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Ligand 2-oxohexanoic acid

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Product in Enzyme-catalyzed Reactions (5 results)

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Show Natural Product (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.15

2-hydroxycaproate + O2 = 2-oxocaproate + H2O2

0

-

1.1.3.15

DL-2-hydroxycaproate + O2 = 2-oxocaproate + H2O2

389685, 389691, 389693, 389698, 389700, 389699

-

1.1.3.15

2 entries

1.4.3.2

DL-norleucine + H2O + O2 = 2-oxocaproate + NH3 + H2O2

0

-

1.4.3.3

D-norleucine + H2O + O2 = 2-oxohexanoate + NH3 + H2O2

0

-

2.6.1.67

L-norleucine + 2-oxoglutarate = 2-oxohexanoate + L-glutamate

0, 640188

-

Substrate in Enzyme-catalyzed Reactions (68 results)

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Show Substrate (68 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.28

2-ketocaproate + NADH = 2-hydroxycaproate + NAD+

669152

-

1.1.1.28

2-oxocaproate + NADH + H+ = 2-hydroxycaproate + NAD+

739841

-

1.1.1.28

2 entries

1.1.1.337

2-oxocaproate + NADH + H+ = 2-hydroxycaproate + NAD+

726750, 727405, 728726

-

1.1.1.345

2-oxocaproate + NADH + H+ = ?

722588

-

1.1.1.345

2-oxocaproate + NADH + H+ = ? + NAD+

712292

-

1.1.1.345

2-oxohexanoate + NADH + H+ = 2-hydroxyhexanoate + NAD+

685675, 729022, 731741, 731190, 731727

-

1.1.1.345

3 entries

1.1.1.379

2-oxocaproate + NADH + H+ = ? + NAD+

762694

-

1.1.1.428

2-oxocaproate + NADH + H+ = ?

764063

-

1.14.20.1

ampicillin + 2-oxohexanoate + O2 = cephalexin + ?

440371

-

1.14.20.1

penicillin G + 2-oxohexanoate + O2 = phenylacetyl-7-aminodeacetoxy cephalosporanic acid + ?

440368, 440371

-

1.14.20.1

ampicillin + 2-oxohexanoic acid + O2 = ?

440371

-

1.14.20.1

penicillin G + 2-oxohexanoic acid + O2 = phenylacetyl-7-aminodeacetoxycephalosporanic acid + pentanoate + CO2 + H2O

440371

-

1.14.20.1

4 entries

1.2.7.7

2-ketocaproate + CoA + oxidized ferredoxin = pentanoyl-CoA + CO2 + reduced ferredoxin

644696

-

1.4.1.1

2-ketocaproate + NH3 + NADH = 2-aminocaproate + H2O + NAD+

349555, 655887

-

1.4.1.2

2-oxocaproate + NH3 + NADH + H+ = L-2-aminohexanoate + H2O + NAD+

742464

-

1.4.1.20

2-oxohexanoate + NH3 + NADH = 2-aminohexanoate + H2O + NAD+

349634, 349649, 349647, 349635, 349638

-

1.4.1.20

alpha-ketocaproic acid + NH3 + NADH = alpha-aminocaproic acid + H2O + NAD+

656887

-

1.4.1.20

2 entries

1.4.1.23

2-oxohexanoate + NH3 + NADH + H+ = L-norleucine + H2O + NAD+

391694, 391690, 717267

-

1.4.1.9

2-ketocaproate + NH3 + NADH = L-2-aminohexanoate + H2O + NAD+

656565

-

1.4.1.9

2-oxohexanoate + NH3 + NADH + H+ = L-norleucine + H2O + NAD+

656569, 349685

-

1.4.1.9

2-oxohexanoate + NH3 + NADH = L-norleucine + H2O + NAD+

695691

-

1.4.1.9

alpha-ketocaproate + NH3 + NADH + H+ = L-norleucine + H2O + NAD+

693504

-

1.4.1.9

4 entries

1.5.1.21

alpha-ketohexanoate + methylamine + NADPH = N-methyl-2-aminohexanoate + NADP+ + H2O

674509

-

1.5.1.23

Taurine + 2-oxohexanoate + NADH = ?

13440

-

1.5.1.28

L-Met + 2-oxohexanoate + NADH = ?

94167

-

2.2.1.1

pentanal + 2-oxohexanoic acid = 6-hydroxydecan-5-one + CO2

756713

-

2.3.3.17

2-oxohexanoate + acetyl-CoA + H2O = 2-butylmalate + CoA

741215

-

2.6.1.12

L-alanine + 2-oxohexanoate = pyruvate + 2-aminohexanoate

636593

-

2.6.1.18

3-amino-5-methylhexanoate + 2-oxohexanoate = 3-oxo-5-methylhexanoate + 2-aminohexanoate

