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Ligand L-threonine

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

aminopropanol phosphate biosynthesis, threonine metabolism

KEGG

ABC transporters, Aminoacyl-tRNA biosynthesis, Biosynthesis of amino acids, Biosynthesis of plant secondary metabolites, Biosynthesis of secondary metabolites, D-Amino acid metabolism, Glycine, serine and threonine metabolism, Microbial metabolism in diverse environments, Mineral absorption, Monobactam biosynthesis, Porphyrin metabolism, Protein digestion and absorption, Valine, leucine and isoleucine biosynthesis more

MetaCyc

acinetobactin biosynthesis, actinomycin D biosynthesis, aminopropanol phosphate biosynthesis I, aminopropanol phosphate biosynthesis II, antimycin biosynthesis, bacillibactin biosynthesis, coenzyme B biosynthesis, echinocandin B biosynthesis, fluoroacetate and fluorothreonine biosynthesis, glycine biosynthesis IV, hypoglycin biosynthesis, L-isoleucine biosynthesis I (from threonine), L-threonine biosynthesis, L-threonine degradation I, L-threonine degradation II, L-threonine degradation III (to methylglyoxal), L-threonine degradation IV, L-threonine degradation V, mycobactin biosynthesis, N6-L-threonylcarbamoyladenosine37-modified tRNA biosynthesis, polymyxin A biosynthesis, protein N-glycosylation (Methanococcus voltae), pseudomonine biosynthesis, pyoverdine I biosynthesis, tabtoxinine-beta-lactam biosynthesis, tRNA charging, vibriobactin biosynthesis more

Show all BRENDA pathways known for L-threonine

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (21 results)

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Show Natural Substrate (21 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.103

L-threonine + NAD+ = (2S)-2-amino-3-oxobutanoate + NADH + H+

285701, 285717, 285720, 737579, 285707, 285708, 285705, 285713, 668567, 285721, 285719, 738606, 285715, 668536, 669546, 285703, 285704, 285706, 285709, 285710, 285711, 285712, 285714, 285716, 285718, 285702, 722747, 738933, 687461, 688343, 721272, 729112, 668111

-

1.1.1.103

L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+

762647, 762551, 762728

-

1.1.1.103

2 entries

1.4.1.1

L-threonine + H2O + NAD+ = 3-hydroxy-2-oxobutyrate + NH3 + NADH + H+

724147

-

2.2.1.8

L-threonine + fluoroacetaldehyde = 4-fluoro-L-threonine + acetaldehyde

703173

-

2.2.1.8

L-threonine + fluoroacetaldehyde = acetaldehyde + 4-fluoro-L-threonine

755884, 636461, 639494

-

2.2.1.8

2 entries

2.7.1.177

ATP + L-threonine = ADP + O-phospho-L-threonine

717877, 717878, 760602, 761921

-

2.7.7.87

L-threonine + ATP + bicarbonate = L-threonylcarbamoyladenylate + diphosphate + H2O

723758, 723287, 726476

-

2.7.7.87

L-threonine + ATP + CO2 = L-threonylcarbamoyl-AMP + diphosphate

721678

-

2.7.7.87

2 entries

4.1.2.48

L-Thr = glycine + acetaldehyde

702834

-

4.2.1.122

L-threonine + indole = (2S,3S)-beta-methyltryptophan + H2O

748036, 747116

-

4.3.1.17

L-threonine = alpha-ketobutyrate + NH3

680934, 680935

-

4.3.1.19

L-Thr = ?

210838, 210831, 210819, 210857, 210855, 210865, 210818, 210825, 210837

-

4.3.1.19

L-threonine = 2-oxobutanoate + NH3

677340, 680728, 649402, 653575, 650401, 654175, 649943, 650119, 676427, 662025, 682322, 682413, 747392, 692849, 692908, 690910, 747616, 747154

-

4.3.1.19

2 entries

5.1.1.18

L-threonine = D-threonine

680516

-

6.1.1.3

ATP + L-threonine + tRNA1Thr = AMP + diphosphate + L-threonyl-tRNA1Thr

728681

-

6.1.1.3

ATP + L-threonine + tRNA2Thr = AMP + diphosphate + L-threonyl-tRNA2Thr

728681

-

6.1.1.3

ATP + L-threonine + tRNAThr = ?

398

-

6.1.1.3

ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr

650200, 650778, 650784, 653273, 714230, 715520, 716771, 728097, 716387, 727916, 728681, 743906, 705818, 654016, 728410, 745113, 662443, 663379, 726613, 728382, 660587, 745349, 705167, 663210, 652919, 673326, 704188, 653312, 728193, 744225, 745397, 745920, 662829, 663398, 744595, 744913, 653324, 652046, 674339

-

6.1.1.3

ATP + L-threonine + tRNAThr1 = AMP + diphosphate + L-threonyl-tRNAThr1

745918

-

6.1.1.3

ATP + L-threonine + tRNAThr2 = AMP + diphosphate + L-threonyl-tRNAThr2

745918

-

6.1.1.3

6 entries

6.3.2.B23

ATP + 3-formyl-L-tyrosine + L-threonine = 3-formyl-L-tyrosyl-L-threonine + ADP + phosphate

731979

-

In Vivo Product in Enzyme-catalyzed Reactions (4 results)

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Show Natural Product (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.3.16

phospho-L-threonine + H2O = L-threonine + phosphate

0

-

3.4.11.1

Thr-Leu + H2O = Thr + Leu

643878

-

3.4.11.23

Thr-Leu + H2O = Thr + Leu

643878

-

4.2.3.1

O-phospho-L-homoserine + H2O = L-threonine + phosphate

0, 651164, 652228, 653789

-

Substrate in Enzyme-catalyzed Reactions (124 results)

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Show Substrate (124 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.103

L-threonine + 3-acetyl-pyridine adenine dinucleotide = L-2-amino-3-oxobutanoate + ?

655857

-

1.1.1.103

L-threonine + 3-pyridinealdehyde adenine dinucleotide = L-2-amino-3-oxobutanoate + ?

655857

-

1.1.1.103

L-threonine + NAD+ = (2S)-2-amino-3-oxobutanoate + NADH + H+

285701, 285717, 285720, 737579, 285707, 285708, 285705, 285713, 668111, 668567, 285721, 285719, 738606, 285715, 668536, 669546, 285703, 285704, 285706, 285709, 285710, 285711, 285712, 285714, 285716, 285718, 285702, 722747, 738933, 655857, 687461, 688343, 698673, 695358, 699854, 698526, 721272, 729112, 738860

-

1.1.1.103

L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+

762647, 762551, 762728

-

1.1.1.103

L-threonine + nicotinamide guanine dinucleotide = L-2-amino-3-oxobutanoate + ?

655857

-

1.1.1.103

L-threonine + thionicotinamide-NAD+ = L-2-amino-3-oxobutanoate + ?

655857

-

1.1.1.103

6 entries

1.1.1.30

L-threonine + NAD+ = ?

669873

-

1.4.1.1

L-Thr + H2O + NAD+ = 3-hydroxy-2-oxobutyrate + NH3 + NADH

655887

-

1.4.1.1

L-threonine + H2O + NAD+ = 3-hydroxy-2-oxobutyrate + NH3 + NADH + H+

724147

-

1.4.1.1

2 entries

1.4.1.5

L-threonine + H2O + NAD+ = 3-hydroxy-2-oxopropanoate + NH3 + NADH

704871

-

1.4.3.2

L-threonine + H2O + O2 = 2-oxo-3-hydroxybutanoic acid + NH3 + H2O2

692650, 391770

-

1.4.3.2

L-threonine + H2O + O2 = 3-hydroxy-2-oxobutanoate + NH3 + H2O2

724190

-

1.4.3.2

2 entries

1.5.1.17

L-Thr + pyruvate + NADH = ?

13373, 13365

-

1.5.1.22

L-Thr + pyruvate + NADH = ?

711788, 13369, 13373

-

1.5.1.28

L-Thr + pyruvate + NADH = N-[1-(R)-(Carboxy)ethyl]-(S)-Thr + NAD+

94167

-

1.5.99.B2

L-threonine + 2,6-dichlorophenolindophenol + H2O = ? + reduced 2,6-dichlorophenolindophenol

723984

-

1.5.99.B2

L-threonine + 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium + H2O = ?

