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Ligand 2-oxoadipic acid

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

lysine metabolism, tryptophan metabolism

KEGG

2-Oxocarboxylic acid metabolism, Biosynthesis of amino acids, Biosynthesis of cofactors, Biosynthesis of secondary metabolites, Lysine biosynthesis, Lysine degradation, Methane metabolism, Microbial metabolism in diverse environments, Tryptophan metabolism more

MetaCyc

2-amino-3-carboxymuconate semialdehyde degradation to glutaryl-CoA, coenzyme B biosynthesis, L-lysine biosynthesis IV, L-lysine biosynthesis V, L-lysine degradation II (L-pipecolate pathway), L-lysine degradation V, L-lysine degradation XI more

Show all BRENDA pathways known for 2-oxoadipic acid

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Roles as Enzyme Ligand

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

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Show Natural Substrate (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.172

2-oxoadipate + NADH = 2-hydroxyadipate + NAD+

286113, 286112

-

1.13.11.93

2-oxoadipate + O2 = (R)-2-hydroxyglutarate + CO2

765308

-

In Vivo Product in Enzyme-catalyzed Reactions (10 results)

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Show Natural Product (10 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.286

homoisocitrate + NAD+ = 2-oxoadipate + CO2 + NADH + H+

0

-

1.1.1.286

homoisocitrate + NADP+ = 2-oxoadipate + CO2 + NADPH + H+

0

-

1.1.1.87

(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH + H+

0

-

1.1.1.87

(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + NADH + H+ + CO2

0

-

1.1.1.87

1-hydroxy-1,2,4-butanetricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH

644538, 0, 288190

-

1.1.1.87

3-carboxy-2-hydroxyadipate + NAD+ = 2-oxoadipate + CO2 + NADH

0

-

1.1.1.87

homoisocitrate + NAD+ = 2-oxoadipate + CO2 + NADH + H+

0

-

1.1.1.286

2 entries

1.1.1.87

5 entries

1.4.3.3

D-alpha-aminoadipate + H2O + O2 = 2-oxoadipate + NH3 + H2O2

0

-

2.6.1.39

L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate

0, 639974

-

2.6.1.57

alpha-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate

0

-

Substrate in Enzyme-catalyzed Reactions (38 results)

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Show Substrate (38 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.172

2-oxoadipate + NADH = 2-hydroxyadipate + NAD+

286113, 286112

-

1.1.99.30

2-oxoadipate + reduced benzyl viologen = 2-hydroxyadipate + oxidized benzyl viologen

644550

-

1.1.99.30

2-oxoadipate + reduced methyl viologen = 2-hydroxyadipate + oxidized methyl viologen

644550

-

1.1.99.30

2 entries

1.13.11.93

2-oxoadipate + O2 = (R)-2-hydroxyglutarate + CO2

765308

-

1.14.11.17

taurine + alpha-ketoadipate + O2 = sulfite + aminoacetaldehyde + pentan-1,5-dioic acid + CO2

285263

-

1.14.11.48

xanthine + 2-oxoadipate + O2 = ?

731289

-

1.14.11.9

naringenin + 2-oxoadipate + O2 = dihydrokaempferol + pentanedioate + CO2

439124

-

1.14.20.7

2-oxoadipate + L-arginine + O2 = glutarate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O

741936

-

1.2.1.105

2-oxoadipate + CoA + NAD+ = glutaryl-CoA + CO2 + NADH

758854, 759216

-

1.2.1.105

2-oxoadipate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-glutaryldihydrolipoyllysine + CO2

759216, 763053

-

1.2.4.2

2-oxoadipate + 2,6-dichlorophenolindophenol = ? + reduced 2,6-dichlorophenolindophenol

759216

-

1.2.4.2

2-oxoadipate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-glutaryldihydrolipoyllysine + CO2

759216, 763053, 763067

-

1.2.1.105

2 entries

1.2.4.2

2 entries

1.2.7.1

2-oxoadipate + CoA + 2 methyl viologen = ?