738138

-

2.6.1.18

beta-alanine + 2-oxohexanoate = malonic semialdehyde + L-norleucine

288059

-

2.6.1.28

L-phenylalanine + 2-oxohexanoate = phenylpyruvate + L-norleucine

639949

-

2.6.1.28

L-tryptophan + 2-oxohexanoate = 3-indole-2-oxopropanoate + L-norleucine

639949

-

2.6.1.18

2 entries

2.6.1.28

2 entries

2.6.1.36

L-lysine + 2-oxohexanoate = 2-aminoadipate 6-semialdehyde + 2-aminohexanoate

637018

-

2.6.1.38

histidine + 2-oxocaproate = imidazol-5-yl-pyruvate + L-norleucine

639973

-

2.6.1.42

L-leucine + 2-oxo-hexanoate = 2-oxoisohexanoate + 2-aminohexanoate

640019

-

2.6.1.42

L-norvaline + 2-oxocaproate = 2-oxopentanoate + 2-aminohexanoate

738188

-

2.6.1.42

2-oxohexanoate + L-glutamate = L-norleucine + 2-oxoglutarate

738209, 758768, 758848

-

2.6.1.42

2-oxohexanoate + L-glutamate = norleucine + 2-oxoglutarate

758768

-

2.6.1.42

L-allo-isoleucine + 2-oxohexanoate = 3-methyl-2-oxopentanoate + 2-aminohexanoate

640021

-

2.6.1.42

L-isoleucine + 2-oxohexanoate = L-norleucine + 2-oxoisohexanoate

640021

-

2.6.1.42

L-leucine + 2-oxohexanoate = 2-oxoisohexanoate + 2-aminohexanoate

640021

-

2.6.1.42

L-valine + 2-oxohexanoate = 2-oxoisopentanoate + 2-aminohexanoate

640021

-

2.6.1.42

L-leucine + 2-oxohexanoic acid = 4-methyl-2-oxopentanoate + 2-aminohexanoic acid

661957

-

2.6.1.42

9 entries

2.6.1.5

L-tyrosine + 2-oxohexanoate = 3-(4-hydroxyphenyl)-2-oxopropanoate + (2S)-2-aminohexanoate

723682

-

2.6.1.50

L-glutamine + 2-oxocaproate = 2-oxoglutaramate + L-norleucine

640128

-

2.6.1.64

L-glutamine + alpha-keto-n-caproate = 2-oxoglutaramate + L-norleucine

639901

-

2.6.1.64

L-phenylalanine + alpha-keto-n-caproate = phenylpyruvate + L-norleucine

639901

-

2.6.1.7

L-kynurenine + 2-oxocaproate = ?

702779, 746952

-

2.6.1.7

L-kynurenine + 2-oxocaproic acid = ?

705702

-

2.6.1.7

L-kynurenine + 2-oxocaproic acid = kynurenic acid + 2-aminohexanoate

721881

-

2.6.1.7

L-kynurenine + 2-oxohexanoate = kynurenic acid + L-norleucine + H2O

636613

-

2.6.1.B21

2-oxo-hexanoate + isopropylamine = D-norleucine + acetone

759007

-

2.6.1.B21

(R)-alpha-methylbenzylamine + 2-oxohexanoate = acetophenone + L-norleucine

758848

-

2.6.1.B21

2-oxohexanoate + L-glutamate = norleucine + 2-oxoglutarate

758848

-

4.1.1.1

2-ketohexanoic acid = pentanal + CO2

666806

-

4.1.1.1

2-oxohexanoic acid = ?

705199

-

4.1.1.1

2-oxohexanoic acid = n-pentanal + CO2

705199

-

4.1.1.1

2-oxohexanoic acid = pentanal + CO2

678576

-

4.1.1.43

2-ketohexanoic acid = pentanal + CO2

680508

-

4.1.1.43

2-Oxohexanoate = Pentanal + CO2

4562, 4563

-

4.1.1.43

2-oxohexanoic acid = ?

714975

-

4.1.1.64

2-Oxohexanoate + DL-Ile = ?

4751

-

4.1.1.64

2-Oxohexanoate + L-Ala = ?

4751, 4748

-

4.1.1.7

2-ketohexanoate = valeraldehyde + CO2

702341

-

4.1.1.7

2-oxohexanoate = valeraldehyde + CO2

747471, 747171

-

4.1.1.7

2-oxohexanoic acid = valeraldehyde + CO2

666806

-

4.1.1.72

2-oxohexanoate = n-pentanal + CO2

693210

-

4.1.1.72

2-oxohexanoic acid = pentanal + CO2

663706, 677424

-

2.6.1.64

2 entries

2.6.1.7

4 entries

2.6.1.B21

3 entries

4.1.1.1

4 entries

4.1.1.43

3 entries

4.1.1.64

2 entries

4.1.1.7

3 entries

4.1.1.72

2 entries

Product in Enzyme-catalyzed Reactions (40 results)

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Show Product (40 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.337

2-hydroxycaproate + NAD+ = 2-oxocaproate + NADH + H+

0

-

1.1.1.345

L-2-hydroxycaproate + NAD+ = 2-oxocaproate + NADH + H+

0

-

1.1.1.345

2-hydroxyhexanoate + NAD+ = 2-oxohexanoate + NADH + H+

0

-

1.1.1.345

2 entries

1.1.2.3

(S)-2-hydroxyhexanoate + ferricytochrome c = 2-oxohexanoate + ferrocytochrome c

0

-

1.1.3.15

2-hydroxycaproate + O2 = 2-oxocaproate + H2O2

0

-

1.1.3.15

DL-2-hydroxycaproate + 2,6-dichlorophenolindophenol = 2-oxocaproate + reduced 2,6-dichlorophenolindophenol

