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• • Molecular Structure
  • Sum Formula
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• • In Vivo Substrate
  • In Vivo Product
  • Substrate
  • Product
  • Cofactor
  • Activator
  • Inhibitor
  • Metals and Ions
  • 3D Structure (PDB)
• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
  • K_M Value
  • K_i Value
  • IC₅₀ Value
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Ligand prephenate

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

bacilysin biosynthesis, phenylalanine metabolism, tyrosine metabolism

KEGG

Biosynthesis of alkaloids derived from shikimate pathway, Biosynthesis of amino acids, Biosynthesis of phenylpropanoids, Biosynthesis of plant secondary metabolites, Biosynthesis of secondary metabolites, Biosynthesis of various secondary metabolites - part 2, Novobiocin biosynthesis, Phenylalanine, tyrosine and tryptophan biosynthesis more

MetaCyc

3-dimethylallyl-4-hydroxybenzoate biosynthesis, 5-(methoxycarbonylmethoxy)uridine biosynthesis, bacilysin biosynthesis, L-phenylalanine biosynthesis I, L-phenylalanine biosynthesis II, L-phenylalanine biosynthesis III (cytosolic, plants), L-tyrosine biosynthesis I, L-tyrosine biosynthesis II, L-tyrosine biosynthesis III, salinosporamide A biosynthesis more

Show all BRENDA pathways known for prephenate

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (12 results)

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Show Natural Substrate (12 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.12

prephenate + NAD+ = 4-hydroxyphenylpyruvate + NADH + CO2

390513, 390550, 3557, 390516, 390518, 390521, 390522, 390524, 390526, 390527, 390528, 390529, 390530, 390532, 390537, 390538, 390539, 390540, 390546, 390552, 390553, 390523, 390515, 390541, 390542, 390545, 390544, 390535, 390547, 390512, 33885, 390554, 3542, 33883, 390525, 390543, 390517, 33876, 390511, 390548, 390549

-

1.3.1.12

prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH

740113, 746929, 654967, 655472, 692260

-

1.3.1.12

prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH + H+

710738

-

1.3.1.12

prephenate + NAD+ = 4-hydroxyphenylpyruvate + NADH + H+ + CO2

723959

-

1.3.1.13

prephenate + NADP+ = 4-hydroxyphenylpyruvate + CO2 + NADPH

390556, 741040, 390560, 390557, 390558, 390525, 740113, 740420

-

1.3.1.13

prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH

740420, 740113

-

1.3.1.12

4 entries

1.3.1.13

2 entries

1.3.1.43

prephenate + NAD+ = ?

390804

-

2.6.1.78

prephenate + L-aspartate = L-arogenate + oxaloacetate

657636

-

2.6.1.79

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

659858, 657635, 660563

-

4.1.1.100

prephenate = 3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2

729211, 729204, 729203

-

4.2.1.51

prephenate = phenylpyruvate + H2O + CO2

730847, 716582, 714881, 730200, 649516, 649980, 651653, 665625, 663605, 682402, 681657, 727742, 692260

-

4.2.1.51

prephenate = ?

33888, 33889, 33872, 33880, 33881, 3543, 3558, 3570, 3574, 33886, 33887, 33891, 33895, 33896, 33890, 3566, 33901, 33870, 3575, 33874, 33875, 33885, 33899, 33892, 3542, 33883, 33879, 33897, 33898, 33876, 33877, 33878

-

4.2.1.51

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (3 results)

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Show Natural Product (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

5.4.99.5

Chorismate = Prephenate

651598, 649126, 649938, 390552, 649832, 651660, 649515, 651936, 652061, 650528, 651595

1com, 3D-view

5.4.99.5

Chorismate = Prephenate

651598, 649126, 649938, 390552, 649832, 651660, 649515, 651936, 652061, 650528, 651595

3zp7, 3D-view

5.4.99.5

Chorismate = Prephenate

651598, 649126, 649938, 390552, 649832, 651660, 649515, 651936, 652061, 650528, 651595

5j6f, 3D-view

5.4.99.5

3 entries

Substrate in Enzyme-catalyzed Reactions (32 results)

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Show Substrate (32 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.12

prephenate + NAD+ = 4-hydroxyphenylpyruvate + NADH + CO2

390513, 390550, 3557, 390516, 390518, 390521, 390522, 390524, 390526, 390527, 390528, 390530, 390532, 390537, 390538, 390539, 390540, 390546, 390552, 390553, 390555, 671431, 684595, 685716, 390515, 390541, 390542, 390535, 390547, 390512, 33885, 676965, 3542, 33883, 390525, 684578, 390543, 390517, 33876, 674545, 390511, 390548, 390549, 390551, 390554, 390529, 390523, 390545, 390544

-

1.3.1.12

prephenate + NADP+ = 4-hydroxyphenylpyruvate + NADPH + CO2

390551

-

1.3.1.12

prephenate + NADP+ = 4-hydroxyphenylpyruvate + CO2 + NADPH

746929

-

1.3.1.12

prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH

740113, 654967, 655472, 746929, 677010, 698889, 692260

-

1.3.1.12

prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH + H+

710738

-

1.3.1.12

prephenate + NAD+ = 4-hydroxyphenylpyruvate + NADH + H+ + CO2

723959, 726409

-

1.3.1.13

prephenate + NADP+ = 4-hydroxyphenylpyruvate + CO2 + NADPH

390556, 741040, 390560, 390557, 390558, 390525, 740113, 740420

-

1.3.1.13

prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH

740420, 740113

-

1.3.1.43

prephenate + NAD(P)+ = ?