673610

-

1.2.7.11

2-oxoadipate + CoA + 2 methyl viologen = glutaryl-CoA + CO2 + 2 reduced methyl viologen + 2 H+

673610

-

1.4.1.4

2-oxoadipate + NADPH + NH3 = L-2-aminoadipate + NADP+ + H2O

656309

-

1.5.1.7

L-lysine + alpha-ketoadipate + NADH = ?

685171

-

2.3.3.14

acetyl-CoA + H2O + 2-oxoadipate = 2-hydroxyhexane-1,2,6-tricarboxylate

488148

-

2.6.1.11

N2-acetyl-L-ornithine + 2-oxohexanedioic acid = N-acetyl-L-glutamate 5-semialdehyde + 2-aminohexanedioic acid

644949, 644951

-

2.6.1.36

L-lysine + 2-oxoadipate = 2-aminoadipate 6-semialdehyde + L-homoglutarate

637023

-

2.6.1.39

2-oxoadipate + L-glutamate = L-2-aminoadipate + 2-oxoglutarate

659885, 689965, 737334

-

2.6.1.50

L-glutamine + 2-oxoadipate = 2-oxoglutaramate + L-2-amino-1,6-hexandioate

640128

-

2.6.1.57

2-oxoadipate + L-glutamate = alpha-aminoadipate + 2-oxoglutarate

759287

-

2.6.1.57

L-phenylalanine + 2-oxoadipate = phenylpyruvate + L-2-aminoadipate

737334

-

2.6.1.7

L-kynurenine + 2-oxoadipate = ?

702779

-

2.6.1.7

L-kynurenine + 2-oxoadipate = kynurenic acid + 2-aminoadipate + H2O

636633, 636638, 636625

-

2.6.1.7

L-kynurenine + 2-oxohexanedioate = kynurenic acid + 2-aminohexanedioate + H2O

636608, 636623, 636614

-

2.6.1.74

D-Ala-D-Ala + 2-oxoadipate = ? + 2-aminoadipate

640195

-

2.6.1.74

D-alanine + 2-oxoadipate = pyruvate + 2-aminoadipate

640195

-

2.6.1.74

D-aspartate + 2-oxoadipate = oxaloacetate + 2-aminoadipate

640195

-

2.6.1.74

D-cystine + 2-oxoadipate = ? + 2-aminoadipate

640195

-

2.6.1.74

D-glutamate + 2-oxoadipate = 2-oxoglutarate + 2-aminoadipate

640195

-

2.6.1.74

D-leucine + 2-oxoadipate = 4-methyl-2-oxopentanoate + 2-aminoadipate

640195

-

2.6.1.74

D-methionine + 2-oxoadipate = 4-methylsulfanyl-2-oxobutanoate + 2-aminoadipate

640195

-

2.6.1.74

D-serine + 2-oxoadipate = 3-hydroxy-2-oxopropanoate + 2-aminoadipate

640195

-

2.6.1.74

D-tryptophan + 2-oxoadipate = 3-indole-2-oxopropanoate + 2-aminoadipate

640195

-

2.6.1.74

D-valine + 2-oxoadipate = 3-methyl-2-oxobutanoate + 2-aminoadipate

640195

-

2.6.1.57

2 entries

2.6.1.7

3 entries

2.6.1.74

10 entries

2.6.1.9

L-histidinol phosphate + 2-oxoadipate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + 2-aminoadipate

637142

-

2.8.3.6

succinyl-CoA + 2-oxoadipate = succinate + 2-oxoadipyl-CoA

646002

-

Product in Enzyme-catalyzed Reactions (26 results)

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Show Product (26 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.286