725126

-

2.2.1.8

fluoroacetaldehyde + L-threonine = acetaldehyde + 4-fluoro-L-threonine

719042

-

2.2.1.8

L-threonine + chloroacetaldehyde = acetaldehyde + 4-chloro-L-threonine

636461, 755884

-

2.2.1.8

L-threonine + fluoroacetaldehyde = 4-fluoro-L-threonine + acetaldehyde

703173

-

2.2.1.8

L-threonine + fluoroacetaldehyde = acetaldehyde + 4-fluoro-L-threonine

755884, 636461, 639494

-

2.2.1.8

L-threonine + glycolaldehyde = acetaldehyde + 4-hydroxyl-L-threonine

755884

-

2.2.1.8

L-threonine + isobutyraldehyde = acetaldehyde + 4-isobutyl-L-threonine

755884

-

2.2.1.8

L-threonine + phenylacetaldehyde = acetaldehyde + 4-phenyl-L-threonine

755884

-

2.2.1.8

L-threonine + propanal = acetaldehyde + 4-methyl-L-threonine

755884

-

1.5.99.B2

2 entries

2.2.1.8

8 entries

2.3.1.30

acetyl-CoA + L-threonine = CoA + O-acetyl-L-threonine

657835, 486753, 486752

-

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-Thr = 4-nitroaniline + 5-L-glutamyl-L-Thr

658567

-

2.3.2.2

5-L-glutamyl-4-nitroanilide + L-threonine = 4-nitroaniline + 5-L-glutamyl-L-threonine

487947, 487951, 487920

-

2.3.2.2

L-gamma-glutamyl-4-nitroanilide + L-threonine = 4-nitroaniline + 5-L-glutamyl-L-threonine

757413, 756967

-

2.3.2.2

5-L-glutamyl-4-nitroanilide + Thr = 4-nitroaniline + 5-L-glutamyl-Thr

676991, 675471

-

2.3.2.2

4 entries

2.6.1.12

pyruvate + L-threonine = L-alanine + 3-hydroxy-2-oxobutanoate

636593

-

2.6.1.42

L-threonine + 2-oxobutyrate = 2-oxo-3-hydroxybutyrate + 2-aminobutyrate

758697

-

2.6.1.42

L-threonine + 2-oxoglutarate = 2-oxo-3-hydroxybutyrate + L-glutamate

640004, 758768

-

2.6.1.42

L-threonine + 4-methyl-2-oxovalerate = 2-oxo-3-hydroxybutyrate + L-leucine

758768, 759134

-

2.6.1.42

3 entries

2.6.1.51

threonine + phenylpyruvate = 3-hydroxy-2-oxobutanoate + L-phenylalanine

640135

-

2.6.1.64

L-threonine + pyruvate = 3-hydroxy-2-oxobutanoate + L-alanine

662056

-

2.7.1.177

ATP + L-threonine = ADP + O-phospho-L-threonine

717877, 717878, 760602, 761921

-

2.7.1.80

diphosphate + L-threonine = phosphate + O-phospho-L-threonine

642033

-

2.7.7.87

L-threonine + ATP + bicarbonate = L-threonylcarbamoyladenylate + diphosphate + H2O

723758, 723287, 723740, 726476, 725467, 726075, 726076

-

2.7.7.87

L-threonine + ATP + CO2 = L-threonylcarbamoyl-AMP + diphosphate

721678

-

2.7.7.87

2 entries

4.1.2.26

L-Thr = glycine + acetaldehyde

663708

-

4.1.2.48

L-Thr = glycine + acetaldehyde

681356, 702834

-

4.1.2.48

L-threonine = glycine + acetaldehyde

727485, 716291, 747174, 5198, 654020, 5205, 747734, 748403, 5206, 441433, 718557, 728820

-

4.1.2.48

2 entries

4.1.2.49

L-threonine = glycine + acetaldehyde

746614

-

4.1.2.5

L-threonine = glycine + acetaldehyde

5200, 5203, 715411, 748265, 713884, 5191, 5199

-

4.1.99.2

Thr + ? = 2-oxobutanoate + ?

33450

-

4.2.1.122

L-threonine + 2-methylindole = (2S,3S)-2-methyl-beta-methyltryptophan + H2O

747549

-

4.2.1.122

L-threonine + 4-fluoroindole = (2S,3S)-4-fluoro-beta-methyltryptophan + H2O

747549

-

4.2.1.122

L-threonine + 4-methylindole = (2S,3S)-4-methyl-beta-methyltryptophan + H2O

747549

-

4.2.1.122

L-threonine + 5-bromoindole = (2S,3S)-5-bromo-beta-methyltryptophan + H2O

747549

-

4.2.1.122

L-threonine + 5-chloroindole = (2S,3S)-5-chloro-beta-methyltryptophan + H2O

747549

-

4.2.1.122

L-threonine + 5-phenylindole = (2S,3S)-5-phenyl-beta-methyltryptophan + H2O

747549

-

4.2.1.122

L-threonine + 6-methylindole = (2S,3S)-6-methyl-beta-methyltryptophan + H2O

747549

-

4.2.1.122

L-threonine + 7-azaindole = (2S,3S)-2-amino-3-(1H-pyrrolo[2,3-b]pyridin-3-yl)butanoic acid + H2O

748036

-

4.2.1.122

L-threonine + 7-chloroindole = (2S,3S)-7-chloro-beta-methyltryptophan + H2O

747549

-

4.2.1.122

L-threonine + 7-fluoroindole = (2S,3S)-7-fluoro-beta-methyltryptophan + H2O

747549

-

4.2.1.122

L-threonine + 7-methoxyindole = (2S,3S)-7-methoxy-beta-methyltryptophan + H2O

747549

-

4.2.1.122

L-threonine + 7-methylindole = (2S,3S)-7-methyl-beta-methyltryptophan + H2O

747549

-

4.2.1.122

L-threonine + indole = (2S,3S)-beta-methyltryptophan + H2O

747549, 747116, 748036

-

4.2.1.20

L-threonine + 1-C-(indol-3-yl)glycerol 3-phosphate = (2S,3S)-beta-methyltryptophan + D-glyceraldehyde 3-phosphate + H2O

747116

-

4.2.1.20

L-threonine + 2-methylindole = 2-methyl-(2S,3S)-beta-methyltryptophan + H2O

747549, 748036

-

4.2.1.20

L-threonine + 4-fluoroindole = 4-fluoro-(2S,3S)-beta-methyltryptophan + H2O

747549, 748036

-

4.2.1.20

L-threonine + 4-methylindole = 4-methyl-(2S,3S)-beta-methyltryptophan + H2O

747549

-

4.2.1.20

L-threonine + 5-fluoroindole = 5-fluoro-(2S,3S)-beta-methyltryptophan + H2O

748036

-

4.2.1.20

L-threonine + 6-methylindole = 6-methyl-(2S,3S)-beta-methyltryptophan + H2O

747549, 748036

-

4.2.1.20

L-threonine + 7-azaindole = 7-aza-(2S,3S)-beta-methyltryptophan + H2O

748036

-

4.2.1.20

L-threonine + 7-chloroindole = 7-chloro-(2S,3S)-beta-methyltryptophan + H2O

747549

-

4.2.1.20

L-threonine + 7-fluoroindole = 7-fluoro-(2S,3S)-beta-methyltryptophan + H2O

747549

-

4.2.1.20

L-threonine + 7-methoxyindole = 7-methoxy-(2S,3S)-beta-methyltryptophan + H2O

747549

-

4.2.1.20

L-threonine + 7-methylindole = 7-methyl-(2S,3S)-beta-methyltryptophan + H2O

747549

-

4.2.1.20

L-threonine + indole = (2S,3S)-beta-methyltryptophan + H2O

747549, 748036

-

4.2.1.122

13 entries

4.2.1.20

12 entries

4.2.3.1

threonine = 2-oxobutyrate + NH3

137546, 137560, 137545

-

4.3.1.17

L-Thr = 2-oxobutanoate + NH3

210785, 210788, 713970

-

4.3.1.17

L-threonine = 2-oxo-butanoate + NH3

210800

-

4.3.1.17

L-threonine = 2-oxobutanoate + NH3

741824

-

4.3.1.17

L-threonine = 2-oxobutyrate + NH3

665219, 661171, 705606, 662359, 665546

-

4.3.1.17

L-threonine = alpha-ketobutyrate + NH3

680934, 680935, 678411

-

4.3.1.17

5 entries

4.3.1.18

L-Thr = ?