390803, 390802, 390512, 390804, 390782

-

1.3.1.43

prephenate + NAD+ = ?

390804

-

1.3.1.78

prephenate + NAD(P)+ = ?

390557, 390781, 390801

-

1.3.1.78

prephenate + NADP+ = 3-(4-hydroxyphenyl)-2-oxopropanoate + CO2 + NADPH

655440

-

1.3.1.12

6 entries

1.3.1.13

2 entries

1.3.1.43

2 entries

1.3.1.78

2 entries

1.3.1.79

prephenate + NAD(P)+ = p-hydroxyphenylpyruvate + NAD(P)H + CO2

684578

-

2.6.1.17

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

738632

-

2.6.1.42

L-leucine + prephenate = 2-oxoisohexanoate + 1-(2-amino-2-carboxyethyl)-4-hydroxycyclohexa-2,5-diene-1-carboxylic acid

640007

-

2.6.1.5

L-tyrosine + prephenate = ?

721558

-

2.6.1.57

prephenate + L-glutamate = 1-carboxy-4-hydroxy-2,5-cyclohexadien-1-alanine + 2-oxoglutarate

636657, 636653

-

2.6.1.57

prephenate + L-tryptophan = 1-carboxy-4-hydroxy-2,5-cyclohexadien-1-alanine + 3-indole-2-oxopropanoate

636657

-

2.6.1.57

prephenate + Asp = arogenate + 2-oxosuccinate

662080

-

2.6.1.57

prephenate + Glu = arogenate + 2-oxoglutarate

662080

-

2.6.1.57

prephenate + Phe = arogenate + phenylpyruvate

662080

-

2.6.1.57

prephenate + Tyr = arogenate + 4-hydroxyphenylpyruvate

662080

-

2.6.1.78

prephenate + L-aspartate = L-arogenate + oxaloacetate

722267, 657636

-

2.6.1.78

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

657636

-

2.6.1.79

prephenate + L-aspartate = L-arogenate + oxaloacetate

657635, 660563, 659858

-

2.6.1.79

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

659858, 722267, 738632, 657635, 660563

-

2.6.1.79

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

738632

-

2.6.1.57

6 entries

2.6.1.78

2 entries

2.6.1.79

3 entries

4.1.1.100

prephenate = 3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2

729203, 729211, 729204

-

4.2.1.51

prephenate = phenylpyruvate + H2O + CO2

33888, 33889, 33872, 33880, 33881, 3543, 3558, 3570, 3574, 33877, 33878, 33886, 33887, 33891, 33895, 33896, 649980, 706236, 730847, 716582, 33890, 3566, 33901, 33870, 714881, 3575, 33874, 33875, 33885, 33899, 649516, 33892, 677342, 3542, 33883, 33879, 678167, 33897, 33898, 33876, 727742, 748952, 651653, 692260, 702720, 730200, 665625, 663605, 682402, 681657, 694629, 702472

-

4.2.1.51

prephenate = ?

33888, 33889, 33872, 33880, 33881, 3543, 3558, 3570, 3574, 33886, 33887, 33891, 33895, 33896, 33890, 3566, 33901, 33870, 3575, 33874, 33875, 33885, 33899, 33892, 3542, 33883, 33879, 33897, 33898, 33876, 33877, 33878

-

4.2.1.91

prephenate = phenylpyruvate + H2O + CO2

648479, 680833

-

4.2.1.91

prephenate = phenylpyruvate + CO2 + H2O

648479, 648475, 648477, 33892, 648474, 706157, 390805, 706229

-

4.2.1.51

2 entries

4.2.1.91

2 entries

Product in Enzyme-catalyzed Reactions (6 results)

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Show Product (6 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.6.1.78

L-arogenate + oxaloacetate = prephenate + L-aspartate

-

-

2.6.1.79

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

-

-

3.3.2.1

Chorismate = Prephenate

-

-

5.4.99.5

Chorismate = Prephenate

3541, 3534, 3562, 649126, 649938, 651595, 651598, 652061, 3535, 3543, 3544, 3557, 3558, 3559, 3560, 3563, 3564, 3565, 3568, 3570, 390552, 649832, 3553, 3567, 3569, 3571, 3572, 3573, 651660, 651936, 3545, 3539, 3554, 3561, 3547, 3566, 3546, 3538, 3556, 3542, 3551, 3552, 3536, 3555, 3533, 3537, 3540, 3549, 3550, 649515, 3548, 650528