389701

-

1.1.3.15

DL-2-hydroxycaproate + O2 = 2-oxocaproate + H2O2

389685, 389691, 389693, 389698, 389700, 389699

-

1.1.3.15

3 entries

1.1.99.2

2-hydroxy-n-hexanoate + NAD+ = 2-oxo-n-hexanoate + NADH + H+

0

-

1.1.99.31

(R,S)-2-hydroxyhexanoate + acceptor = 2-oxohexanoate + reduced acceptor

0

-

1.1.99.31

2-hydroxyhexanoate + acceptor = 2-oxohexanoate + reduced acceptor

0

-

1.1.99.31

2 entries

1.1.99.6

2(R)-hydroxyhexanoate + acceptor = 2-oxohexanoate + reduced acceptor

287840

-

1.4.1.1

L-norleucine + H2O + NADH + H+ = 2-oxohexanoate + NH3 + NAD+

0

-

1.4.1.20

L-2-aminohexanoic acid + H2O + NAD+ = 2-oxohexanoate + NADH + NH3

0

-

1.4.1.20

L-norleucine + H2O + NAD+ = 2-oxohexanoate + NH3 + NADH

0

-

1.4.1.20

L-norleucine + H2O + NAD+ = 2-oxohexanoic acid + NADH + NH3

0

-

1.4.1.23

L-norleucine + H2O + NAD+ = 2-oxocaproate + NADH + NH3

0

-

1.4.1.23

L-norleucine + H2O + NAD+ = 2-oxohexanoate + NH3 + NADH + H+

0

-

1.4.1.20

3 entries

1.4.1.23

2 entries

1.4.1.8

L-norleucine + H2O + NAD+ = 2-oxocaproate + NADH + NH3

391694, 349539, 0, 391690

-

1.4.1.9

L-norleucine + H2O + NAD+ = 2-oxohexanoate + NH3 + NADH

0, 349661, 349665, 349664, 349680, 349682

-

1.4.3.2

DL-norleucine + H2O + O2 = 2-oxocaproate + NH3 + H2O2

0

-

1.4.3.2

L-norleucine + H2O + O2 = 2-oxohexanoate + NH3 + H2O2

0

-

1.4.3.2

DL-norleucine + H2O + O2 = alpha-ketocaproate + NH3 + H2O2

651026

-

1.4.3.2

L-norleucine + H2O + O2 = alpha-ketocaproate + NH3 + H2O2

0

-

1.4.3.2

4 entries

1.4.3.3

D-norleucine + H2O + O2 = 2-oxohexanoate + NH3 + H2O2

0

-

1.4.99.6

D-norleucine + H2O + 2,6-dichlorophenolindophenol = 2-oxohexanoate + NH3 + reduced 2,6-dichlorophenolindophenol

394974

-

1.4.99.6

D-norleucine + H2O + methylene blue = 2-oxohexanoate + NH3 + reduced methylene blue

394974

-

1.4.99.6

2 entries

1.4.99.B3

L-norleucine + H2O + 2 cytochrome b = 2-oxohexanoate + NH3 + 2 reduced cytochrome b

0

-

2.6.1.12

pyruvate + L-norleucine = L-alanine + 2-oxohexanoate

636592, 636593

-

2.6.1.14

2-oxosuccinamic acid + L-norleucine = L-asparagine + 2-oxohexanoate

0

-

2.6.1.28

phenylpyruvate + L-norleucine = phenylalanine + 2-oxohexanoate

0

-

2.6.1.39

L-norleucine + 2-oxoglutarate = 2-oxohexanoate + L-glutamate

0

-

2.6.1.42

L-norleucine + 2-oxoglutarate = 2-oxohexanoate + L-glutamate

0, 639992, 639993, 639995, 639997

-

2.6.1.42

L-norleucine + 2-oxoisocaproate = 2-oxohexanoate + L-leucine

0

-

2.6.1.42

L-norleucine + 4-methyl-2-oxopentanoate = 2-oxohexanoate + L-leucine

0

-

2.6.1.42

L-norleucine + 4-methyl-2-oxovalerate = 2-oxohexanoate + L-leucine

0

-

2.6.1.42

norleucine + 2-oxoglutarate = 2-oxohexanoate + L-glutamate

0

-

2.6.1.42

5 entries

2.6.1.48

L-norleucine + 2-oxoglutarate = 2-oxohexanoate + L-glutamate

0

-

2.6.1.64

L-norleucine + phenylpyruvate = 2-oxohexanoate + L-phenylalanine

640176

-

2.6.1.67

L-norleucine + 2-oxoglutarate = 2-oxohexanoate + L-glutamate

0, 640188

-

2.6.1.7

L-norleucine + 2-oxoglutarate = 2-oxohexanoate + L-glutamate

636608

-

Inhibitor in Enzyme-catalyzed Reactions (8 results)

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Show Inhibitors (8 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.21

-

286247

-

1.1.1.345

substrate inhibition

731741

-

1.1.1.379

10 mM, 44.1% inhibition

730341

-

1.2.1.104

-

348956

-

2.6.1.13

-

637098

-

2.6.1.42

inhibition of transamination by the oxo substrate at below 10 mM

758768

-

2.7.11.4

-

349056, 640579

-

4.1.1.7

substrate inhibition

666806

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (63 results)

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Show Turnover Number (63 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.28