210802

-

4.3.1.19

L-Thr = 2-oxobutanoate + NH3

705606

-

4.3.1.19

L-Thr = ?

210838, 210831, 210819, 210857, 210855, 210865, 210818, 210825, 210837

-

4.3.1.19

L-threonine = 2-oxobutanoate + NH3

210823, 210837, 210851, 677340, 680728, 730759, 690910, 210820, 210832, 210833, 210835, 210836, 210840, 210841, 210842, 210847, 210856, 210857, 210858, 210862, 210863, 649402, 653575, 210825, 210849, 210850, 210852, 210859, 210861, 650401, 654175, 210822, 210834, 210844, 210838, 210829, 649943, 650119, 676427, 210828, 210839, 210826, 210860, 210831, 210853, 246394, 210855, 210845, 692908, 662025, 210824, 210830, 210843, 210846, 210821, 210792, 210818, 210819, 210827, 682322, 692849, 682413, 747392, 747616, 747154

-

5.1.1.10

L-Thr = L-Thr

2049, 2047

-

5.1.1.10

L-threonine = 2-oxobutyrate + NH3

662359

-

5.1.1.10

L-threonine = D-threonine

745414, 747857

-

5.1.1.18

L-threonine = 2-oxobutanoate + NH3

662359

-

5.1.1.18

L-threonine = ?

714348

-

5.1.1.18

L-threonine = D-threonine

680516

-

4.3.1.19

3 entries

5.1.1.10

3 entries

5.1.1.18

3 entries

5.1.1.6

L-Thr = D-Thr

2134, 2047

-

6.1.1.11

ATP + L-threonine + tRNASer = AMP + diphosphate + L-threonyl-tRNASer

726813

-

6.1.1.3

2-Chloroadenosine 5'-triphosphate + L-threonine + tRNAThr = ?

411, 273

-

6.1.1.3

ATP + L-threonine + tRNA1Thr = AMP + diphosphate + L-threonyl-tRNA1Thr

728681

-

6.1.1.3

ATP + L-threonine + tRNA2Thr = AMP + diphosphate + L-threonyl-tRNA2Thr

728681

-

6.1.1.3

ATP + L-threonine + tRNAThr = ?

398

-

6.1.1.3

ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr

413, 652046, 395, 409, 397, 398, 401, 406, 407, 650200, 650778, 650784, 653273, 714230, 715520, 716771, 728097, 400, 169, 396, 403, 404, 405, 411, 273, 399, 402, 414, 716387, 727916, 728681, 743906, 92, 415, 705818, 654016, 728410, 745113, 662443, 663379, 726613, 728382, 660587, 745349, 705167, 663210, 652919, 673326, 704188, 653312, 653324, 728193, 744225, 745397, 745920, 662829, 663398, 744595, 744913, 674339, 728383

-

6.1.1.3

ATP + L-threonine + tRNAThr1 = AMP + diphosphate + L-threonyl-tRNAThr1

745918

-

6.1.1.3

ATP + L-threonine + tRNAThr2 = AMP + diphosphate + L-threonyl-tRNAThr2

745918

-

6.1.1.3

Formycin 5'-triphosphate + L-threonine + tRNAThr = ?

411, 273

-

6.1.1.3

8 entries

6.1.1.6

ATP + L-threonine + tRNALys = AMP + L-threonyl-tRNALys + diphosphate

649906

-

6.1.1.9

ATP + L-threonine + tRNAVal = ?

653390

-

6.1.1.9

ATP + L-threonine + tRNAVal = AMP + diphosphate + L-threonyl-tRNAVal

531, 650122

-

6.2.1.70

ATP + L-threonine + holo-[L-threonyl-carrier protein] = AMP + diphosphate + L-threonyl-[L-threonyl-carrier protein]

753966, 747063, 749157

-

6.2.1.70

ATP + L-threonine = diphosphate + (L-threonyl)adenylate

749157

-

6.3.2.2

ATP + L-Glu + L-Thr = ADP + phosphate + gamma-L-Glu-L-Thr

1122, 1133

-

6.3.2.2

ATP + L-Glu + L-threonine = ADP + phosphate + gamma-L-Glu-L-threonine

652341, 649263

-

6.3.2.49

ATP + cis-4-hydroxy-L-proline + L-threonine = ADP + phosphate + cis-4-hydroxy-L-prolyl-L-threonine

726743

-

6.3.2.49

ATP + L-asparagine + L-threonine = ADP + phosphate + L-asparaginyl-L-threonine

726743

-

6.3.2.49

ATP + L-azetidine-2-carboxylate + L-threonine = ADP + phosphate + L-azetidine-2-carboxyl-L-threonine

726743

-

6.3.2.49

ATP + L-glutamine + L-threonine = ADP + phosphate + L-glutaminyl-L-threonine

726743

-

6.3.2.49

ATP + L-phenylalanine + L-threonine = ADP + phosphate + L-phenylalanyl-L-threonine

726743

-

6.3.2.49

ATP + L-pipecolic acid + L-threonine = ADP + phosphate + L-pipecoloyl-L-threonine

726743

-

6.3.2.49

ATP + L-proline + L-threonine = ADP + phosphate + L-prolyl-L-threonine

726743

-

6.3.2.49

ATP + L-threonine + beta-alanine = ADP + phosphate + beta-alanyl-L-threonine

726743

-

6.3.2.49

ATP + L-threonine + L-methionine = ADP + phosphate + L-threonyl-L-methionine

693286

-

6.3.2.49

ATP + L-tryptophan + L-threonine = ADP + phosphate + L-tryptophyl-L-threonine

726743

-

6.3.2.49

ATP + L-tyrosine + L-threonine = ADP + phosphate + L-tyrosyl-L-threonine

726743

-

6.3.2.49

ATP + trans-4-hydroxy-L-proline + L-threonine = ADP + phosphate + trans-4-hydroxy-L-prolyl-L-threonine

726743

-

6.3.2.49

ATP + cysteine + threonine = ADP + phosphate + L-cysteinyl-L-threonine

702771

-

6.3.2.49

ATP + leucine + threonine = ADP + phosphate + L-leucyl-L-threonine

702771

-

6.3.2.49

ATP + methionine + threonine = ADP + phosphate + L-methionyl-L-threonine

702771

-

6.3.2.49

ATP + phenylalanine + threonine = ADP + phosphate + L-phenylalanyl-L-threonine

702771

-

6.3.2.49

ATP + tryptophan + threonine = ADP + phosphate + L-tryptophanyl-L-threonine

702771

-

6.1.1.9

2 entries

6.2.1.70

2 entries

6.3.2.2

2 entries

6.3.2.49

17 entries

6.3.2.8

ATP + UDP-N-acetylmuramate + L-Thr = ADP + phosphate + UDP-N-acetylmuramoyl-L-Thr

1290

-

6.3.2.B16

2 ATP + 2 L-Val + L-Thr = 2 ADP + 2 phosphate + L-Val-L-Val-L-Thr

702768

-

6.3.2.B23

ATP + 3-formyl-L-tyrosine + L-threonine = 3-formyl-L-tyrosyl-L-threonine + ADP + phosphate

731979

-

Product in Enzyme-catalyzed Reactions (69 results)