1com, 3D-view

5.4.99.5

Chorismate = Prephenate

3541, 3534, 3562, 649126, 649938, 651595, 651598, 652061, 3535, 3543, 3544, 3557, 3558, 3559, 3560, 3563, 3564, 3565, 3568, 3570, 390552, 649832, 3553, 3567, 3569, 3571, 3572, 3573, 651660, 651936, 3545, 3539, 3554, 3561, 3547, 3566, 3546, 3538, 3556, 3542, 3551, 3552, 3536, 3555, 3533, 3537, 3540, 3549, 3550, 649515, 3548, 650528

3zp7, 3D-view

5.4.99.5

Chorismate = Prephenate

3541, 3534, 3562, 649126, 649938, 651595, 651598, 652061, 3535, 3543, 3544, 3557, 3558, 3559, 3560, 3563, 3564, 3565, 3568, 3570, 390552, 649832, 3553, 3567, 3569, 3571, 3572, 3573, 651660, 651936, 3545, 3539, 3554, 3561, 3547, 3566, 3546, 3538, 3556, 3542, 3551, 3552, 3536, 3555, 3533, 3537, 3540, 3549, 3550, 649515, 3548, 650528

5j6f, 3D-view

5.4.99.5

3 entries

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

4.1.3.27

slight activation in presence of His

33288

-

Inhibitor in Enzyme-catalyzed Reactions (23 results)

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Show Inhibitors (23 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.43

-

390782

-

1.3.1.43

competitive inhibition

390784

-

1.3.1.43

no inhibition

390512, 390785

-

1.3.1.78

no inhibition

390788

-

1.3.1.78

-

655440

-

2.5.1.54

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

639782

5j6f, 3D-view

2.5.1.54

50% at 0.02 mM; feedback inhibition, noncompetitive against D-erythrose 4-phosphate and phosphoenolpyruvate

639791

5j6f, 3D-view

2.5.1.54

1 mM, 3% residual activity

657873

5j6f, 3D-view

2.5.1.54

IC50: 0.1 mM

674736

5j6f, 3D-view

1.3.1.43

3 entries

1.3.1.78

2 entries

2.5.1.54

4 entries

2.6.1.57

substrate inhibition

636657

-

2.6.1.79

substrate inhibition above 1 mM, antagonism by L-glutamate

657635

-

2.6.1.79

substrate inhibition above 1 mM, 80% of maximal activity at 2 mM, 38% of maximal activity at 20 mM

659858

-

4.2.1.91

competitive inhibition

33892

-

4.2.1.91

competitive inhibition; competitive to L-arogenate; reaction with L-arogenate is inhibited

648479

-

5.4.99.5

competitive

3566, 3574

1com, 3D-view

5.4.99.5

competitive

3566, 3574

3zp7, 3D-view

5.4.99.5

competitive

3566, 3574

5j6f, 3D-view

5.4.99.5

competitive inhibition

390552

1com, 3D-view

5.4.99.5

competitive inhibition

390552

3zp7, 3D-view

5.4.99.5

competitive inhibition

390552

5j6f, 3D-view

5.4.99.5

-

693664

1com, 3D-view

5.4.99.5

-

693664

3zp7, 3D-view

5.4.99.5

-

693664

5j6f, 3D-view

2.6.1.79

2 entries

4.2.1.91

2 entries

5.4.99.5

9 entries

3D Structure of Enzyme-Ligand-Complex (PDB) (4 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (4 entries)

EC NUMBER

ENZYME 3D STRUCTURE

2.5.1.54

5j6f, 3D-view

5.4.99.5

1com, 3D-view

5.4.99.5

3zp7, 3D-view

5.4.99.5

5j6f, 3D-view

5.4.99.5

3 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (70 results)

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Show Turnover Number (70 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.3.1.12

