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Ligand 2,5-dioxopentanoate

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

d-xylose degradation, degradation of pentoses

KEGG

Ascorbate and aldarate metabolism, D-Amino acid metabolism, Pentose and glucuronate interconversions

MetaCyc

D-arabinose degradation III, D-galactarate degradation II, D-galacturonate degradation II, D-glucarate degradation II, D-glucuronate degradation II, D-xylose degradation III, D-xylose degradation V, L-arabinose degradation III, L-lyxonate degradation, trans-4-hydroxy-L-proline degradation II more

Show all BRENDA pathways known for 2,5-dioxopentanoate

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (6 results)

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Show Natural Substrate (6 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.16

2-oxoglutarate semialdehyde + NAD+ + H2O = 2-oxoglutarate + NADH + H+

722211

-

1.2.1.16

2-oxoglutarate semialdehyde + NADP+ + H2O = 2-oxoglutarate + NADPH + H+

722211

-

1.2.1.26

2,5-dioxopentanoate + NAD(P)+ + H2O = 2-oxoglutarate + NAD(P)H

33852, 5607, 288177

-

1.2.1.26

2,5-dioxopentanoate + NADP+ + H2O = 2-oxoglutarate + NADPH + 2 H+

719837

-

1.2.1.26

2-oxoglutaric semialdehyde + NAD(P)+ + H2O = 2-oxoglutarate + NAD(P)H + H+

763713

-

1.2.1.26

2-oxoglutaric semialdehyde + NAD+ + H2O = 2-oxoglutarate + NADH + H+

763717

-

1.2.1.16

2 entries

1.2.1.26

4 entries

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

3.5.4.22

1-pyrroline-4-hydroxy-2-carboxylate + H2O = 2,5-dioxopentanoate + NH3

0

-

3.5.4.22

L-1-pyrroline-4-hydroxy-2-carboxylate + H2O = 2,5-dioxopentanoate + NH3

0

-

3.5.4.22

2 entries

4.2.1.141

2-dehydro-3-deoxy-D-arabinonate = 2,5-dioxopentanoate + H2O

0

-

4.2.1.41

5-dehydro-4-deoxy-D-glucarate = 2,5-dioxopentanoate + H2O + CO2

0

-

Substrate in Enzyme-catalyzed Reactions (15 results)

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Show Substrate (15 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.16

2-oxoglutarate semialdehyde + NAD+ + H2O = 2-oxoglutarate + NADH + H+

722211

-

1.2.1.16

2-oxoglutarate semialdehyde + NADP+ + H2O = 2-oxoglutarate + NADPH + H+

722211

-

1.2.1.16

2 entries

1.2.1.20

2-oxoglutaric semialdehyde + NAD+ + H2O = 2-oxoglutarate + NADH

288125

-

1.2.1.24

2,5-dioxopentanoate + NAD+ + H2O = ?

722211

-

1.2.1.24

alpha-ketoglutaric semialdehyde + NAD+ + H2O = alpha-ketoglutarate + NADH

674654

-

1.2.1.24

alpha-ketoglutaric semialdehyde + NADP+ + H2O = alpha-ketoglutarate + NADPH

674654

-

1.2.1.26

2,5-dioxopentanoate + NAD(P)+ + H2O = 2-oxoglutarate + NAD(P)H

33852, 5607, 288177

-

1.2.1.26

2,5-dioxopentanoate + NAD+ + H2O = 2-oxoglutarate + NADH + H+

693021, 288177, 693064

-

1.2.1.26

2,5-dioxopentanoate + NADP+ + H2O = 2-oxoglutarate + NADPH + 2 H+

719837, 715548

-

1.2.1.26

2-oxoglutaric semialdehyde + NAD(P)+ + H2O = 2-oxoglutarate + NAD(P)H + H+

763713

-

1.2.1.26

2-oxoglutaric semialdehyde + NAD+ + H2O = 2-oxoglutarate + NADH + H+

763717

-

1.2.1.26

alpha-ketoglutaric semialdehyde + NAD(P)+ + H2O = alpha-ketoglutarate + NAD(P)H + H+

693021, 693064

-

1.2.1.26

alpha-ketoglutaric semialdehyde + NADP+ + H2O = alpha-ketoglutarate + NADPH + H+

693064

-

1.2.1.79

2,5-dioxopentanoate + NAD+ + H2O = ?

722211

-

1.2.1.79

2,5-dioxopentanoate + NADP+ + H2O = ?

722211

-

1.2.1.24

3 entries

1.2.1.26

7 entries

1.2.1.79

2 entries

Product in Enzyme-catalyzed Reactions (9 results)

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Show Product (9 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.5.4.22