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Show Product (69 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.3.1

phospho-DL-Thr + H2O = phosphate + Thr

0

-

3.1.3.1

phosphothreonine + H2O = phosphate + Thr

0

-

3.1.3.1

O-phosphothreonine + H2O = threonine + phosphate

651385, 0

-

3.1.3.16

phospho-L-threonine + H2O = L-threonine + phosphate

0

-

3.1.3.16

phosphothreonine + H2O = threonine + phosphate

0

-

3.1.3.2

L-phosphothreonine + H2O = L-threonine + phosphate

0

-

3.1.3.2

O-phospho-DL-threonine + H2O = L-threonine + phosphate

0

-

3.1.3.2

O-phospho-L-threonine + H2O = L-threonine + phosphate

0

-

3.1.3.2

O-phospho-L-threonine + H2O = phosphate + L-threonine

653409

-

3.1.3.2

phospho-L-threonine + H2O = L-threonine + phosphate

0

-

3.1.3.2

phosphothreonine + H2O = Thr + phosphate

0

-

3.1.3.2

phosphothreonine + H2O = threonine + phosphate

0

-

3.1.3.3

L-phosphothreonine + H2O = L-Thr + phosphate

0

-

3.1.3.3

O-phospho-L-threonine + H2O = L-threonine + phosphate

0

-

3.1.3.48

O-phospho-L-threonine + H2O = L-threonine + phosphate

0

-

3.1.3.48

phosphothreonine + H2O = threonine + phosphate

0

-

3.1.3.1

3 entries

3.1.3.16

2 entries

3.1.3.2

7 entries

3.1.3.3

2 entries

3.1.3.48

2 entries

3.1.3.60

O-phospho-L-threonine + H2O = L-threonine + phosphate

0

-

3.1.4.13

L-threonine-phosphoethanolamine + H2O = L-threonine + ethanolamine phosphate

81109

-

3.4.11.1

L-Thr 7-amido-4-methylcoumarin + H2O = L-Thr + 7-amino-4-methylcoumarin

0

-

3.4.11.1

L-Thr-4-nitroanilide + H2O = L-Thr + 4-nitroaniline

0

-

3.4.11.1

L-Thr-L-Leu + H2O = L-Thr + L-Leu

651119

-

3.4.11.1

Thr-Leu + H2O = Thr + Leu

651057, 643878

-

3.4.11.10

L-Thr-7-amido-4-methylcoumarin + H2O = 7-amino-4-methylcoumarin + L-Thr

0

-

3.4.11.10

L-Thr-7-amido-4-methylcoumarin + H2O = L-Thr + 7-amino-4-methylcoumarin

0

-

3.4.11.10

Thr-beta-naphthylamide + H2O = Thr + beta-naphthylamine

81181

-

3.4.11.1

4 entries

3.4.11.10

3 entries

3.4.11.14

Thr-2-naphthylamide + H2O = Thr + 2-naphthylamine

0

-

3.4.11.18

Met-Thr + H2O = Met + Thr

0

-

3.4.11.2

L-Thr-2-naphthylamide + H2O = L-Thr + 2-naphthylamine

0

-

3.4.11.2

L-Thr-7-amido-4-methylcoumarin + H2O = 7-amino-4-methylcoumarin + L-Thr

0

-

3.4.11.22

L-Ala-L-Thr + H2O = L-Ala + L-Thr

0

-

3.4.11.22

TTQRTRALV-NH2 + H2O = L-Thr + TQRTRALV-NH2

0

-

3.4.11.2

2 entries

3.4.11.22

2 entries

3.4.11.23

Thr-Leu + H2O = Thr + Leu

643878

-

3.4.11.4

L-Thr-7-amido-4-methylcoumarin + H2O = 7-amino-4-methylcoumarin + L-Thr

0

-

3.4.11.9

L-Thr-Pro-7-amido-4-carbamoylmethylcoumarin + H2O = L-Thr + Pro-7-amido-4-carbamoylmethylcoumarin

0

-

3.4.11.B9

Thr-7-amido-4-methylcoumarin + H2O = Thr + 7-amino-4-methylcoumarin

0

-

3.4.13.12

Met-Thr + H2O = Met + Thr

81205, 36096, 0

-

3.4.13.12

Thr-Ala + H2O = Thr + Ala

81205, 36096

-

3.4.13.12

2 entries

3.4.13.18

Thr-Leu + H2O = Thr + Leu

137201

-

3.4.13.9

Thr-Pro + H2O = Thr + Pro

0

-

3.4.18.1

2-aminobenzoyl-Phe-Arg-Thr + H2O = 2-aminobenzoyl-Phe-Arg + Thr

0

-

3.4.19.1

N-acetyl-Ala-Thr + H2O = N-acetyl-Ala + Thr

0

-

3.4.19.3

L-pyroglutamyl-L-Thr + H2O = L-pyroglutamate + L-Thr

0

-

3.4.19.3

pyroglutamyl-Thr + H2O = pyroglutamate + Thr

0

-

3.4.19.3

2 entries

3.4.19.5

beta-Asp-Thr + H2O = Asp + Thr

647271

-

3.4.22.40

Thr-Ser + H2O = Thr + Ser

0

-

3.4.24.15

LTLRTKL + H2O = LTLR + Thr + Lys-Leu

0

-

3.5.1.101

L-threonine amide + H2O = L-threonine + NH3

0

-

3.5.1.127

jasmonoyl-L-threonine + H2O = jasmonic acid + L-threonine

0

-

3.5.1.14

N-acetyl-L-threonine + H2O = acetate + L-threonine

0

-

3.5.1.14

N-alpha-acetyl-L-threonine + H2O = acetate + L-threonine

0

-

3.5.1.14

N-benzoyl-L-threonine + H2O = benzoate + L-threonine

0

-

3.5.1.14

N-lauroyl-L-threonine + H2O = laurate + L-threonine

0

-

3.5.1.14

4 entries

3.5.1.64

Nalpha-benzyloxycarbonyl-L-Thr + H2O = benzyl alcohol + CO2 + L-Thr

172071

-

3.5.1.87

N-carbamoyl-DL-threonine + H2O = L-threonine + CO2 + NH3

288945, 209293

-

3.5.2.9

L-trans-2-oxo-5-methyloxazolidine-4-carboxylate + H2O = L-threonine + ADP + phosphate

0

-

4.1.2.48

glycine + acetaldehyde = L-threonine

0

-

4.1.2.5

glycine + acetaldehyde = L-threonine

0

-

4.2.3.1

DL-vinylglycine + H2O = L-threonine

137560

-

4.2.3.1

L-vinylglycine + phosphate + H2O = L-threonine + phosphate

0

-

4.2.3.1

O-phospho-L-homoserine + H2O = L-threonine + phosphate

137547, 137545, 137546, 137552, 137554, 652479, 0, 137549, 137551, 652228, 137544, 137548, 137558, 651164, 137555, 137557, 137556, 137550, 137553, 653789

-

5.1.1.10

D-Thr = L-Thr

0

-

5.1.1.10

L-Thr = L-Thr

0, 2047

-

5.1.1.10

D-threonine = L-threonine

0

-

4.2.3.1

3 entries

5.1.1.10

3 entries

5.1.1.18

D-threonine = L-threonine

0

-

6.1.1.3

AMP + diphosphate + L-threonyl-tRNAThr = ATP + L-threonine + tRNAThr

0

-

6.1.1.6

AMP + L-threonyl-tRNALys + diphosphate = ATP + L-threonine + tRNALys

0

-

6.1.1.9

L-threonyl-tRNAVal = L-threonine + tRNAVal

653390

-

6.1.1.9

L-threonyl-tRNAVal-AMP = L-threonine + tRNAVal + AMP

653390

-

6.1.1.9

2 entries

7.4.2.2

ATP + H2O + L-threonine-[L-threonine-binding protein][side 1] = ADP + phosphate + L-threonine[side 2] + [L-threonine-binding protein][side 1]

0

-

Activator in Enzyme-catalyzed Reactions (10 results)

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Show Activating Compound (10 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.4.1.2

-

727059

-

2.5.1.48

2 mM, increases the expression level of CGS

666989

-

2.7.2.4

0.01 mM, mutant G135A, activity 110%, mutant R150A, activity 115%

642333

-

2.7.2.4

enhances activity up to 140% at 0.2 mM

660868

-

2.7.2.4

slight activation at low concentration

642313

-

2.7.2.4

3 entries

2.7.4.3

activation

642602

-

3.5.4.1

1 mM, relative activity 120%

209497

-

6.4.1.3

activates

1864

-

7.4.2.1

slight activation

718559

-

7.4.2.11

120% activity at 50 mM with D-methionine as substrate

749753

-

Inhibitor in Enzyme-catalyzed Reactions (78 results)

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Show Inhibitors (78 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.3

-

246382, 246384, 246385, 246386, 246387, 246392, 246394, 246395, 246398, 246399, 246403, 657018, 712490

-

1.1.1.3

allosteric inhibitor

739791

-

1.1.1.3

degree of inhibition depends on age of plant; sensitive and insensitive isozymes

246388

-

1.1.1.3

not inhibitory

246393

-

1.1.1.3

sensitive and insensitive isozymes

246391

-

1.1.1.3

strong inhibition of both enzyme activities, aspartate dehydrogenase and aspartate kinase activity, by decreasing the affinity of the enzyme for substrate and cofactors, kinetic effects