0.056

-

30°C, pH 5.5, mutant enzyme Y52L

669152

1.1.1.28

0.3

-

30°C, pH 5.5, mutant enzyme Y52V

669152

1.1.1.28

0.36

-

30°C, pH 5.5, mutant enzyme Y52R/F299G

669152

1.1.1.28

0.7

-

30°C, pH 5.5, mutant enzyme Y52A

669152

1.1.1.28

15.9

-

30°C, pH 5.5, mutant enzyme Y52R

669152

1.1.1.28

21

-

30°C, pH 5.5, wild-type enzyme

669152

1.1.1.28

160

-

pH 7.0, 30°C, recombinant enzyme

739841

1.1.1.28

230

-

pH 7.0, 30°C, recombinant enzyme

739841

1.1.1.337

0.63

-

pH 7.0, 30°C, mutant enzyme del I81

727405

1.1.1.337

6.58

-

pH 7.0, 30°C, mutant enzyme L239M/T245A

728726

1.1.1.337

13

-

pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88

727405

1.1.1.337

20

-

pH 7.0, 30°C, mutant enzyme del I81/delK82

727405

1.1.1.337

27

-

pH 7.0, 30°C, mutant enzyme T245A

728726

1.1.1.337

40

-

pH 7.0, 30°C, mutant enzyme delK82

727405

1.1.1.337

320

-

pH 7.0, 30°C, mutant enzyme L239F

728726

1.1.1.337

620

-

pH 7.0, 30°C, mutant enzyme delP88

727405

1.1.1.337

1000

-

pH 7.0, 30°C, mutant enzyme del L 83

727405

1.1.1.337

2100

-

pH 7.0, 30°C, mutant enzyme F236S

728726

1.1.1.337

2400

-

pH 7.0, 30°C, mutant enzyme L239W

728726

1.1.1.337

4400

-

pH 7.0, 30°C, mutant enzyme delN87

727405

1.1.1.337

5600

-

pH 7.0, 30°C, mutant enzyme L239A

728726

1.1.1.337

6900

-

pH 7.0, 30°C, mutant enzyme F236V

728726

1.1.1.337

7600

-

pH 7.0, 30°C, mutant enzyme G234V/G235D

728726

1.1.1.337

7900

-

pH 7.0, 30°C, mutant enzyme L239M

728726

1.1.1.337

21000

-

pH 7.0, 30°C, mutant enzyme delN87/delP88

727405

1.1.1.337

360000

-

pH 7.0, 30°C, wild-type enzyme

727405, 728726

1.1.1.28

8 entries

1.1.1.337

18 entries

1.1.1.345

139

-

pH 7.0, temperature not specified in the publication

731727

1.2.7.7

0.933

-

pH 6.9, 85°C, under argon

644696

1.2.7.7

1

-

pH 6.9, 85°C, under argon

644696

1.4.1.20

51

-

25°C, pH 10.4

654620

1.4.1.20

79

-

wild-type enzyme

349649

1.2.7.7

2 entries

1.4.1.20

2 entries

1.4.1.23

107

-

pH 9.5, 21°C

391694

1.4.1.8

107

-

-

391694

1.4.1.9

24

-

mutant enzyme A113A/V291L

656569

1.4.1.9

110

-

wild-type enzyme

656569

1.4.1.9

140

-

mutant enzyme A113A

656569

2.6.1.42

0.22

-

pH 8.0, 25°C

758768

2.6.1.42

23.1

-

pH 8.0, 37°C

738209

2.6.1.42

91

-

half transamination reaction, pH 8.0, 90°C

738188

1.4.1.9

3 entries

2.6.1.42

3 entries

2.6.1.5

1.83

-

pH 7.0, 38°C

723682

2.6.1.7

0.41

-

pH 7.5, 38°C

721881

2.6.1.7

2.59

-

in 100 mM boric acid buffer, pH 9.0, at 45°C

705702

2.6.1.7

4.83

-

in 100 mM potassium phosphate buffer (pH 7.4), at 37°C

702779

4.1.1.1

0.8

-

mutant I476F, pH 6.5, 30°C

666806

4.1.1.1

4

-

wild type, pH 6.5, 30°C

666806

4.1.1.1

82

-

mutant I472A/I476F, pH 6.5, 30°C

666806

4.1.1.1

130

-

mutant I472A, pH 6.5, 30°C

666806

4.1.1.43

0.29

-

in 10 mM MES, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate, 0.35 mM NADH, and 0.125 units alcohol dehydrogenase, at pH 6.5 and 30°C

680508

4.1.1.43

0.41

-

mutant enzyme I335Y/M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C

714975

4.1.1.43

0.96

-

mutant enzyme M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C

714975

4.1.1.43

1.3

-

mutant enzyme Q448W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C

714975

4.1.1.43

3.3

-

mutant enzyme I335Y, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C

714975

4.1.1.43

8.8

-

wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C

714975

4.1.1.7

1.1

-

mutant enzyme T377L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C

702341

4.1.1.7

1.2

-

mutant enzyme T377L/A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C

702341

4.1.1.7

4.1

-

wild type enzyme, at pH 6.0 and 30°C

747471

4.1.1.7

4.4

-

mutant enzyme A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C

702341

4.1.1.7

5.3

-

wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C

702341

4.1.1.7

5.9

-

mutant enzyme T377L/A460Y, at pH 6.0 and 30°C

747471

4.1.1.7

20

-

wild type enzyme, at pH 6.0 and 30°C

747171

4.1.1.7

21

-

pH 6.0, 30°C, wild-type enzyme

666806

4.1.1.7

71.8

-

pH 6.0, 30°C, mutant enzyme A460I

666806

2.6.1.7

3 entries

4.1.1.1

4 entries

4.1.1.43

6 entries

4.1.1.7

9 entries

4.1.1.72

7.06

-

-

693210

K_M Value (74 results)