0.00005

-

mutant enzyme H197N

390552

1.3.1.12

0.0034

-

mutant H147N, pH 7.5, 55°C

698889

1.3.1.12

0.1

-

with NAD+ as cosubstrate, pH 7.6 and 37°C

746929

1.3.1.12

0.383

-

mutant enzyme K37Q

390552

1.3.1.12

0.417

-

mutant form R294Q

390553

1.3.1.12

0.45

-

wild-type enzyme

390552

1.3.1.12

0.45

-

wild-type enzyme

390553

1.3.1.12

0.5

-

mutant H217N, pH 7.5, 55°C

698889

1.3.1.12

0.8

-

mutant H217A, pH 7.5, 55°C; mutant S126A, pH 7.5, 55°C

698889

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

3.09

-

with NAD+ as cosubstrate, pH 7.6 and 37°C

746929

1.3.1.12

6.8

-

at 55°C, wild-type

677010

1.3.1.12

9.9

-

mutant R250Q, pH 7.5, 55°C

698889

1.3.1.12

10.08

-

pH 8.0, 45°C

723959

1.3.1.12

10.5

-

pH 6.8, 37°C

726409

1.3.1.12

13

-

at 55°C, delta19PD

677010

1.3.1.12

13

-

wild-type, pH 7.5, 55°C

698889

1.3.1.12

35

-

at pH 7.2 and 30°C

740113

1.3.1.12

68

-

at 80°C, delta19PD

677010

1.3.1.12

135

-

-

390522

1.3.1.12

170.4

-

-

676965

1.3.1.13

15

-

at pH 8.0 and 80°C

740113

1.3.1.13

21.8

-

at 37°C, pH not specified in the publication

741040

1.3.1.13

26.3

-

at 37°C, pH not specified in the publication

741040

1.3.1.12

23 entries

1.3.1.13

3 entries

1.3.1.78

3.4

-

-

655440

2.6.1.17

24

-

pH 8.0, 30°C

738632

2.6.1.79

24

-

cosubstrate N-succinyl-L-2,6-diaminoheptanedioate, pH 8.0, 30°C

738632

2.6.1.79

43

-

pH 8.0, 30°C

738632

2.6.1.79

54

-

cosubstrate L-glutamate, pH 8.0, 30°C

738632

2.6.1.79

60

-

pH 8.0, 30°C

738632

4.1.1.100

3.2

-

pH 8, 22°C

729204

4.1.1.100

4.1

-

pH and temperature not specified in the publication

729203

4.2.1.51

0.01

-

mutant F185Y, pH 7.5, 30°C; mutant T183S, pH 7.5, 30°C

649516

4.2.1.51

0.03

-

mutant S99A, pH 7.5, 30°C

649516

4.2.1.51

0.031

-

pH 8.0, 37°C, prephenate dehydratase Cmut1

748952

4.2.1.51

0.036

-

pH 8.0, 37°C, prephenate dehydratase Gmut11

748952

4.2.1.51

0.04

-

pH 8.0, 37°C; pH 8.0, 37°C, prephenate dehydratase Gmut9

748952

4.2.1.51

0.09

-

mutant S99C, pH 7.5, 30°C

649516

4.2.1.51

0.11

-

mutant S99T, pH 7.5, 30°C

649516

4.2.1.51

0.12

-

mutant S99M, pH 7.5, 30°C; wild-type enzyme, pH 7.5, 30°C

649516

4.2.1.51

0.13

-

mutant R184L, pH 7.5, 30°C

649516

4.2.1.51

0.21

-

mutant E164D, pH 7.5, 30°C

649516

4.2.1.51

0.3539

-

pH 8.0, 37°C

748952

4.2.1.51

0.7158

-

pH 8.0, 37°C

748952

4.2.1.51

12.3

-

30°C

678167

4.2.1.51

13

-

mutant N160A, 37°C

649980

4.2.1.51

24.6

-

mutant T278S, 37°C

649980

4.2.1.51

1227

-

mutant W226L, 37°C

649980

4.2.1.51

1230

-

mutant W226L, 37°C

649980

4.2.1.51

1890

-

recombinant prephenate dehydratase domain, 37°C

649980

4.2.1.51

1893

-

recombinant prephenate dehydratase domain, 37°C

649980

4.2.1.51

1930

-

native P-protein, 37°C

649980

4.2.1.51

1932

-

native P-protein, 37°C

649980

4.2.1.51

2096

-

mutant C216S, 37°C

649980

4.2.1.51

2100

-

mutant C216S, 37°C

649980

4.2.1.51

2400

-

mutant E232A, 37°C

649980

4.2.1.51

2401

-

mutant E232A, 37°C

649980

4.2.1.51

2528

-

mutant E159A, 37°C

649980

4.2.1.51

2530

-

mutant E159A, 37°C

649980

4.2.1.51

2960

-

mutant E159A/E232A, 37°C

649980

4.2.1.51

2962

-

mutant E159A/E232A, 37°C

649980

4.2.1.91

0.012

-

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

706229

4.2.1.91

0.03

-

37°C

680833

4.2.1.91

0.04

-

37°C

680833

4.2.1.91

0.06

-

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

706229

4.2.1.91

0.16

-

37°C

680833

5.4.99.5

94100

-

37°C, pH 7.8, in presence of P-protein

650528

5.4.99.5

94140

-

37°C, pH 7.8, in presence of P-protein

650528

2.6.1.79

4 entries

4.1.1.100

2 entries

4.2.1.51

29 entries

4.2.1.91

5 entries

5.4.99.5

2 entries

K_M Value (107 results)

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Show KM Value (107 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