(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH + H+

0

-

1.1.1.286

homoisocitrate + NAD+ = 2-oxoadipate + CO2 + NADH + H+

0

-

1.1.1.286

homoisocitrate + NADP+ = 2-oxoadipate + CO2 + NADPH + H+

0

-

1.1.1.87

(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH + H+

0

-

1.1.1.87

(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + NADH + H+ + CO2

0

-

1.1.1.87

1-hydroxy-1,2,4-butanetricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH

0, 644538, 288190, 644539

-

1.1.1.87

3-carboxy-2-hydroxyadipate + NAD+ = 2-oxoadipate + CO2 + NADH

0

-

1.1.1.87

homoisocitrate + NAD+ = 2-oxoadipate + CO2 + NADH + H+

0

-

1.1.1.87

2(R),3(S)-homoisocitrate + NAD+ = alpha-ketoadipate + NADH + CO2 + H+

0

-

1.1.1.87

homoisocitrate + NAD+ = alpha-ketoadipate + NADH + CO2

0

-

1.1.1.87

homoisocitrate + NAD+ = alpha-ketoadipate + NADH + CO2 + H+

0

-

1.1.1.87

homoisocitrate + NAD+ = alpha-ketoadipate + NADH + H+ + CO2

0

-

1.1.1.87

homoisocitrate + NADP+ = alpha-ketoadipate + NADPH + H+ + CO2

0

-

1.1.1.286

3 entries

1.1.1.87

10 entries

1.4.3.1

D-alpha-aminoadipic acid + H2O + O2 = 2-oxoadipic acid + NH3 + H2O2

0

-

1.4.3.3

D-alpha-aminoadipate + H2O + O2 = 2-oxoadipate + NH3 + H2O2

0

-

2.3.3.9

glyoxylate + butyryl-CoA + H2O = 2-oxohexanedioic acid + CoA

0

-

2.6.1.1

2-aminohexanedioic acid + 2-oxoglutarate = 2-oxohexanedioic acid + L-glutamate

0

-

2.6.1.39

2-aminoadipate + pyruvate = 2-oxoadipate + L-alanine

0

-

2.6.1.39

2-oxoglutarate + L-2-aminoadipate = 2-oxoadipate + L-glutamate

0

-

2.6.1.39

DL-2-aminopimelic acid + 2-oxoglutarate = 2-oxoadipate + L-glutamate

0

-

2.6.1.39

L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate

639983, 639985, 0, 639979, 639974

-

2.6.1.39

L-2-aminoadipate + 4-hydroxyphenylpyruvate = 2-oxoadipate + L-tyrosine

0

-

2.6.1.39

5 entries

2.6.1.57

alpha-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate

0

-

2.6.1.7

L-2-aminohexane-1,6-dioate + 2-oxoglutarate = 2-oxohexane-1,6-dioate + L-glutamate

636614

-

2.6.1.9

3-(imidazol-4-yl)-2-oxopropyl phosphate + L-2-aminoadipate = L-histidinol phosphate + 2-oxoadipate

0

-

3.1.1.41

alpha-ketoadipinyl-7-aminocephalosporanic acid + H2O = 7-aminocephalosporanic acid + alpha-ketoadipate

0

-

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.87

required for reductive carboxylation

644539

-

Inhibitor in Enzyme-catalyzed Reactions (13 results)

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Show Inhibitors (13 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.87

-

644540

-

1.14.11.2

-

439217

-

1.14.11.2

competitive inhibitor with respect to 2-oxoglutarate, noncompetitive with respect to Fe2+

439193

-

1.14.11.2

2 entries

1.14.11.3

38% inhibition at 2.5 mM

439174

-

1.14.11.7

-

349014

-

1.5.1.7

-

685171

-

2.6.1.19

-

637035

-

2.6.1.7

-

636608, 636623

-

2.7.11.4

-

349056, 640583

-

2.8.3.6

38% inhibition at 2.5 mM, 58% inhibition at 5 mM

646002

-

4.1.3.17

competitive with respect to DL-4-carboxy-4-hydroxy-2-oxoadipate

33193

-

4.3.3.7

maximal inhibition of 40% (highest inhibition achieved relative to that in absence of inhibitor by varying the concentration of the inhibitor at a given concentration of other substrates pyruvate 0.5 mM and 0.4 mM L-aspartate-4-semialdehyde), in a coupled assay with recombinant dihydrodipicolinate reductase

746457

-

6.4.1.1

-

1759

-

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

1.13.12.19

5v2z, 3D-view

1.14.11.34

5v2z, 3D-view

4.1.1.77

5d2k, 3D-view

4.2.1.41

5hwm, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (9 results)