top print hide

Show KM Value (74 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.28

1.18

-

30°C, pH 5.5, mutant enzyme Y52R

669152

1.1.1.28

2.6

-

pH 7.0, 30°C, recombinant enzyme

739841

1.1.1.28

5.8

-

pH 7.0, 30°C, recombinant enzyme

739841

1.1.1.28

13.3

-

30°C, pH 5.5, wild-type enzyme

669152

1.1.1.28

14.1

-

30°C, pH 5.5, mutant enzyme Y52R/F299G

669152

1.1.1.28

51

-

30°C, pH 5.5, mutant enzyme Y52V

669152

1.1.1.28

102

-

30°C, pH 5.5, mutant enzyme Y52A

669152

1.1.1.28

189

-

30°C, pH 5.5, mutant enzyme Y52L

669152

1.1.1.337

0.071

-

pH 7.0, 30°C, mutant enzyme delP88

727405

1.1.1.337

0.1

1

pH 7.0, 30°C, wild-type enzyme

727405

1.1.1.337

0.1

2

pH 7.0, 30°C

726750

1.1.1.337

0.62

-

pH 7.0, 30°C, mutant enzyme delN87/delP88

727405

1.1.1.337

2

-

pH 7.0, 30°C, mutant enzyme delN87

727405

1.1.1.337

5

-

pH 7.0, 30°C, mutant enzyme delK82

727405

1.1.1.337

6.4

-

pH 7.0, 30°C, mutant enzyme del L83

727405

1.1.1.337

18

-

pH 7.0, 30°C, mutant enzyme del I81

727405

1.1.1.337

19

-

pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88

727405

1.1.1.337

62

-

pH 7.0, 30°C, mutant enzyme del I81/delK82

727405

1.1.1.345

0.02

-

pH 7.5, 25°C

731741

1.1.1.345

0.11

-

pH 7.0, 25°C

731190

1.1.1.345

0.13

-

pH 7.0, temperature not specified in the publication

731727

1.1.1.345

0.6

-

pH 7.5, 30°C, D-mandelate dehydrogenase D-ManDH2

729022

1.1.1.345

1.5

-

pH 7.5, 30°C

685675

1.1.1.345

2.4

-

at pH 7.0 and 37°C

712292

1.1.1.345

40

-

in 100 mM Tris-HC1 buffer, pH 8.0, at 30°C

722588

1.2.7.7

0.049

-

pH 6.9, 85°C, under argon

644696

1.2.7.7

0.311

-

pH 6.9, 85°C, under argon

644696

1.1.1.28

8 entries

1.1.1.337

10 entries

1.1.1.345

7 entries

1.2.7.7

2 entries

1.4.1.1

7

-

-

349555

1.4.1.20

2.44

-

-

349634

1.4.1.20

2.5

-

wild-type enzyme

349649

1.4.1.20

13

-

25°C, pH 10.4

654620

1.4.1.20

47

-

mutant enzyme F124M/V125S/H126I/A127I/A128Y/R129Q

349649

1.4.1.23

0.81

-

pH 9.5, 21°C

391694

1.4.1.23

2.23

-

pH 8.8, 30°C

391690

1.4.1.8

0.81

-

-

391694

1.4.1.8

2.23

-

-

391690

1.4.1.9

1.2

-

-

349661

1.4.1.9

1.4

-

-

349685

1.4.1.9

2

-

mutant enzyme A113A

656569

1.4.1.9

2.7

-

-

349664

1.4.1.9

4.7

-

wild-type enzyme

656569

1.4.1.9

6.2

-

-

349680

1.4.1.9

7

-

-

349665

1.4.1.9

28

-

mutant enzyme A113A/V291L

656569

1.4.1.20

4 entries

1.4.1.23

2 entries

1.4.1.8

2 entries

1.4.1.9

8 entries

1.5.1.28

28

-

L-Met and NADH as cosubstrate

94167

2.6.1.28

0.08

-

with tryptophan, pH 8.0, 30°C

639949

2.6.1.42

0.06

-

half transamination reaction, pH 8.0, 90°C

738188

2.6.1.42

0.22

-

pH 8.0, 37°C

738209

2.6.1.42

0.41

-

pH 8.3, 37°C, leucine as amino group donor

640031

2.6.1.42

3 entries

2.6.1.5

7.3

-

pH 7.0, 38°C

723682

2.6.1.64

8.7

-

pH 8.5, 37°C, L-phenylalanine as amino group donor

639901

2.6.1.7

0.5

-

in 100 mM boric acid buffer, pH 9.0, at 45°C

705702

2.6.1.7

1.5

-

in 100 mM potassium phosphate buffer (pH 7.4), at 37°C

702779

2.6.1.7

10.4

-

pH 7.5, 38°C

721881

4.1.1.1

0.2

-

mutant I472A, pH 6.5, 30°C

666806

4.1.1.1

0.5

-

mutant I472A/I476F, pH 6.5, 30°C

666806

4.1.1.1

12.7

-

wild type, pH 6.5, 30°C

666806

4.1.1.43

0.17

-

mutant enzyme M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C

714975

4.1.1.43

0.46

-

mutant enzyme Q448W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C

714975

4.1.1.43

0.55

-

mutant enzyme I335Y, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C

714975

4.1.1.43

0.69

-

wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C

714975

4.1.1.43

1

-

mutant enzyme I335Y/M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C

714975

4.1.1.43

5.51

-

in 10 mM MES, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate, 0.35 mM NADH, and 0.125 units alcohol dehydrogenase, at pH 6.5 and 30°C