0.045

0.09

-

33883, 3557, 390513, 390522, 390535, 390548, 390549, 390552, 390553

1.3.1.12

0.048

-

at pH 7.2 and 30°C

740113

1.3.1.12

0.054

0.055

mutant forms K37Q and H197N

390552

1.3.1.12

0.097

-

at 55°C, wild-type

677010

1.3.1.12

0.104

-

mutant H147N, pH 7.5, 55°C

698889

1.3.1.12

0.11

-

presence of bovine serum albumin

390530

1.3.1.12

0.135

-

at 55°C, delta19PD

677010

1.3.1.12

0.135

-

wild-type, pH 7.5, 55°C

698889

1.3.1.12

0.136

-

at 80°C, wild-type

677010

1.3.1.12

0.22

-

-

33876

1.3.1.12

0.249

-

at 80°C, delta19PD

677010

1.3.1.12

0.25

-

with NAD+ as cosubstrate, at pH 7.6 and 37°C

746929

1.3.1.12

0.32

-

with NAD+ as cosubstrate, at pH 7.6 and 37°C

746929

1.3.1.12

0.35

0.37

-

390537, 390539, 390542

1.3.1.12

0.41

-

-

676965

1.3.1.12

0.45

-

pH 6.5, 87°C

692260

1.3.1.12

0.56

-

cofactor NADP+

390551

1.3.1.12

0.57

-

cofactor NAD+

390551

1.3.1.12

0.75

-

pH 6.8, 37°C

726409

1.3.1.12

0.83

-

-

33885

1.3.1.12

0.87

-

pH 8.0, 45°C

723959

1.3.1.12

1.185

-

mutant R250Q, pH 7.5, 55°C

698889

1.3.1.12

1.335

-

mutant S126A, pH 7.5, 55°C

698889

1.3.1.12

2

-

-

390513

1.3.1.12

2

-

-

390550

1.3.1.12

3.213

-

mutant H217N, pH 7.5, 55°C

698889

1.3.1.12

4.132

-

mutant H217A, pH 7.5, 55°C

698889

1.3.1.12

5

-

mutant form R294Q

390553

1.3.1.13

0.033

-

-

390560

1.3.1.13

0.077

-

-

390557

1.3.1.13

0.127

-

at 37°C, pH not specified in the publication

741040

1.3.1.13

0.13

-

-

390556

1.3.1.13

0.18

-

-

390556

1.3.1.13

0.223

-

at 37°C, pH not specified in the publication

741040

1.3.1.13

0.319

-

at pH 8.0 and 80°C

740113

1.3.1.13

0.319

-

with NAD+ as cosubstrate, at pH 8.0 and 80°C

740420

1.3.1.13

0.443

-

with NADP+ as cosubstrate, at pH 8.0 and 80°C

740420

1.3.1.13

0.69

-

with NAD+ as cosubstrate, at pH 8.0 and 80°C

740420

1.3.1.13

0.73

-

with NADP+ as cosubstrate, at pH 8.0 and 80°C

740420

1.3.1.43

0.07

-

-

390802

1.3.1.43

0.07

-

-

390803

1.3.1.43

0.25

-

-

390804

1.3.1.12

30 entries

1.3.1.13

11 entries

1.3.1.43

3 entries

1.3.1.78

17

-

-

655440

2.6.1.17

0.021

-

pH 8.0, 30°C

738632

2.6.1.42

1.4

-

pH 7.5, 25°C

640007

2.6.1.57

0.08

-

pH 8.6, 37°C, AAT I

636657

2.6.1.78

0.08

-

pH 9.0, 40°C

657636

2.6.1.79

0.02

-

cosubstrate L-glutamate, pH 8.0, 30°C

738632

2.6.1.79

0.021

-

cosubstrate N-succinyl-L-2,6-diaminoheptanedioate, pH 8.0, 30°C

738632

2.6.1.79

0.07

-

pH 8.0

660563

2.6.1.79

0.1

-

pH 8.0, 30°C

738632

2.6.1.79

0.13

-

pH 8.0, 30°C

738632

4.1.1.100

0.07

-

pH 8, 22°C

729204

4.1.1.100

0.17

-

pH and temperature not specified in the publication

729203

4.2.1.51

0.01

-

presence of 1 mM L-Trp

33879

4.2.1.51

0.015

-

presence of 1 mM L-Tyr

33879

4.2.1.51

0.017

-

presence of 1 mM L-Phe

33879

4.2.1.51

0.02

-

presence of L-Tyr

33890

4.2.1.51

0.022

-

30°C

678167

4.2.1.51

0.07

-

wild-type enzyme, pH 7.5, 30°C

649516

4.2.1.51

0.08

-

mutant S99T, pH 7.5, 30°C

649516

4.2.1.51

0.09

-

mutant S99C, pH 7.5, 30°C

649516

4.2.1.51

0.1

-

-

33885

4.2.1.51

0.12

-

mutant E159A/E232A, 37°C

649980

4.2.1.51

0.13

-

mutant S99A, pH 7.5, 30°C

649516

4.2.1.51

0.15

-

pH 8.0, 37°C

748952

4.2.1.51

0.16

-

mutant E232A, 37°C

649980

4.2.1.51

0.17

-

-

33892

4.2.1.51

0.18

-

mutant S99M, pH 7.5, 30°C

649516

4.2.1.51

0.25

-

mutant E159A, 37°C

649980

4.2.1.51

0.29

-

mutant E164D, pH 7.5, 30°C

649516

4.2.1.51

0.3

-

pH 8.0, 37°C, prephenate dehydratase Cmut1

748952

4.2.1.51

0.33

-

-

33876

4.2.1.51

0.34

-

pH 8.0, 37°C

748952

4.2.1.51

0.46

-

mutant T183S, pH 7.5, 30°C

649516

4.2.1.51

0.47

1

-

3574

4.2.1.51

0.5

-

-

665625

4.2.1.51

0.56

-

native P-protein, 37°C

649980

4.2.1.51

0.57

-

mutant T278S, 37°C

649980

4.2.1.51

0.61

-

mutant R184L, pH 7.5, 30°C

649516

4.2.1.51

0.65

-

recombinant prephenate dehydratase domain, 37°C

649980

4.2.1.51

0.67

-

-

33883

4.2.1.51

1

-

-

33886

4.2.1.51

1.2

-

absence of L-Tyr

33890

4.2.1.51

1.2

-