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Show Turnover Number (9 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.13.11.93

5.5

-

pH 7, 30°C

765308

1.14.11.48

7.6

-

25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli

731289

1.14.20.7

0.0042

-

pH 7.5, 25°C, recombinant enzyme

741936

1.2.1.105

3.5

-

enzyme-specific activity, pH 7.5, 37°C

759216

1.2.1.105

3.6

-

overall-assay, pH 7.5, 37°C

759216

1.2.4.2

3.5

-

enzyme-specific activity, pH 7.5, 37°C

759216

1.2.4.2

3.6

-

overall-assay, pH 7.5, 37°C

759216

1.2.1.105

2 entries

1.2.4.2

2 entries

2.6.1.39

22.3

-

pH 7.5, 45°C

659885

2.6.1.7

4.84

-

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

702779

K_M Value (27 results)

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Show KM Value (27 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.172

2.6

-

-

286112

1.1.1.87

1.5

-

-

644539

1.13.11.93

0.06

-

pH 7, 30°C

765308

1.14.11.48

0.16

-

25°C, pH 7.4, recombinant enzyme isolated from Escherichia coli

731289

1.14.11.9

1.4

-

-

439124

1.14.20.7

0.031

-

pH 7.5, 25°C, recombinant enzyme

741936

1.2.1.105

0.107

-

component E1, pH 7.5, 37°C

758854

1.2.1.105

0.52

-

recombinant enzyme complex, pH 7.5, 37°C

758854

1.2.4.2

0.008

-

preparation from liver, low affinity state, pH 7, temperature not specified in the publication

763067

1.2.4.2

0.27

-

preparation from liver, pH 7, temperature not specified in the publication

763067

1.2.4.2

0.45

-

preparation from heart, pH 7, temperature not specified in the publication

763067

1.2.4.2

0.45

-

preparation from liver, low affinity state, pH 7, temperature not specified in the publication

763067

1.2.4.2

0.55

-

preparation from heart, pH 7, temperature not specified in the publication

763067

1.2.1.105

2 entries

1.2.4.2

5 entries

1.5.1.7

5.3

-

at pH 7.0

685171

2.3.3.14

1.24

-

-

488148

2.6.1.39

0.01

-

pH 6.5, 37°C

636623

2.6.1.39

0.024

-

pH 7.5, 45°C

659885

2.6.1.39

0.1

-

pH 7.0, 22°C

737334

2.6.1.39

0.12

-

pH 7.0, temperature not specified in the publication

721430

2.6.1.39

0.5

-

pH 7.0, 37°C

639979

2.6.1.39

1

-

pH 8.0, 37°C isoenzyme AadAT-II

639983

2.6.1.39

2.5

-

pH 8.0, 37°C isoenzyme AadAT-I

639983

2.6.1.57

0.1

-

pH 7.0, 22°C

737334

2.6.1.57

0.1

-

pH and temperature not specified in the publication, with L-glutamate

759287

2.6.1.57

0.13

-

pH and temperature not specified in the publication, with L-glutamate

759287

2.6.1.7

0.01

-

-

636623

2.6.1.7

20.9

-

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

702779

2.6.1.39

7 entries

2.6.1.57

3 entries

2.6.1.7

2 entries

K_i Value (4 results)

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Show KI Value (4 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.11.2

0.2

-

-

439217

1.14.11.2

0.9

-

-

439193

1.14.11.2

2 entries

1.14.11.7

1

-

competitive inhibition with respect to 2-oxoglutarate and noncompetitive with respect to Fe2+ and the peptide substrate

349014

1.5.1.7

5.3

-

at pH 7.0

685171

References & Links

Literature References (53)

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Show Reference (53 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

1759

3971971

The sub-cellular localisation and regulatory properties of pyruvate carboxylase from Rhizopus arrhizus

1985

Osmani, S.A.; Scrutton, M.C.

Eur. J. Biochem.

147

119-128

33193

2229032

Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae grown on phthalate

1990

Maruyama, K.