680508

4.1.1.7

0.14

-

mutant enzyme T377L/A460Y, at pH 6.0 and 30°C

747471

4.1.1.7

0.15

-

mutant enzyme T377L/A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C

702341

4.1.1.7

0.28

-

mutant enzyme A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C

702341

4.1.1.7

1

-

pH 6.0, 30°C, mutant enzyme A460I

666806

4.1.1.7

1.3

-

mutant enzyme T377L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C

702341

4.1.1.7

4.1

-

wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C

702341

4.1.1.7

4.1

-

pH 6.0, 30°C, wild-type enzyme

666806

4.1.1.7

5.3

-

wild type enzyme, at pH 6.0 and 30°C

747471

4.1.1.7

21

-

wild type enzyme, at pH 6.0 and 30°C

747171

4.1.1.72

0.6

-

in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate

677424

4.1.1.72

0.83

-

-

693210

2.6.1.7

3 entries

4.1.1.1

3 entries

4.1.1.43

6 entries

4.1.1.7

9 entries

4.1.1.72

2 entries

K_i Value (2 results)

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Show KI Value (2 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

4.1.1.7

2

5

pH 6.0, 30°C, wild-type enzyme

666806

4.1.1.7

10

-

pH 6.0, 30°C, mutant enzyme A460I

666806

4.1.1.7

2 entries

References & Links

Literature References (108)

top print hide

Show Reference (108 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

4562

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Metabolism of phenylalanine. (Achromobacter eurydice)

1970

Fujioka, M.; Morino, Y.; Wada, H.

Methods Enzymol.

17

585-596

4563

4303395

Enzymatic conversion of phenylpyruvate to phenylacetate

1968

Asakawa, T.; Wada, H.; Yamano, T.

Biochim. Biophys. Acta

170

375-391

4748

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L-Alanine-alpha-ketobutyrate aminotransferase of Pseudomonas sp.

1981

Koide, Y.; Honma, M.; Shimomura, T.

Agric. Biol. Chem.

45

775-776

4751

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Purification and properties of an alpha-dialkyl amino acid transaminase

1967

Bailey, G.B.; Dempsey, W.B.

Biochemistry

6

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13440

8840516

Tauropine dehydrogenase from the sandworm Arabella iricolor (polychaeta: errantia): purification and characterization

1996

Kanno, N.; Sato, M.; Nagahisa, E.; Sato, Y.

Comp. Biochem. Physiol. B

114

409-416

94167

2753861

A new NAD+-dependent opine dehydrogenase from Arthrobacter sp. strain 1C

1989

Asano, Y.; Yamaguchi, K.; Kondo, K.

J. Bacteriol.

171

4466-4471

286247

14275148

Isolation and properties of lens aldose reductase

1965

Hayman, S.; Kinoshita, J.H.

J. Biol. Chem.

240

877-882

287840

236454

D-2-hydroxy acid dehydrogenase from animal tissue

1975

Cammack, R.

Methods Enzymol.

41

323-329

288059

13712439

Enzymatic studies on the metabolism of beta-alanine

1961

Hayaishi, O.; Nishizuka, Y.; Tatibana, M.; Takeshita, M.; Kuno, S.

J. Biol. Chem.

236

781-790

348956

7005225

Substrate specificity of the pyruvate dehydrogenase complex from Escherichia coli

1981

Bisswanger, H.

J. Biol. Chem.

256

815-822

349056

2853818

Branched-chain alpha-keto acid dehydrogenase and its kinase from rabbit liver and heart

1988

Paxton, R.

Methods Enzymol.

166

313-320

349539

-

Synthesis of L-alanine and L-valine by enzyme systems from Bacillus megaterium

1990

Honorat, A.; Monot, F.; Ballerini, D.

Enzyme Microb. Technol.

12

515-520

349555

14298830

Enzymic properties of Alanine dehydrogenase of Bacillus subtilis

1965

Yoshida, A.; Freese, E.

Biochim. Biophys. Acta

96

248-262

349634

3112142

Novel phenylalanine dehydrogenases from Sporosarcina ureae and Bacillus sphaericus. Purification and characterization

1987

Asano, Y.; Nakazawa, A.; Endo, K.

J. Biol. Chem.

262

10346-10354

349635

-

Purification, characterization and regulation of a monomeric L-phenylalanine dehydrogenase from the facultative methylotroph Nocardia sp. 239

1989

De Boer, L.; Van Rijssel, M.; Euverink, G.J.; Dijkhuizen, L.

Arch. Microbiol.

153

12-18

349638

3311741

Phenylalanine dehydrogenase of Bacillus badius. Purification, characterization and gene cloning [published erratum appears in Eur J Biochem 1988 Jan 1;170(3):667]

1987

Asano, Y.; Nakazawa, A.; Endo, K.; Hibino, Y.; Ohmori, M.; Numao, N.; Kondo, K.

Eur. J. Biochem.

168

153-159

349647

7883771

Construction and characterization of chimeric enzyme consisting of an amino-terminal domain of phenylalanine dehydrogenase and a carboxy-terminal domain of leucine dehydrogenase

1994

Kataoka, K.; Takada, H.; Tanizawa, K.; Yoshimura, T.; Esaki, N.; Ohshima, T.; Soda, K.