pH and temperature not specified in the publication

727742

4.2.1.51

1.3

-

77°C, pH not specified in the publication

692260

4.2.1.51

1.65

-

mutant N160A, 37°C

649980

4.2.1.51

1.73

-

mutant F185Y, pH 7.5, 30°C

649516

4.2.1.51

2.09

-

mutant C216S, 37°C

649980

4.2.1.51

2.11

-

pH 8.0, 37°C, prephenate dehydratase Gmut11

748952

4.2.1.51

2.15

-

pH 8.0, 37°C, prephenate dehydratase Gmut9

748952

4.2.1.51

2.29

-

wild-type, rice PDT is a bifunctional enzyme

694629

4.2.1.51

2.72

-

pH 8.0, 37°C

748952

4.2.1.51

3

-

above, mutant W226L, 37°C

649980

4.2.1.51

4.88

-

mutant S298I, rice PDT is a bifunctional enzyme

694629

4.2.1.91

0.17

-

pH 7.2, 37°C

33892

4.2.1.91

0.4

-

enzyme purified directly from Pseudomonas aeruginosa

648479

4.2.1.91

0.42

-

pH 7.5, 22°C; pH 7.5, 37°C; recombinant protein, purified from Escherichia coli

648479

4.2.1.91

0.4658

-

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

706229

4.2.1.91

0.68

-

37°C

680833

4.2.1.91

0.752

-

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

706229

4.2.1.91

0.8

-

37°C

680833

4.2.1.91

2.44

-

37°C

680833

5.4.99.5

0.47

1

-

3574

5.4.99.5

0.549

-

37°C, pH 7.8, in presence of P-protein

650528

2.6.1.79

5 entries

4.1.1.100

2 entries

4.2.1.51

41 entries

4.2.1.91

8 entries

5.4.99.5

2 entries

K_i Value (9 results)

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Show KI Value (9 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

TABLE ID

1.3.1.78

2.4

-

pH 7.5, 25°C, with 0.1 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT2

655440

2852

1.3.1.78

4.2

-

pH 7.5, 25°C, with 0.1 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT1

655440

2853

1.3.1.78

20.2

-

pH 7.5, 25°C, with 0.07 mM arogenate as fixed substrate and NADP+ as varied substrate, TyrAAT1

655440

2856

1.3.1.78

22.5

-

pH 7.5, 25°C, with 0.07 mM arogenate as fixed substrate and NADP+ as varied substrate, TyrAAT2

655440

2857

2.6.1.57

0.4

-

AAT I and III, substrate inhibition; AAT I, substrate inhibition

636657

13904

2.6.1.57

15

-

AAT II, substrate inhibition

636657

13909

1.3.1.78

4 entries

2.6.1.57

2 entries

4.2.1.91

0.4

-

; pH 7.5, 22°C; pH 7.5, 37°C

648479

39652

5.4.99.5

0.07

-

dimeric chorismate mutase, at 20°C

693664

41330

5.4.99.5

0.17

-

monomeric chorismate mutase, at 20°C

693664

41331

5.4.99.5

2 entries

IC₅₀ Value (1 result)

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Show IC50 Value (1 entry)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

2.5.1.54

0.1

-

IC50: 0.1 mM

674736

References & Links

Literature References (195)

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Show Reference (195 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

3533

5443801

Eigenschaften der Chorismat-Mutase aus verschiedenen Claviceps-Staemmen

1970

Sproessler, B.; Lingens, F.

Hoppe-Seyler's Z. Physiol. Chem.

351

448-459

3534

4962500

Multiple molecular forms of chorismate mutase in Bacillus subtilis

1967

Lorence, J.H.; Nester, E.W.

Biochemistry

6

1541-1553

3535

14323651

The biosynthesis of phenylalanine and tyrosine enzymes converting chorismic acid into prephenic acid and their relationships to prephenate dehydratase and prephenate dehydrogenase

1965

Cotton, R.G.H.; Gibson, F.

Biochim. Biophys. Acta

100

76-88

3536

5024635

Properties of chorismate mutase of Streptomyces venezuelae

1972

Görisch, H.; Lingens, F.

Arch. Microbiol.

82

147-154

3537

4196250

Chorismate mutase from Streptomyces aureofaciens: a heat-stable enzyme

1973

Görisch, H.; Lingens, F.

J. Bacteriol.

114

645-651

3538

4708674

Evidence for three isoenzymes of chorismate mutase in alfalfa

1973

Woodin, T.S.; Nishioka, L.

Biochim. Biophys. Acta

309

211-223

3539

4267751

Chorismate mutase isozyme patterns in three fungi

1973

Woodin, T.S.; Nishioka, L.

Biochim. Biophys. Acta

309

224-231

3540

4211872

Chorismate mutase from Streptomyces. Purification, properties, and subunit structure of the enzyme from Streptomyces aureofaciens Tu 24

1974

Görisch, H.; Lingens, F.

