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Basic Ligand Information
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Enzyme Kinetic Parameters
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Ligand 4-hydroxy-2-oxoglutarate

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Basic Ligand Information

Molecular Structure

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Molecular Formula

BRENDA Name

InChIKey

C₅H₆O₆

4-hydroxy-2-oxoglutarate

WXSKVKPSMAHCSG-UHFFFAOYSA-N

Synonyms:

2-hydroxy-4-oxopentanedioic acid, 4-Hydroxy-2-ketoglutarate, 4-hydroxy-alpha-ketoglutarate, D,L-4-hydroxy-2-oxoglutarate, DL-2-keto-4-hydroxyglutarate, DL-4-hydroxy-2-oxoglutarate

Pathway Source

Pathways

KEGG

Glyoxylate and dicarboxylate metabolism

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Roles as Enzyme Ligand

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

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EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.1.3.16

4-hydroxy-2-oxoglutarate = ?

2159, 5238

4.1.3.16

4-Hydroxy-2-oxoglutarate = Pyruvate + glyoxylate

748294, 728378, 747772, 746867, 746641

4.1.3.16

2 entries

4.1.3.42

4-hydroxy-2-oxoglutarate = ?

4971, 5256, 5242, 4984

In Vivo Product in Enzyme-catalyzed Reactions (1 result)

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EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.6.1.23

4-hydroxy-L-glutamate + oxo acid = 4-hydroxy-2-oxoglutarate + L-glutamate

639934, 639935

Substrate in Enzyme-catalyzed Reactions (9 results)

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EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.6.1.14

L-asparagine + 4-hydroxy-2-oxoglutarate = 2-oxosuccinamate + 2-amino-4-hydroxyglutarate

637254

4.1.3.16

4-hydroxy-2-oxoglutarate = ?

2159, 5238

4.1.3.16

4-Hydroxy-2-oxoglutarate = Pyruvate + glyoxylate

748294, 5237, 5238, 728378, 747772, 721727, 723542, 746867, 746641, 2159, 5241

4.1.3.17

2-hydroxy-4-oxopentanedioic acid = ?

715556

4.1.3.17

4-Hydroxy-2-oxoglutarate = Pyruvate + glyoxylate

33192, 33193

4.1.3.17

DL-4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate

650628

4.1.3.42

4-hydroxy-2-oxoglutarate = ?

4971, 5256, 5242, 4984

4.1.3.42

4-Hydroxy-2-oxoglutarate = Pyruvate + glyoxylate

5242, 5245, 5248

4.1.3.42

D,L-4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate + D-4-hydroxy-2-oxoglutarate

Product in Enzyme-catalyzed Reactions (6 results)

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EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.6.1.23

4-hydroxy-L-glutamate + 2-oxoglutarate = 4-hydroxy-2-oxoglutarate + L-glutamate

639935, 639934

2.6.1.23

4-hydroxy-L-glutamate + oxaloacetate = 4-hydroxy-2-oxoglutarate + L-aspartate

2.6.1.23

4-hydroxy-L-glutamate + oxo acid = 4-hydroxy-2-oxoglutarate + L-glutamate

Glyoxylate + pyruvate = 4-Hydroxy-2-ketoglutarate

5237, 0

4.1.3.17

pyruvate + glyoxylate = 4-hydroxy-2-oxoglutarate

33193

4.1.3.42

Glyoxylate + pyruvate = 4-Hydroxy-2-ketoglutarate

Inhibitor in Enzyme-catalyzed Reactions (2 results)

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EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

4.1.3.16

substrate inhibition, Ki: 35 mM

5253

4.2.1.3

competitive

33784

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (13 results)

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EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

4.1.3.16

0.8

mutant S77T, pH 8.5, 37°C

723542

4.1.3.16

1.2

mutant S77V, pH 8.5, 37°C

723542

4.1.3.16

2.4

mutant S198A, pH 8.5, 37°C

723542

4.1.3.16

2.5

mutant S77A, pH 8.5, 37°C

723542

4.1.3.16

mutant N78T, pH 8.5, 37°C

723542

4.1.3.16

5.2

mutant Y140F, pH 8.5, 37°C

723542

4.1.3.16

6.1

wild-type, pH 8.5, 37°C

723542

4.1.3.16

6.2

mutant N78Q, pH 8.5, 37°C

723542

4.1.3.16

7.6

mutant N78A, pH 8.5, 37°C

723542

4.1.3.16

7.8

mutant S198T, pH 8.5, 37°C

13.5

0.058

wild type protein, 1.0 mM Mg2+, pH 8.0, 25°C

715556

4.1.3.17

0.25

wild type protein, 1.0 mM Mn2+, pH 8.0, 25°C

K_M Value (16 results)

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EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

4.1.3.16

0.008

mutant Y140F, pH 8.5, 37°C

723542

4.1.3.16

0.011

wild-type, pH 8.5, 37°C

723542

4.1.3.16

0.016

mutant N78T, pH 8.5, 37°C

723542

4.1.3.16

0.044

mutant S198A, pH 8.5, 37°C

723542

4.1.3.16

0.058

mutant S77T, pH 8.5, 37°C

723542

4.1.3.16

0.066

mutant N78A, pH 8.5, 37°C

723542

4.1.3.16

0.077

mutant S198T, pH 8.5, 37°C

723542

4.1.3.16

0.082

mutant S77V, pH 8.5, 37°C

723542

4.1.3.16

0.084

mutant S77A, pH 8.5, 37°C

0.1

0.281

mutant N78Q, pH 8.5, 37°C

1.33

0.071

wild type protein, 1.0 mM Mn2+, pH 8.0, 25°C

715556

4.1.3.17

0.15

wild type protein, 1.0 mM Mg2+, pH 8.0, 25°C

715556

4.1.3.17

0.24

pH 8.0, 25°C

0.039

K_i Value (1 result)

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EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

4.1.3.16

substrate inhibition

5253

References & Links

Literature References (27)

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Show Reference (27 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

2159

Enzymes and intermediates of hydroxyproline degradation

1971

Adams, E.