642340

-

1.1.1.3

the enzyme activity is subjected to feedback regulation by L-threonine

738802

-

1.1.1.3

the natural threonine binding sites of the enzyme are predicted and verified by mutagenesis experiments

739779

-

1.1.1.3

the regulatory domain of the enzyme contains 2 binding sites, interaction with Gln443 leads to inhibition of the aspartate kinase activity and facilitates the binding of a second threonine on Gln524 leading to inhibition of the homoserine dehydrogenase activity, inhibition of the forward reactions

642341

-

1.1.1.3

weakly inhibits reverse but not forward reaction

246401

-

1.1.1.3

-

662432

-

1.1.1.3

90% inhibition of homoserine dehydrogenase 2 at 10 mM

670165

-

1.1.1.3

feedback inhibition, one isozyme is resistant and another is sensitive to threonine inhibition, 46.9% inhibition at 1 mM, 63.9% at 5 mM

689647

-

1.1.1.3

the methionine-producing strain contains a deregulated homoserine dehydrogenase that is not sensitive to feedback inhibition as the wild-type enzyme

688822

-

1.1.1.3

14 entries

1.1.1.95

-

287525

-

1.2.1.11

-

390187

-

1.2.1.11

at 1 mM: 25% repression of the enzyme synthesis, at 5 mM: 43% repression of the enzyme synthesis, at 10 mM: 37% inhibition of the enzyme activity assayed in the reverse reaction

390201

-

1.2.1.11

enzyme assayed in the reverse reaction at pH 10

390193

-

1.2.1.11

represses the enzyme considerably

390196

-

1.4.1.1

-

349567

-

1.4.1.1

inhibition of aminating activity

349566

-

1.4.1.1

reductive amination of pyruvate, 10 mM, 37% inhibition

349563

-

1.2.1.11

4 entries

1.4.1.1

3 entries

1.4.7.1

-

392005

-

2.1.2.1

-

441400

-

2.2.1.6

5 mM, 6.6% inhibition

395883

-

2.3.1.37

-

486820

-

2.3.1.50

competitive to L-serine

487172

-

2.5.1.76

1 mM, more than 80% reemaining activity

696127

-

2.7.1.39

-

641462, 641465

-

2.7.1.39

10 mM, 18% inhibition

641461

-

2.7.1.39

8.1 mM, 50% inhibition

641466

-

2.7.1.39

competitive to the substrate L-homoserine

641470

-

2.7.1.39

half-maximal inhibition at 10 mM

641468

-

2.7.1.39

substrate inhibition

641471

-

2.7.1.39

competitive inhibition

759641

-

2.7.1.39

competitive inhibition, interaction with ThrB residue A20 is important. Highly reduced inhibition of enzyme mutant A20G. The changes in L-threonine affinity to the CglThrB-A20G active site derive from loss of van der Waals interactions

758579

-

2.7.1.39

8 entries

2.7.1.40

fructose 1,6-diphosphate protects

641562

-

2.7.1.80

100 mM, weak inhibition

642033

-

2.7.2.4

-

642308, 642310, 642311, 642312, 642314, 642316, 642320, 642327, 642331, 642332, 642337, 642339, 642340, 642341, 660862, 660868, 677365, 703647, 722530, 722849, 738419, 762121, 762473

-

2.7.2.4

61.33% residual activity at 10 mM

762390

-

2.7.2.4

75% inhibition at 10 mM, 22°C culture temperature, 22°C assay temperature, 71% inhibition at 10 mM, 37°C culture temperature, 22°C assay temperature, 87% inhibition at 10 mM, 22°C culture temperature, 37°C assay temperature, 86% inhibition at 10 mM, 37°C culture temperature, 37°C assay temperature, 93% inhibition of glutathione-S-transferase fusion protein at 10 mM, 22°C assay temperature, 73% inhibition of glutathione-S-transferase fusion protein at 10 mM, 37°C assay temperature; reduced sensitivity to threonine inhibition, 0% inhibition at 10 mM, 22°C culture temperature, 22°C assay temperature, 15% inhibition at 10 mM, 37°C culture temperature, 22°C assay temperature, 4% inhibition at 10 mM, 22°C culture temperature, 37°C assay temperature, 14% inhibition at 10 mM, 37°C culture temperature, 37°C assay temperature; resistance to feedback inhibition, 16% inhibition at 10 mM, 22°C culture temperature, 22°C assay temperature, 15% inhibition at 10 mM, 37°C culture temperature, 22°C assay temperature, 9% inhibition at 10 mM, 22°C culture temperature, 37°C assay temperature, 6% inhibition at 10 mM, 37°C culture temperature, 37°C assay temperature, 31% inhibition of GST-fusion protein at 10 mM, 22°C assay temperature, 16% inhibition of glutathione-S-transferase fusion protein at 10 mM, 37°C assay temperature

663452

-

2.7.2.4

89.37% residual activity at 5 mM. The inhibition rate for a single inhibitor is about 10%, this rate is further increased to 65% under the combined action of two inhibitors (Lys+Thr, Lys+Met, and Thr+Met)

762307

-

2.7.2.4

89.76% residual activity at 10 mM

761955

-

2.7.2.4

above 10 mM

642313

-

2.7.2.4

allosteric inhibition, causes a decrease in the apparent molecular mass of the enzyme, no inhibition is detected in the threonine insensitive mutant up to 50 mM threonine

660880

-

2.7.2.4

almost insensitive to threonine

660868

-

2.7.2.4

aspartokinase II, competitive inhibition

642314

-

2.7.2.4

concerted inhibition together with L-lysine

642315

-

2.7.2.4

enzyme is inhibited by lysine and threonine in a concerted manner: comparison of the crystal structures between inhibitory and active forms reveal that binding inhibitors causes a conformational change to a closed inhibitory form, and the interaction between the catalytic domain in the alpha subunit and beta subunit

722683

-

2.7.2.4

enzyme is inhibited synergistically by L-threonine and L-lysine with the binding of threonine first. In the absence of L-threonine, the enzyme is inhibited by Lys in a cooperative manner, but the inhibition requires very high concentrations of L-lysine

722962

-

2.7.2.4

feedback inhibition

654640, 737413, 738802

-

2.7.2.4

feedback inhibition by the end product

677391

-

2.7.2.4

feedback resistance of Ask, more than 20% relative activity of Ask in the assay mixture even with extremely high concentrations of 100 mM L-lysine and L-threonine each, L-threonine alone has no effect on activity; more than 20% activity in the rAsk is detected even with extremely high concentrations of L-lysine and L-threonine (100 mM each), L-threonine alone has no effect on activity

677773

-

2.7.2.4

in the presence of 1 mM aspartate and 2 mM ATP

662432

-

2.7.2.4

inhibition at 0.5-1.0 mM in complemented S2207A cells is variable, it does not exceed 67%

657018

-

2.7.2.4

inhibits AK activity in a cooperative manner by 90% at 0.35 mM. The distinctive sequence of the regulatory domain in Thermotoga maritima AK-HseDH is likely responsible for the unique sensitivity to L-threonine. The quaternary structure of this enzyme is not affected by L-threonine

760736

-

2.7.2.4

isoenzyme II

642323

-

2.7.2.4

mechanism for allosteric regulation in which the domain movements induced by L-threonine binding causes displacement of the substrates from the enzyme, resulting in a relaxed, inactive conformation

693065

-

2.7.2.4

no inhibitory effect at 2 mM

663387

-

2.7.2.4

represses, reduces growth rate, no concerted inhibition by L-lysine plus L-threonine

670165

-

2.7.2.4

repression of aspartokinase gene transcription

390201

-

2.7.2.4

some inhibition of the first isoenzyme, together with L-lysine total inhibition

677561

-

2.7.2.4

Thr alone has no effect on the inhibitory profile, the enzyme is inhibited dramatically by simultaneous addition of Lys and Thr; threonine alone has no effect, simultaneous addition of lysine and threonine inhibits dramatically