Biochemistry

13

3790-3794

3541

1122289

Chorismate mutase of Chlamydomonas reinhardi. Partial purification and some properties

1975

Zurawski, G.; Brown, K.D.

Biochim. Biophys. Acta

377

473-481

3542

1262315

Purification and properties of chorismate mutase-prephenate dehydratase and prephenate dehydrogenase from Alcaligenes eutrophus

1976

Friedrich, B.; Friedrich, C.G.; Schlegel, H.G.

J. Bacteriol.

126

712-722

3543

795664

Chorismate mutase/prephenate dehydratase from Escherichia coli K12. 1. The effect of NaCl and its use in a new purification involving affinity chromatography on sepharosyl-phenylalanine

1976

Gething, M.J.; Davidson, B.E.; Dopheide, T.A.A.

Eur. J. Biochem.

71

317-325

3544

795665

Chorismate mutase/prephenate dehydratase from Escherichia coli K12. 2. Evidence for identical subunits catalysing the two activities

1976

Gething, M.J.; Davidson, B.E.

Eur. J. Biochem.

71

327-336

3545

16660432

Comparison of chorismate mutase isozyme patterns in selected plants

1978

Woodin, T.S.; Nishioka, L.; Hsu, A.

Plant Physiol.

61

949-952

3546

479120

Two components of chorismate mutase in Brevibacterium flavum

1979

Shiio, I.; Sugimoto, S.

J. Biochem.

86

17-25

3547

7093222

Inhibition of chorismate mutase activity of chorismate mutase-prephenate dehydrogenase from Aerobacter aerogenes

1982

Chao, H.S.I.; Berchtold, G.A.

Biochemistry

21

2778-2781

3548

7049179

Chorismate mutase-catalyzed reaction of (+/-)-chorismic acid

1982

Hoare, J.H.; Berchtold, G.A.

Biochem. Biophys. Res. Commun.

106

660-662

3549

24254043

Subcellular localization of chorismate-mutase isoenzymes in protoplasts from mesophyll and suspension-cultured cells of Nicotiana silvestris

1984

d'Amato, T.A.; Ganson, R.J.; Gaines, C.G.; Jensen, R.A.

Planta

162

104-108

3550

24254044

Separation and characterization of two chorismate-mutase isoenzymes from Nicotiana silvestris

1984

Goers, S.K.; Jensen, R.A.

Planta

162

109-116

3551

4083892

Chorismate mutase isoenzymes from Sorghum bicolor: purification and properties

1985

Singh, B.K.; Connelly, J.A.; Conn, E.E.

Arch. Biochem. Biophys.

243

374-384

3552

3085591

Chorismate mutase isoenzymes from Sorghum bicolor: immunologicical characterization

1986

Singh, B.K.; Conn, E.E.

Arch. Biochem. Biophys.

246

617-621

3553

3027508

Chorismate mutase-prephenate dehydratase from Escherichia coli

1986

Ball, S.G.; Wickner, R.B.; Cottarel, G.; Schmaus, M.; Tirtiaux, C.

Mol. Gen. Genet.

205

326-330

3554

3341760

Purification and characterization of an inducible aromatic amino acid-sensitive form of chorismate mutase from Solanum tuberosum L. tubers

1988

Kuroki, G.W.; Conn, E.E.

Arch. Biochem. Biophys.

260

616-621

3555

3037265

Chorismate mutase from Streptomyces aureofaciens

1987

Görisch, H.

Methods Enzymol.

142

463-472

3556

-

Chorismate mutase from mung bean and Sorghum

1987

Gilchrist, D.G.; Connelly, J.A.

Methods Enzymol.

142

450-463

3557

3298984

Chorismate mutase-prephenate dehydrogenase from Escherichia coli

1987

Davidson, B.E.; Hudson, G.S.

Methods Enzymol.

142

440-450

3558

-

Chorismate mutase/prephenate dehydratase from Escherichia coli: subcloning, overproduction and purification

1991

Stewart, J.; Wilson, D.B.; Ganem, B.

Tetrahedron

47

2573-2577

3559

-

Chorismate mutase inhibitors: synthesis and evaluation of some potential transition-state analogues

1988

Bartlett, P.A.; Nakagawa, Y.; Johnson, C.R.; Reich, S.H.; Luis, A.

J. Org. Chem.

53

3195-3210

3560

-

A genetically engineered monofunctional chorismate mutase

1990

Stewart, J.; Wilson, D.B.; Ganem, B.

J. Am. Chem. Soc.

112

4582-4584

3561

8953244

Cytosolic and plastidic chorismate mutase isoenzymes from Arabidopsis thaliana: molecular characterization and enzymatic properties

1996

Eberhard, J.; Ehrler, T.T.; Epple, P.; Felix, G.; Raesecke, H.R.; Amrhein, N.; Schmid, J.

Plant J.

10

815-821

3562

2105742

Monofunctional chorismate mutase from Bacillus subtilis: purification of the protein, molecular cloning of the gene, and overexpression of the gene product in Escherichia coli

1990

Gray, J.V.; Golinelli-Pimpaneau, B.; Knowles, J.R.