J. Biochem.

108

327-333

285263

9287300

Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli

1997

Eichhorn, E.; Van der Ploeg, J.R.; Kertesz, M.A.; Leisinger, T.

J. Biol. Chem.

272

23031-23036

286112

185965

Purification and properties of alpha-ketoadipate reductase, a newly discovered enzyme from human placenta

1976

Suda, T.; Robinson, J.C.; Fjellstedt, T.A.

Arch. Biochem. Biophys.

176

610-620

286113

901489

Subcellular localization and tissue distribution of alpha-ketoadipate reduction and oxidation in the rat

1977

Suda, T.; Robinson, J.C.; Fjellstedt, T.A.

Biochem. Biophys. Res. Commun.

77

586-591

288190

3142867

Lysine biosynthesis pathway and biochemical blocks of lysine auxotrophs of Schizosaccharomyces pombe

1988

Ye, Z.H.; Bhattacharjee, J.K.

J. Bacteriol.

170

5968-5970

349014

2994628

Differences between collagen hydroxylases and 2-oxoglutarate dehydrogenase in their inhibition by structural analogues of 2-oxoglutarate

1985

Majamaa, K.; Turpeenniemi-Hujanen, T.M.; Latipää, P.; Gunzler, V.; Hanauske-Abel, H.M.; Hassinen, I.E.; Kivirikko, K.I.

Biochem. J.

229

127-133

349056

2853818

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

1988

Paxton, R.

Methods Enzymol.

166

313-320

439124

9395322

Identification of strictly conserved histidine and arginine residues as part of the active site in Petunia hybrida flavanone 3beta-hydroxylase

1997

Lukacin, R.; Britsch, L.

Eur. J. Biochem.

249

748-757

439174

4265566

Thymidine 2-hydroxylation in Neurospora crassa

1972

Bankel, L.; Lindstedt, G.; Lindstedt, S.

J. Biol. Chem.

247

6128-6134

439193

6321169

The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for 2-oxoglutarate decarboxylation in a ligand reaction at the enzyme-bound ferrous ion

1984

Majamaa, K.; Hanauske-Abel, H.M.; Gunzler, V.; Kivirikko, K.I.

Eur. J. Biochem.

138

239-245

439217

3036064

Characterization of a low-relative-molecular-mass prolyl 4-hydroxylase from the green alga Chlamydomonas reinhardii

1987

Kaska, D.D.; Gunzler, V.; Kivirikko, K.I.; Myllylä, R.

Biochem. J.

241

483-490

488148

9294461

Purification of the Acobacter vinelandii nifV-encoded homocitrate synthase

1997

Zheng, L.; White, H.R.; Dean, D.R.

J. Bacteriol.

179

5963-5966

636608

3037259

Kynurenine-oxoglutarate aminotransferase from rat kidney

1987

Tobes, M.C.

Methods Enzymol.

142

217-224

636614

3003516

L-Kynurenine transaminase from Hansenula schneggii

1985

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

Methods Enzymol.

113

90-95

636623

6830814

Purification, characterization and identification of rat liver mitochondrial kynurenine aminotransferase with alpha-aminoadipate aminotransferase

1983

Takeuchi, F.; Otsuka, H.; Shibata, Y.

Biochim. Biophys. Acta

743

323-330

636625

7493966

Cloning and functional expression of a soluble form of kynurenine/alpha-aminoadipate aminotransferase from rat kidney

1995

Buchli, R.; Alberati-Giani, D.; Malherbe, P.; Kohler, C.; Broger, C.; Cesura, A.M.

J. Biol. Chem.

270

29330-29335

636633

9078543

Kynurenic acid and kynurenine aminotransferase in heart

1997

Baran, H.; Amann, G.; Lubec, B.; Lubec, G.

Pediatr. Res.

41

404-410

636638

12110301

Isolation, characterization, and functional expression of kynurenine aminotransferase cDNA from the yellow fever mosquito, Aedes aegypti(1)

2002

Fang, J.; Han, Q.; Li, J.

Insect Biochem. Mol. Biol.

32

943-950

637023

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Links to other databases for 2-oxoadipic acid

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