681433

-

2.7.2.4

threonine and lysine exhibit concerted feedback inhibition of asparatate kinase

737927

-

2.7.2.4

-

721208, 723684, 760525

-

2.7.2.4

27 entries

2.7.8.4

27-34% inhibition of the reaction

643775

-

3.5.1.9

19% inhibition at 20 mM

209242

-

3.7.1.3

competitive inhibition, 10 mM

289258

-

4.3.1.17

competitive

210774

-

4.3.1.17

100 mM, 56% inhibition

651494

-

4.3.3.7

at 100 mM 23% residual activity, at 100 mM 33% residual activity

702448

-

4.3.3.7

at 100 mM 40% residual activity

702448

-

4.3.1.17

2 entries

4.3.3.7

2 entries

4.4.1.1

weak

34507

-

4.4.1.28

less effective inhibitor, Ki-value above 150 mM

34507

-

6.1.1.11

-

692299

-

7.4.2.1

-

718559

-

7.4.2.1

1% cell growth, 1% viability of cells

675890

-

7.4.2.1

2 entries

7.4.2.11

89% residual activity at 5 mM with L-methionine as substrate

749753

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (109 results)

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Show Turnover Number (109 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.103

0.07

-

30°C, pH not specified in the publication, mutant enzyme T177A

762728

1.1.1.103

0.37

-

25°C, pH 10, mutant enzyme D180A

762551

1.1.1.103

0.52

-

30°C, pH not specified in the publication, mutant enzyme S111A

762728

1.1.1.103

0.55

-

pH 7.5, 65°C, recombinant mutant E199A

688343

1.1.1.103

0.6

-

30°C, pH not specified in the publication, mutant enzyme Y136F

762728

1.1.1.103

0.667

-

pH 7.5, 65°C, recombinant mutant R204A

688343

1.1.1.103

0.73

-

25°C, pH 10, mutant enzyme I113A

762551

1.1.1.103

1.6

-

25°C, pH 10, mutant enzyme G114A

762551

1.1.1.103

1.7

-

25°C, pH 10, wild-type enzyme

762551

1.1.1.103

7.2

-

pH 7.5, 65°C

669546

1.1.1.103

11

-

pH 7.5, 65°C, recombinant wild-type enzyme

688343

1.1.1.103

23.3

-

-

285713

1.1.1.103

43.8

-

pH 10.0, 30°C, native enzyme

721272

1.1.1.103

46.7

-

mutant enzyme M333E, at pH 7.5 and 37°C

738933

1.1.1.103

47.3

-

wild type enzyme, at pH 7.5 and 37°C

738933

1.1.1.103

48.8

-

30°C, pH not specified in the publication, wild-type enzyme

762728

1.1.1.103

50

-

wild type enzyme, at pH 10.0 and 30°C

738606

1.1.1.103

135

-

-

285716

1.1.1.103

551.7

-

pH 7.5, 65°C

669546

1.1.1.103

19 entries

2.2.1.8

0.052

-

at pH 7.5 and 28°C

755884

2.6.1.64

0.013

-

pH 8.0, 25°C

662056

2.7.1.177

0.016

-

mutant D135N, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.0188

-

mutant E24Q, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.0193

-

mutant E132A, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.0238

-

mutant S255A, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.0258

-

mutant E132Q, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.0287

-

mutant S253A, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.0322

-

mutant D103A, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.0325

-

mutant S99A, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.0353

-

mutant T134A, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.0358

-

mutant D103N, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.037

-

mutant T101A, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.0427

-

wild-type, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

12 entries

4.1.2.26

580

-

pH 8.5, 30°C

663708

4.1.2.48

0.0073

-

pH 7.0, 30°C, mutant enzyme H83F/H126F

747734

4.1.2.48

0.0178

-

mutant enzyme H177Y, in 50 mM Tris-HCl buffer (pH 8.0)

681356

4.1.2.48

0.0195

-

recombinant wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0)

681356

4.1.2.48

0.02

-

mutant H83F, pH 7.0, 30°C

727485

4.1.2.48

0.2

-

mutant D95N/E96S, pH 8.0, 30°C

728820

4.1.2.48

0.28

-

mutant H83N, pH 7.0, 30°C

727485

4.1.2.48

0.33

-

pH 7.0, 30°C, mutant enzyme F87D

747734

4.1.2.48

0.6

-

mutant D95G/E96G, pH 8.0, 30°C

728820

4.1.2.48

0.72

-

pH 7.0, 30°C, mutant enzyme F87A

747734

4.1.2.48

0.72

-

pH 7.0, 30°C, mutant enzyme K222A

747734

4.1.2.48

1.1

-

pH 8.0, 25°C

716291

4.1.2.48

1.87

-

pH 7.0, 30°C, wild-type enzyme

747734

4.1.2.48

1.87

-

wild-type, pH 7.0, 30°C

727485

4.1.2.48

3

-

mutant D95C, pH 8.0, 30°C

728820

4.1.2.48

3.3

-

wild-type, pH 8.0, 30°C

728820

4.1.2.48

3.5

-

mutant D95Y, pH 8.0, 30°C

728820

4.1.2.48

3.6

-

mutant D95M, pH 8.0, 30°C

728820

4.1.2.48

3.8

-

mutant D95L, pH 8.0, 30°C

728820

4.1.2.48

4.37

-

mutant H126N, pH 7.0, 30°C

727485

4.1.2.48

6

-

mutant H126F, pH 7.0, 30°C

727485

4.1.2.48

9.6

-

mutant D95W, pH 8.0, 30°C

728820

4.1.2.48

43

-

pH 8.0, 30°C

5205

4.1.2.49

0.641

-

pH 8.0, 30°C, wild-type enzyme

746614

4.1.2.49

0.913

-

pH 8.0, 30°C, mutant enzyme S292R

746614

4.1.2.49

1.81

-

pH 8.0, 30°C, mutant enzyme H128Y

746614

4.1.2.49

2.14

-

pH 8.0, 30°C, mutant enzyme H128Y/S292R

746614

4.2.1.122

0.00068

-

recombinant wild-type enzyme, pH 7.8, 37°C

747549

4.2.1.122

0.0035

-

recombinant mutant L166A, pH 7.8, 37°C

747549

4.2.1.122

0.007

-

recombinant mutant L166V, pH 7.8, 37°C

747549

4.2.1.20

0.0007

-

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

747549

4.2.1.20

0.0035

-

mutant L166A, pH not specified in the publication, temperature not specified in the publication

747549

4.2.1.20

0.007

-

mutant L166V, pH not specified in the publication, temperature not specified in the publication