Biochemistry

29

376-383

3563

9636050

Thermodynamics of a transition state analogue inhibitor binding to Escherichia coli chorismate mutase: probing the charge state of an active site residue and its role in inhibitor binding and catalysis

1998

Lee, A.Y.; Zhang, S.; Kongsaeree, P.; Clardy, J.; Ganem, B.; Erickson,J.W.; Xie, D.

Biochemistry

37

9052-9057

3564

-

Purification and characterization of chorismate mutase isoenzymes from Ruta graveolens

1991

Hertel, S.C.; Hieke, M.; Gröger, D.

Acta Biotechnol.

11

39-48

3565

8224252

Cloning and expression in yeast of a higher plant chorismate mutase. Molecular cloning, sequencing of the cDNA and characterization of the Arabidopsis thaliana enzyme expressed in yeast

1993

Eberhard, J.; Raesecke, H.R.; Schmid, J.; Amrhein, N.

FEBS Lett.

334

233-236

3566

3046943

Chorismate mutase: prephenate dehydratase from Acinetobacter calcoaceticus. Purification, properties and immunological cross-reactivity

1988

Ahmad, S.; Wilson, A.T.; Jensen, R.A.

Eur. J. Biochem.

176

69-79

3567

7971967

The crystal structure of allosteric chorismate mutase at 2.2-A resolution

1994

Xue, Y.; Lipscomb, W.N.; Graf, R.; Schnappauf, G.; Braus, G.

Proc. Natl. Acad. Sci. USA

91

10814-10818

3568

8831972

Site-directed mutagenesis of monofunctional chorismate mutase engineered from the E. coli P-protein

1996

Zhang, S.; Kongaeree, P.; Clardy, J.; Wilson, D.B.; Ganem, B.

Bioorg. Med. Chem.

4

1015-1020

3569

8057366

The crystallization and preliminary X-ray analysis of allosteric chorismate mutase

1994

Xue, Y.; Lipscomb, W.N.

J. Mol. Biol.

241

273-274

3570

9497350

Chorismate mutase-prephenate dehydratase from Escherichia coli. Study of catalytic and regulatory domains using genetically engineered proteins

1998

Zhang, S.; Pohnert, G.; Kongsaeree, P.; Wilson, D.B.; Clardy, J.; Ganem, B.

J. Biol. Chem.

273

6248-6253

3571

9384560

Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures

1997

Sträter, N.; Schnappauf, G.; Braus, G.; Lipscomb, W.N.

Structure

5

1437-1452

3572

9501182

Separation of inhibition and activation of the allosteric yeast chorismate mutase

1998

Schnappauf, G.; Lipscomb, W.N.; Braus, G.H.

Proc. Natl. Acad. Sci. USA

95

2868-2873

3573

8622937

Crystal structure of the T state of allosteric yeast chorismate mutase and comparison with the R state

1996

Sträter, N.; Hakansson, K.; Schnappauf, G.; Braus, G.; Lipscomb, W.N.

Proc. Natl. Acad. Sci. USA

93

3330-3334

3574

3037264

Chorismate mutase-prephenate dehydratase from Escherichia coli

1987

Davidson, B.E.

Methods Enzymol.

142

432-439

3575

1780276

Purification of prephenate dehydratase from Corynebacterium glutamicum by affinity chromatography

1991

Bertaux, S.; Harrison, R.G.

Prep. Biochem.

21

269-275

33288

-

Zur Charakterisierung der Anthranilat-Synthetase bei Claviceps

1976

Schmauder, H.P.; Gröger, D.

Biochem. Physiol. Pflanz.

169

471-486

33870

11540103

An extreme-halophile archaebacterium possesses the interlock type or prephenate dehydratase characteristic of gram-positive eubacteria

1988

Jensen, R.A.; d'Amato, T.A.; Hochstein, L.I.

Arch. Microbiol.

148

365-371

33872

3110557

Prephenate dehydratase (monofunctional)

1987

Fischer, R.; Jensen, R.

Methods Enzymol.

142

507-512

33874

3525519

Molecular cloning and nucleotide sequence of the Corynebacterium glutamicum pheA gene

1986

Follettie, M.T.; Sinskey, A.J.

J. Bacteriol.

167

695-702

33875

-

Cloning of the genes concerend in phenylalanine biosynthesis in Corynebacterium glutamicum and its application to breeding of a phenylalanine producing strain

1985

Ozaki, A.; Katsumata, R.; Oka, T.; Furuya, A.

Agric. Biol. Chem.

49

2925-2930

33876

-

Regulation of chorismate mutase, prephenate dehydrogenase and prephenate dehydratase of Candida maltosa

1985

Bode, R.; Melo, C.; Birnbaum, D.

J. Basic Microbiol.

25

291-298

33877

6337635

Kinetic studies on the mechanism of chorismate mutase/prephenate dehydratase from Escherichia coli K12

1983

Baldwin, G.S.; Davidson, B.E.

Biochim. Biophys. Acta

742

374-383

33878

7030215

The self-association of chorismate mutase/prephenate dehydratase from Escherichia coli K12

1981

Baldwin, G.S.; McKenzie, G.H.; Davidson, B.E.

Arch. Biochem. Biophys.

211

76-85

33879

7399403

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