J. Biochem.

116

931-936

349649

8407879

Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine dehydrogenase from Thermoactinomyces intermedius

1993

Kataoka, K.; Takada, H.; Yoshimura, T.; Furuyoshi, S.; Esaki, N.; Ohshima, T.; Soda, K.

J. Biochem.

114

69-75

349661

-

L-Leucine dehydrogenase from Bacillus cereus

1985

Schuette, H.; Hummel, W.; Tsai, H.; Kula, M.R.

Appl. Microbiol. Biotechnol.

22

306-317

349664

-

Purification and characterization of leucine dehydrogenase from the thermophile Bacillus caldolyticus

1989

Kaerst, U.; Schuette, H.; Baydoun, H.; Tsai, H.

J. Gen. Microbiol.

135

1305-1313

349665

670223

Properties of crystalline leucine dehydrogenase from Bacillus sphaericus

1978

Ohshima, T.; Misono, H.; Soda, K.

J. Biol. Chem.

253

5719-5725

349680

-

Leucine dehydrogenase of a thermophilic anaerobe, Clostridium thermoaceticum: gene cloning, purification and characterization

1987

Shimoi, H.; Nagata, S.; Esaki, N.; Tanaka, H.; Soda, K.

Agric. Biol. Chem.

51

3375-3381

349682

8597545

Gene cloning, purification, and characterization of thermostable and halophilic leucine dehydrogenase from a halophilic thermophile, Bacillus licheniformis TSN9

1995

Nagata, S.; Bakthavatsalam, S.; Galkin, A.G.; Asada, H.; Sakai, S.; Esaki, N.; Soda, K.; Ohshima, T.; Nagasaki, S.; Misono, H.

Appl. Microbiol. Biotechnol.

44

432-438

349685

8020469

The purification, characterization, cloning and sequencing of the gene for a halostable and thermostable leucine dehydrogenase from Thermoactinomyces intermedius

1994

Ohshima, T.; Nishida, N.; Bakthavatsalam, S.; Kataoka, K.; Takada, H.; Yoshimura, T.; Esaki, N.; Soda, K.

Eur. J. Biochem.

222

305-312

389685

3061453

Rat kidney L-2-hydroxyacid oxidase. Structural and mechanistic comparison with flavocytochrome b2 from bakerÆs yeast

1988

Urban, P.; Chirat, I.; Lederer, F.

Biochemistry

27

7365-7371

389691

1148170

Rat kidney L-alpha-hydroxy acid oxidase: Isolation of enzyme with one flavine coenzyme per two subunits

1975

Cromartie, T.H.; Walsh, C.T.

Biochemistry

14

2588-2596

389693

4750770

Molecular forms of L-alpha-hydroxy acid oxidase from rat kidney

1973

Domenech, S.E.; Machado De Domenech, E.E.; Blanco, A.

Biochim. Biophys. Acta

321

54-63

389698

5686300

Aliphatic L-alpha-hydroxyacid oxidase from rat livers. Purification and properties

1968

Nakano, M.; Ushijima, Y.; Saga, M.; Tsutsumi, Y.; Asami, H.

Biochim. Biophys. Acta

167

9-22

389699

5972358

Oxidation of L-alpha-hydroxy acids by Tetrahymena pyriformis

1966

Eichel, H.J.

Biochim. Biophys. Acta

128

183-186

389700

5946631

Crystalline mammalian L-amino acid oxidase from rat kidney mitochondria

1966

Nakano, M.; Danowski, T.S.

J. Biol. Chem.

241

2075-2083

389701

14492912

L-alpha-Hydroxy acid oxidases of hog renal cortex

1962

Robinson, J.C.; Keay, L.; Molinari, R.; Sizer, I.W.

J. Biol. Chem.

237

2001-2010

391690

3269392

Valine dehydrogenase from Streptomyces fradiae: purification and properties

1988

Vancura, A.; Vancurova, I.; Volc, J.; Fussey, S.P.M.; Flieger, M.; Neuzil, J.; Marsalek, J.; Behal, V.

J. Gen. Microbiol.

134

3213-3219

391694

2803248

Purification and catalytic properties of L-valine dehydrogenase from Streptomyces cinnamonensis

1989

Priestley, N.D.; Robinson, J.A.

Biochem. J.

261

853-861

394974

-

D-Amino acid dehydrogenase (Pseudomonas fluorescens)

1971

Tsukada, K.

Methods Enzymol.

17B

623-624

440368

11352583

Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS)

2001

Lee, H.J.; Lloyd, M.D.; Harlos, K.; Clifton, I.J.; Baldwin, J.E.; Schofield, C.J.

J. Mol. Biol.

308

937-948

440371

12631288

The kinetic properties of various R258 mutants of deacetoxycephalosporin C synthase

2003

Lee, H.J.; Dai, Y.F.; Shiau, C.Y.; Schofield, C.J.; Lloyd, M.D.

Eur. J. Biochem.

270

1301-1307

636592

13084587

Transaminase in smooth Brucella abortus, strain 19

1953

Altenbern, R.A.; Housewright, R.D.

J. Biol. Chem.

204

159-167

636593

-

L-alanine-alpha-keto acid aminotransferase of Pseudomonas sp.

1977

Koide, Y.; Honma, M.; Shimomura, T.

Agric. Biol. Chem.

41

781-784

636608

3037259

Kynurenine-oxoglutarate aminotransferase from rat kidney

1987

Tobes, M.C.