Methods Enzymol.

17B

266-306

4971

2-Keto-3-deoxy-6-phosphogluconic and related aldolases

1972

Wood, W.A.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

281-302

4984

8166720

Purification and characterization of 2-keto-3-deoxy-6-phosphogluconate aldolase from Azotobacter vinelandii: evidence that the enzyme is bifunctional towards 2-keto-4-hydroxyglutarate cleavage

1994

Taha, T.S.; Deits, T.L.

Biochem. Biophys. Res. Commun.

200

459-466

5237

14089442

The metabolism of gamma-hydroxyglutamate in rat liver. 1. Enzymic synthesis of gamma-hydroxy-alpha-ketoglutarate from pyruvate and glyoxylate

1963

Kuratomi, K.; Fukunaga, K.

Biochim. Biophys. Acta

617-628

5238

5580656

2-keto-4-Hydroxybutyrate aldolase. Identification as 2-keto-4-hydroxyglutarate aldolase, catalytic properties, and role in mammalian metabolism of L-homoserine

1971

Lane, R.S.; Shapley, A.; Dekker, E.E.

Biochemistry

1353-1364

5241

5168885

Variant properties of bovine liver 2-keto-4-hydroxyglutarate aldolase: its beta-decarboxylase activity, lack of substrate stereospecificity, and structural requirements for binding substrate analogs

1971

Kobes, R.D.; Dekker, E.E.

Biochim. Biophys. Acta

251

238-250

5242

4560498

Purification, substrate specificity and binding, beta-decarboxylase activity, and other properties of Escherichia coli 2-keto-4-hydroxyglutarate aldolase

1972

Nishihara, H.; Dekker, E.E.

J. Biol. Chem.

247

5079-5087

5245

1098660

Enzyme stereoselectivity: the reversible reaction catalyzed by 2-keto-4-hydroxyglutarate aldolase of Escherichia coli

1975

Meloche, H.P.; Monti, C.T.; Dekker, E.E.

Biochem. Biophys. Res. Commun.

1033-1039

5248

Aldol-type reactions and 2-keto-4-hydroxyglutarate aldolase

1977

Dekker, E.E.

Bioorg. Chem.

59-77

5253

3966804

Rat liver 4-hydroxy-2-ketoglutarate aldolase: purification and kinetic characterization

1985

Anderson, M.; Scholtz, J.M.; Schuster, S.M.

Arch. Biochem. Biophys.

236

82-97

5256

8524853

Recovery of respiration following thew SOS-response of Escherichia coli requires RecA-mediated induction of 2-keto-4-hydroxyglutarate aldolase

1995

Cayrol, C.; Petit, C.; Raynaud, B.; Capdevielle, J.; Guillemot, J.C.; Defais, M.

Proc. Natl. Acad. Sci. USA

11806-11809

33192

2229033

Activation of Pseudomonas ochraceae 4-hydroxy-4-methyl-2-oxoglutarate aldolase by inorganic phosphate

1990

Maruyama, K.

J. Biochem.

334-340

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

33784

Aconitase

1971

Pickworth Glusker, J.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

413-439

637254

3099645

Kinetic properties and characteristics of mouse liver mitochondrial asparagine aminotransferase

1986

Maul, D.M.; Schuster, S.M.

Arch. Biochem. Biophys.

251

585-593

639934

13948827

Metabolism of gamma-hydroxyglutamic acid. I. Conversion to alpha-hydroxy-gamma-ketoglutarate by purified glutamic-aspartic transaminase of rat liver

1962

Goldstone, A.; Adams, E.

J. Biol. Chem.

237

3476-3485

639935

14089443

The metabolism of gamma hydroxyglutamate in rat liver. II. A transaminase concerned in gamma-hydroxyglutamate metabolism

1963

Kuratomi, K.; Fukunaga, K.; Kobayashi, Y.

Biochim. Biophys. Acta

629-636

650628

11826967

Cloning, sequencing, and expression of the gene encoding 4-hydroxy-4-methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae NGJ1

2001

Maruyama, K.; Miwa, M.; Tsujii, N.; Nagai, T.; Tomita, N.; Harada, T.; Sobajima, H.; Sugisaki, H.

Biosci. Biotechnol. Biochem.

2701-2709

715556

20843800

Structural and kinetic characterization of 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolase, a protocatechuate degradation enzyme evolutionarily convergent with the HpaI and DmpG pyruvate aldolases

2010

Wang, W.; Mazurkewich, S.; Kimber, M.S.; Seah, S.Y.

J. Biol. Chem.

285

36608-36615

721727

22771891

4-Hydroxy-2-oxoglutarate aldolase inactivity in primary hyperoxaluria type 3 and glyoxylate reductase inhibition

2012

Riedel, T.J.; Knight, J.; Murray, M.S.; Milliner, D.S.; Holmes, R.P.; Lowther, W.T.

Biochim. Biophys. Acta

1822