747549

4.2.1.20

0.61

-

pH 8.0, temperature not specified in the publication

747116

4.3.1.17

5.2

-

-

705606

4.3.1.17

10.5

-

pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction

661171

4.3.1.18

17.2

-

pH 8.9, 25°C

210802

4.3.1.18

19.6

-

pH 7.8, 25°C

210802

4.3.1.19

5.2

-

pH 9.0, 37°C

705606

4.3.1.19

9.42

-

pH 8.0, 30°C

747154

4.3.1.19

287

-

-

210849

4.3.1.19

1230

-

pH 7.5, 30°C, mutant enzyme F510L

747392

4.3.1.19

1256

-

pH 7.5, 30°C, mutant enzyme T344A

747392

4.3.1.19

1261

-

pH 7.5, 30°C, mutant enzyme A14T

747392

4.3.1.19

1273

-

pH 7.5, 30°C, mutant enzyme R449C

747392

4.3.1.19

1283

-

pH 7.5, 30°C, mutant enzyme G323D/F510L

747392

4.3.1.19

1298

-

pH 7.5, 30°C, mutant enzyme G323D/F510L/R449C

747392

4.3.1.19

1301

-

pH 7.5, 30°C, mutant enzyme G323D/F510L/T344A/R449C

747392

4.3.1.19

1309

-

pH 7.5, 30°C, mutant enzyme G323D/F510L/T344A

747392

4.3.1.19

1312

-

pH 7.5, 30°C, mutant enzyme G323D/R449C

747392

4.3.1.19

1369

-

pH 7.5, 30°C, mutant enzyme A14T/G323D

747392

4.3.1.19

1394

-

pH 7.5, 30°C, mutant enzyme G323D/T344A

747392

4.3.1.19

1398

-

pH 7.5, 30°C, mutant enzyme G323D

747392

4.3.1.19

1414

-

pH 7.5, 30°C, wild-type enzyme

747392

4.1.2.48

22 entries

4.1.2.49

4 entries

4.2.1.122

3 entries

4.2.1.20

4 entries

4.3.1.17

2 entries

4.3.1.18

2 entries

4.3.1.19

16 entries

6.1.1.11

0.14

-

in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication

726813

6.1.1.3

0.64

-

wild-type enzyme complementing the null mutant

653273

6.1.1.3

1.2

-

pH 7.5, 65°C, wild-type enzyme

662443

6.1.1.3

1.9

-

pH 7.2, 60°C, recombinant wild-type enzyme

663210

6.1.1.3

2

8

pH 7.4, 30°C, recombinant mutant G459D

744225

6.1.1.3

2.16

-

pH 7.5, 30°C

745349

6.1.1.3

3

6

pH 7.2, 37°C, wild-type enzyme

653312

6.1.1.3

3.32

-

in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C

727916

6.1.1.3

3.8

-

pH 7.5, 65°C, wild-type enzyme

662443

6.1.1.3

6.08

-

wild-type enzyme complementing the null mutant

653273

6.1.1.3

6.31

-

pH 7.5, 30°C

745349

6.1.1.3

13.5

-

pH 7.2, 60°C, recombinant wild-type enzyme

663210

6.1.1.3

16

-

pH 7.5, 55°C, wild-type enzyme

662443

6.1.1.3

30

-

mutant enzyme W434Y, pH 7.2, 37°C

650200

6.1.1.3

30

-

pH 7.4, 30°C, recombinant mutant P424K

744225

6.1.1.3

33

-

pH 7.5, 37°C, wild-type enzyme

662443

6.1.1.3

34

-

pH 7.4, 30°C, recombinant mutant E458D

744225

6.1.1.3

35

-

pH 7.4, 30°C, recombinant wild-type enzyme

744225

6.1.1.3

37

-

pH 7.2, 37°C, truncated enzyme DELTAN

653312

6.1.1.3

90

-

wild-type enzyme, pH 7.2, 37°C

650200

6.1.1.3

19 entries

6.2.1.70

0.485

-

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

749157

6.3.2.8

23.3

-

-

1290

K_M Value (193 results)

top print hide

Show KM Value (193 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.103

0.00057

-

25°C, pH 10, mutant enzyme G114A

762551

1.1.1.103

0.0026

-

25°C, pH 10, wild-type enzyme

762551

1.1.1.103

0.0088

-

25°C, pH 10, mutant enzyme I113A

762551

1.1.1.103

0.011

-

25°C, pH 10, mutant enzyme T178A

762551

1.1.1.103

0.01129

-

at pH 8.8 and 37°C

738860

1.1.1.103

0.0118

-

pH 7.5, 65°C, recombinant wild-type enzyme

688343

1.1.1.103

0.013

-

pH 7.5, 65°C

669546

1.1.1.103

0.043

-

25°C, pH 10, mutant enzyme D180A

762551

1.1.1.103

0.7

-

-

285703

1.1.1.103

1.1

-

demetallized enzyme

285714

1.1.1.103

1.1

-

metal-ion free enzyme

285712

1.1.1.103

1.43

-

-

285716, 285718

1.1.1.103

1.5

-

pH 7.0, 70°C, recombinant enzyme

668567

1.1.1.103

1.51

-

pH 7.5, 65°C, recombinant mutant E199A

688343

1.1.1.103

1.6

-

at 50°C

698673

1.1.1.103

2.5

-

pH 7.5, 65°C, recombinant mutant R204A

688343

1.1.1.103

3.56

-

pH 9.0, 20°C

655857

1.1.1.103

3.81

-

pH 9.0, 10°C

655857

1.1.1.103

5.38

-

-

285701

1.1.1.103

5.5

-

-

285715

1.1.1.103

5.96

-

pH 9.0, 30°C

655857

1.1.1.103

6.1

-

-

285721

1.1.1.103

8.2

-

enzyme activated with 0.07 mM Cd2+

285712

1.1.1.103

8.4

-

-

285717

1.1.1.103

8.7

-

-

285720

1.1.1.103

10.5

-

at pH 7.5

285719

1.1.1.103

11.2

-

pH 9.0, 40°C

655857

1.1.1.103

11.6

-

pH 10.0, 30°C, native enzyme

721272

1.1.1.103

13

-

-

285713

1.1.1.103

15.2

-

wild type enzyme, at pH 10.0 and 30°C

738606

1.1.1.103

17.5

-

pH 10.0, 70°C

722747

1.1.1.103

18

-

pH 9.0, 37°C

729112

1.1.1.103

19.5

-

pH 9.0, 50°C

655857

1.1.1.103

23.7

-

30°C, pH not specified in the publication, mutant enzyme T177A

762728

1.1.1.103

25.3

-

30°C, pH not specified in the publication, wild-type enzyme

762728

1.1.1.103

40.6

-

30°C, pH not specified in the publication, mutant enzyme Y136F

762728

1.1.1.103

72.4

-

wild type enzyme, at pH 7.5 and 37°C

738933

1.1.1.103

151.9

-

mutant enzyme M333E, at pH 7.5 and 37°C

738933

1.1.1.103

211

-

enzyme activated with 0.25 mM Mn2+

285712

1.1.1.103

221

-

enzyme saturated with 0.25 mM Mn2+

285714

1.1.1.103

246

-

30°C, pH not specified in the publication, mutant enzyme S111A

762728

1.1.1.103

41 entries

1.1.1.30

388

-

-

669873

1.5.1.17

25.5

-

-

13373

1.5.1.17

110

-

-

13365

1.5.1.22

48

-

-

13373

1.5.1.22

303

-

pH 7.5, 25°C

711788

1.5.1.17

2 entries

1.5.1.22

2 entries

1.5.1.28

7.4

-

pyruvate and NADH as cosubstrates

94167

2.2.1.8

1.18

-

at pH 7.5 and 28°C

755884

2.6.1.64

55

-

pH 8.0, 25°C

662056

2.7.1.177

0.127

-

calculated from double-reciprocal plots, pH 7.4, temperature not specified in the publication

717877

2.7.1.177

0.142

-

mutant T134A, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.144

-

mutant E132Q, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.146

-

Michaelis-Menten kinetics, pH 7.4, temperature not specified in the publication

717877

2.7.1.177

0.146

-

wild-type, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.176

-

mutant S99A, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.184

-

mutant D103N, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.198

-

mutant E132A, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.22

-

mutant T101A, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.258

-

mutant D103A, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.273

-

mutant D135N, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

0.464

-

mutant E24Q, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

3.708

-

mutant S255A, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

4.698

-

mutant S253A, pH 7.4, temperature not specified in the publication

717878

2.7.1.177

14 entries

2.7.7.87

0.00011

-

pH 8.0, temperature not specified in the publication

726076

4.1.2.26

29

-

pH 8.5, 30°C

663708

4.1.2.48

0.00016

-

mutant enzyme H177Y, in 50 mM Tris-HCl buffer (pH 8.0)

681356

4.1.2.48

0.00018

-

recombinant wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0)