Methods Enzymol.

142

217-224

636613

3086302

Purification and characterization of yeast L-kynurenine aminotransferase with broad substrate specificity

1986

Asada, Y.; Sawa, Y.; Tanizawa, K.; Soda, K.

J. Biochem.

99

1101-1110

637018

-

L-Lysine-ketoglutarate aminotransferase (Acetobacter liquidum)

1971

Soda, K.; Misono, H.

Methods Enzymol.

17B

222-228

637098

14284729

Purification and properties of rat liver ornithine DELTA-transaminase

1965

Strecker, H.J.

J. Biol. Chem.

240

1225-1230

639901

4822504

Isolation and properties of a new glutamine transaminase form rat kidney

1974

Cooper, A.J.L.; Meister, A.

J. Biol. Chem.

249

2554-2561

639949

-

L-tryptophan-alpha-ketoisocaproate aminotransferase from Pseudomonas sp.

1980

Koide, Y.; Honma, M.; Shimomura, T.

Agric. Biol. Chem.

44

2013-2019

639973

-

Purification and characterization of L-histidine aminotransferase from nikkomycin-producing Streptomyces tendae Tu901

1993

Roos, U.; Bormann, C.

J. Gen. Microbiol.

139

2773-2778

639992

13034817

Transamination in Escherichia coli

1953

Rudman, D.; Meister, A.

J. Biol. Chem.

200

591-604

639993

5943594

Transaminase of branched chain amino acids. I. Branched chain amino acids-alpha-ketoglutarate transaminase

1966

Ichihara, A.; Koyama, E.

J. Biochem.

59

160-169

639995

5922965

Leucine aminotransferase. II. Purification and characterization

1966

Taylor, R.T.; Jenkins, W.T.

J. Biol. Chem.

241

4396-4405

639997

4979711

Transaminase of branched chain amino acids. VI. Purification and properties of the hog brain enzyme

1969

Aki, K.; Yokojima, A.; Ichihara, A.

J. Biochem.

65

539-544

640019

8381418

Branched chain aminotransferase isoenzymes. Purification and characterization of the rat brain isoenzyme

1993

Hall, T.R.; Wallin, R.; Reinhart, G.D.; Hutson, S.M.

J. Biol. Chem.

268

3092-3098

640021

24178815

Human branched-chain L-amino acid aminotransferase: activity and subcellular localization in cultured skin fibroblasts

1995

Schadewaldt, P.; Wendel, U.; Hammen, H.W.

Amino Acids

9

147-160

640031

10989414

Determination of branched-chain L-amino-acid aminotransferase activity

2000

Schadewaldt, P.

Methods Enzymol.

324

23-32

640128

2729940

Reactions catalyzed by purified L-glutamine:keto-scyllo-inositol aminotransferase, an enzyme required for biosynthesis of aminocyclitol antibiotics

1989

Lucher, L.A.; Chen, Y.M.; Walker, J.B.

Antimicrob. Agents Chemother.

33

452-459

640176

3709533

The transamination of L-cystathionine, L-cystine and related compounds by a bovine kidney transaminase

1986

Ricci, G.; Nardini, M.; Federici, G.; Cavallini, D.

Eur. J. Biochem.

157

57-63

640188

3622507

Candida L-norleucine,leucine:2-oxoglutarate aminotransferase. Purification and properties

1987

Der Garabedian, P.A.; Vermeersch, J.J.

Eur. J. Biochem.

167

141-147

640579

6721501

Regulation of branched-chain alpha-ketoacid dehydrogenase kinase

1984

Paxton, R.; Harris, R.A.

Arch. Biochem. Biophys.

231

48-57

644696

8550513

Characterization of 2-ketoisovalerate ferredoxin oxidoreductase, a new and reversible coenzyme A-dependent enzyme involved in peptide fermentation by hyperthermophilic archaea

1996

Heider, J.; Mai, X.; Adams, M.W.

J. Bacteriol.

178

780-787

651026

-

A new bacterial L-amino acid oxidase with a broad substrate specificity: purification and characterization

2002

Geueke, B.; Hummel, W.

Enzyme Microb. Technol.

31

77-87

654620

12234181

Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its discrimination between phenylalanine and tyrosine substrates

2002

Seah, S.Y.; Britton, K.L.; Rice, D.W.; Asano, Y.; Engel, P.C.

Biochemistry

41

11390-11397

655887

15516582

A novel archaeal alanine dehydrogenase homologous to ornithine cyclodeaminase and mu-crystallin

2004

Schröder, I.; Vadas, A.; Johnson, E.; Lim, S.; Monbouquette, H.G.

J. Bacteriol.

186

7680-7689

656565

-

Purification and characterization of leucine dehydrogenase from an alkalophilic halophile, Natronobacterium magadii MS-3

2003

Katoh, R.; Ngata, S.; Ozawa, A.; Ohshima, T.; Kamekura, M.; Misono, H.

J. Mol. Catal. B

23

231-238

656569

-

Alteration of substrate specificity of leucine dehydrogenase by site-directed mutagenesis

2003

Kataoka, K.; Tanizawa, K.

J. Mol. Catal. B

23

299-309

656887

15351834

Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis

2004

Busca, P.; Paradisi, F.; Moynihan, E.; Maguire, A.R.; Engel, P.C.

Org. Biomol. Chem.

2

2684-2691

661957

14962140

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Links to other databases for 2-oxohexanoic acid

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