, D.; Crouzy, S.; Robin, A.; Curien, G.; Matringe, M.

FEBS J.

286

2118-2134

759965

29405514

Structural basis for substrate recognition and inhibition of prephenate aminotransferase from Arabidopsis

2018

Holland, C.K.; Berkovich, D.A.; Kohn, M.L.; Maeda, H.; Jez, J.M.

Plant J.

94

304-314

763088

29164132

Conserved molecular mechanism of TyrA dehydrogenase substrate specificity underlying alternative tyrosine biosynthetic pathways in plants and microbes

2017

Schenck, C.; Men, Y.; Maeda, H.

Front. Mol. Biosci.

4

73

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