681356

4.1.2.48

0.4

-

mutant F87A, pH 7.0, 30°C

727485

4.1.2.48

1

3

mutant D95G/E96G, pH 8.0, 30°C

728820

4.1.2.48

1.1

-

mutant H83F/H126F, pH 7.0, 30°C

727485

4.1.2.48

1.3

-

mutant F87D, pH 7.0, 30°C

727485

4.1.2.48

1.7

-

mutant H126F, pH 7.0, 30°C

727485

4.1.2.48

2.85

-

pH 8.0, 30°C

5206

4.1.2.48

3.7

-

mutant K222A, pH 7.0, 30°C

727485

4.1.2.48

4

-

pH 8.0, 25°C

716291

4.1.2.48

7

-

mutant H83F, pH 7.0, 30°C

727485

4.1.2.48

8.7

-

pH 7.0, 30°C, mutant enzyme F87A

747734

4.1.2.48

13.6

-

wild-type, pH 8.0, 30°C

728820

4.1.2.48

14.7

-

pH 8.0, 30°C

441433

4.1.2.48

19.4

-

pH 7.0, 30°C, wild-type enzyme

747734

4.1.2.48

19.4

-

wild-type, pH 7.0, 30°C

727485

4.1.2.48

21

-

pH 7.0, 30°C, mutant enzyme H83F/H126F

747734

4.1.2.48

24.9

-

pH 7.0, 30°C, mutant enzyme F87D

747734

4.1.2.48

32

-

mutant D95N/E96S, pH 8.0, 30°C

728820

4.1.2.48

38

-

mutant H83N, pH 7.0, 30°C

727485

4.1.2.48

43.1

-

pH 7.0, 37°C

718557

4.1.2.48

44

-

mutant D95C, pH 8.0, 30°C

728820

4.1.2.48

44

-

mutant D95W, pH 8.0, 30°C

728820

4.1.2.48

50

-

mutant D95M, pH 8.0, 30°C

728820

4.1.2.48

53

-

mutant D95L, pH 8.0, 30°C

728820

4.1.2.48

55

-

pH 8.0, 30°C

5205

4.1.2.48

61

-

mutant H126N, pH 7.0, 30°C

727485

4.1.2.48

63

-

mutant D95Y, pH 8.0, 30°C

728820

4.1.2.48

72

-

pH 7.0, 30°C, mutant enzyme K222A

747734

4.1.2.49

3.27

-

pH 8.0, 30°C, mutant enzyme H128Y/S292R

746614

4.1.2.49

4.48

-

pH 8.0, 30°C, mutant enzyme H128Y

746614

4.1.2.49

31.6

-

pH 8.0, 30°C, wild-type enzyme

746614

4.1.2.49

32.7

-

pH 8.0, 30°C, mutant enzyme S292R

746614

4.1.2.5

0.42

-

pH 7.0, 30°C

5199

4.1.2.5

10

-

pH and temperature not specified in the publication

713884

4.1.2.5

14.7

-

pH and temperature not specified in the publication

713884

4.2.1.122

210

-

recombinant wild-type enzyme, pH 7.8, 37°C

747549

4.2.1.122

310

-

recombinant mutant L166V, pH 7.8, 37°C

747549

4.2.1.122

340

-

recombinant mutant L166A, pH 7.8, 37°C

747549

4.2.1.20

1.3

-

pH 8.0, temperature not specified in the publication

747116

4.2.1.20

210

-

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

747549

4.2.1.20

310

-

mutant L166V, pH not specified in the publication, temperature not specified in the publication

747549

4.2.1.20

340

-

mutant L166A, pH not specified in the publication, temperature not specified in the publication

747549

4.3.1.17

0.5

-

-

680934

4.3.1.17

3.1

-

cSDH

678411

4.3.1.17

3.5

-

cSDH +Pro

678411

4.3.1.17

4.2

-

cSDH L287V

678411

4.3.1.17

7.3

-

-

705606

4.3.1.17

13.2

-

cSDH-hSDH

678411

4.3.1.17

14.9

-

hSDH -Pro

678411

4.3.1.17

50

-

37°C, pH 8.3, recombinant SDH

210800

4.3.1.17

57

-

pH 8.3, 37°C

665219

4.3.1.17

59.5

-

hSDH

678411

4.3.1.17

130

-

in presence and in absence of 20 mM NH4Cl

210785

4.3.1.19

0.25

-

-

210827

4.3.1.19

0.25

-

Ile-sensitive enzyme form and Ile-insensitive form

210855

4.3.1.19

1.3

-

Ile-sensitive enzyme

210818

4.3.1.19

1.5

-

in presence of 1 mM AMP

210830

4.3.1.19

1.6

-

Ile-sensitive enzyme

210819

4.3.1.19

1.66

-

pH 8.0, 30°C

747154

4.3.1.19

2.3

-

processed TD2

682413

4.3.1.19

2.5

-

-

210839

4.3.1.19

2.5

-

in absence of phosphate

210820

4.3.1.19

3

-

-

210821

4.3.1.19

3

-

in presence of 50 mM phosphate

210820

4.3.1.19

3

-

with AMP

210823

4.3.1.19

3

3.5

pH 7.5, 30°C, mutant enzyme G323D/R449C

747392

4.3.1.19

3.2

-

-

210824

4.3.1.19

4

-

in presence of 250 mM phosphate

210820

4.3.1.19

4.5

-

wild type enzyme

210851

4.3.1.19

5.7

-

at 40°C

210834

4.3.1.19

7.3

-

pH 9.0, 37°C

705606

4.3.1.19

7.7

-

-

210792

4.3.1.19

8

-

with AMP

210823

4.3.1.19

11

-

in presence of AMP

210833

4.3.1.19

13

-

dehydratase II

210822

4.3.1.19

13.9

-

at 65°C

210834

4.3.1.19

14

-

-

210843

4.3.1.19

14.5

-

pH 7.5, 30°C, wild-type enzyme

747392

4.3.1.19

16

-

-

210845

4.3.1.19

16

-

in the presence of 5 mM AMP

680728

4.3.1.19

19

-

mutant strain DU-21

210851

4.3.1.19

20

-

Ile-insensitive enzyme

210818, 210819

4.3.1.19

21.3

-

Ile-sensitive enzyme

210818

4.3.1.19

24

-

in absence of AMP

210830

4.3.1.19

26.2

-

pH 7.5, 30°C, mutant enzyme G323D/F510L/T344A

747392

4.3.1.19

26.4

-

pH 7.5, 30°C, mutant enzyme G323D/F510L

747392

4.3.1.19

26.9

-

pH 7.5, 30°C, mutant enzyme G323D/F510L/T344A/R449C

747392

4.3.1.19

27.1

-

pH 7.5, 30°C, mutant enzyme G323D/F510L/R449C

747392

4.3.1.19

28.3

-

pH 7.5, 30°C, mutant enzyme F510L

747392

4.3.1.19

30.1

-

pH 7.5, 30°C, mutant enzyme A14T/G323D

747392

4.3.1.19

32

-

in the presence of 5 mM CMP

680728

4.3.1.19

32.5

-

pH 7.5, 30°C, mutant enzyme A14T

747392

4.3.1.19

32.8

-

pH 7.5, 30°C, mutant enzyme R449C

747392

4.3.1.19

33.3

-

pH 7.5, 30°C, mutant enzyme T344A

747392

4.3.1.19

33.6

-

pH 7.5, 30°C, mutant enzyme G323D

747392

4.3.1.19

33.7

-

pH 7.5, 30°C, mutant enzyme G323D/T344A

747392

4.3.1.19

34

-

dehydratase I

210822

4.3.1.19

70

-

without AMP

210823

4.3.1.19

91

-

in absence of AMP

210833

4.3.1.19

99.5

-

-

210849

4.3.1.19

123

-

-

680728

4.3.1.19

125

-

without AMP

210823

4.3.1.19

129

-

-

210852

4.1.2.48

29 entries

4.1.2.49

4 entries

4.1.2.5

3 entries

4.2.1.122

3 entries

4.2.1.20

4 entries

4.3.1.17

11 entries

4.3.1.19

50 entries

5.1.1.10

31

-

-

2047

6.1.1.11

2

3.4

in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication

726813

6.1.1.3

0.00003

-

wild-type enzyme complementing the null mutant

653273

6.1.1.3

0.00189

-

-

409

6.1.1.3

0.09

-

pH 7.5, 65°C, wild-type enzyme

662443

6.1.1.3

0.1

-

pH 7.2, 60°C, recombinant wild-type enzyme

663210

6.1.1.3

0.1

-

pH 7.5, 55°C, wild-type enzyme

662443

6.1.1.3

0.1

-

pH 7.5, 65°C, wild-type enzyme

662443

6.1.1.3

0.101

-

pH 7.4, 30°C, recombinant mutant G459D

744225

6.1.1.3

0.104

-

pH 7.4, 30°C, recombinant mutant E458D

744225

6.1.1.3

0.105

-

pH 7.4, 30°C, recombinant wild-type enzyme

744225

6.1.1.3

0.108

-

pH 7.4, 30°C, recombinant mutant P424K

744225

6.1.1.3

0.11

-

pH 7.2, 37°C, wild-type enzyme

653312

6.1.1.3

0.11

-

pH 7.2, 60°C, recombinant wild-type enzyme

663210

6.1.1.3

0.11

-

pH 7.5, 37°C, wild-type enzyme

662443

6.1.1.3

0.18

-

pH 7.2, 37°C, truncated enzyme DELTAN

653312

6.1.1.3

0.201

-

wild-type enzyme, pH 7.2, 37°C

650200

6.1.1.3

0.3

-

in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C

727916

6.1.1.3

0.897

-

mutant enzyme W434Y, pH 7.2, 37°C

650200

6.1.1.3

3.39

-

pH 7.5, 30°C

745349

6.1.1.3

4.4

-

pH 7.5, 30°C

745349

6.1.1.3

19 entries

6.1.1.9

0.3

-

ATP-diphosphate exchange reaction, native wild-type enzyme, pH 7.5, 25°C

650122

6.2.1.70

3.1

-

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

749157

6.3.2.8

25

-

-

1290