1-pyrroline-4-hydroxy-2-carboxylate + H2O = 2,5-dioxopentanoate + NH3

0

-

3.5.4.22

D-1-pyrroline-4-hydroxy-2-carboxylate + H2O = 2,5-dioxopentanoate + NH3

0

-

3.5.4.22

L-1-pyrroline-4-hydroxy-2-carboxylate + H2O = 2,5-dioxopentanoate + NH3

0

-

3.5.4.22

3 entries

4.2.1.141

2-dehydro-3-deoxy-D-arabinonate = 2,5-dioxopentanoate + H2O

0

-

4.2.1.41

5-dehydro-4-deoxy-D-glucarate = 2,5-dioxopentanoate + CO2

0

-

4.2.1.41

5-dehydro-4-deoxy-D-glucarate = 2,5-dioxopentanoate + H2O + CO2

0, 5699, 5700, 5698

-

4.2.1.41

3-deoxy-2-dehydro-L-threo-hexarate = 2-oxoglutaric semialdehyde + CO2

0

-

4.2.1.43

2-dehydro-3-deoxy-L-arabinonate = 2,5-dioxopentanoate + H2O

0

-

4.2.1.43

L-2-keto-3-deoxyarabonate = 2-oxoglutarate semialdehyde + H2O

33849, 33850, 33851, 0

-

4.2.1.41

3 entries

4.2.1.43

2 entries

Inhibitor in Enzyme-catalyzed Reactions (1 result)

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Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.24

substrate inhibition

722211

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (16 results)

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Show Turnover Number (16 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.2.1.16

7.1

-

in 0.1 M HEPES/KOH (pH 6.5), at 70°C

722211

1.2.1.16

21.2

-

with NADP+ as cosubstrate, at pH 6.5 and 70°C

722211

1.2.1.16

27.3

-

with NAD+ as cosubstrate, at pH 6.5 and 70°C

722211

1.2.1.24

7.1

-

pH 6.5, 70°C, cofactor NAD+

722211

1.2.1.24

12.3

-

1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NADP+. 25°C

674654

1.2.1.24

51.2

-

1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NAD+. 25°C

674654

1.2.1.26

1.12

-

with NAD+ as cofactor

693021

1.2.1.26

2.75

-

with NADP+ as cofactor

693021

1.2.1.26

8.6

-

pH 7.5, 70°C

719837

1.2.1.26

15.4

-

with NADP+ as cofactor

693021

1.2.1.26

21.3

-

with NAD+ as cofactor

693021

1.2.1.26

23

-

with NADP+ as cofactor

693021

1.2.1.26

53.9

-

with NAD+ as cofactor

693021

1.2.1.26

197

-

-

693064

1.2.1.79

21.2

-

pH 6.5, 70°C, cofactor NADP+

722211

1.2.1.79

27.3

-

pH 6.5, 70°C, cofactor NAD+

722211

1.2.1.16

3 entries

1.2.1.24

3 entries

1.2.1.26

8 entries

1.2.1.79

2 entries

K_M Value (16 results)

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Show KM Value (16 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.2.1.16

0.1

-

with NAD+ as cosubstrate, at pH 6.5 and 70°C

722211

1.2.1.16

0.2

-

with NADP+ as cosubstrate, at pH 6.5 and 70°C

722211

1.2.1.16

0.3

-

in 0.1 M HEPES/KOH (pH 6.5), at 70°C

722211

1.2.1.24

0.011

-

1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NAD+. 25°C

674654

1.2.1.24

0.0159

-

1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NADP+. 25°C

674654

1.2.1.24

0.3

-

pH 6.5, 70°C, cofactor NAD+

722211

1.2.1.26

0.0065

-

with NAD+ as cofactor

693021

1.2.1.26

0.0075

-

with NADP+ as cofactor

693021

1.2.1.26

0.011

-

with NADP+ as cofactor

693021

1.2.1.26

0.014

-

-

693064

1.2.1.26

0.0246

-

with NAD+ as cofactor

693021

1.2.1.26

0.05

0.1

-

288177

1.2.1.26

0.094

-

with NADP+ as cofactor

693021

1.2.1.26

0.5569

-

with NAD+ as cofactor

693021

1.2.1.79

0.1

-

pH 6.5, 70°C, cofactor NAD+

722211

1.2.1.79

0.2

-

pH 6.5, 70°C, cofactor NADP+

722211

1.2.1.16

3 entries

1.2.1.24

3 entries

1.2.1.26

8 entries

1.2.1.79

2 entries

References & Links

Literature References (18)

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Show Reference (18 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

5607

-

Regulation of L-arabinose metabolism in Pseudomonas fluorescens

1975

Schimz, K.L.; Kurz, G.

Biochem. Soc. Trans.

3

1087-1089

5698

237186

D-4-Deoxy-5-ketoglucarate hydro-lyase (decarboxylating)

1975

Dagley, S.; Jeffcoat, R.

Methods Enzymol.

42C

272-276

5699

1156361

Studies on the subunit structure of 4-deoxy-5-oxoglucarate hydro-lyase (decarboxylating) from Pseudomonas acidovorans

1975

Jeffcoat, R.

Biochem. J.

145

305-309

5700

4982840

Purification and properties of D-4-deoxy-5-oxoglucarate hydro-lyase (decarboxylating)

1969

Jeffcoat, R.; Hassall, H.; Dagley, S.

Biochem. J.

115

977-983

33849

237190

L-2-Keto-3-deoxyarabonate dehydratase

1975

Stoolmiller, A.C.

Methods Enzymol.

42C

308-315

33850

6027246

Studies on the mechanism of action of 2-keto-3-deoxy-L-arabonate dehydratase. The participation of an enzyme-substrate Schiff base in a dehydration

1967

Portsmouth, D.; Stoolmiller, A.C.; Abeles, R.H.

J. Biol. Chem.

242

2751-2759

33851

5954356

Formation of alpha-ketoglutaric semialdehyde from L-2-keto-3-deoxyarabonic acid and isolation of L-2-keto-3-deoxyarabonate dehydratase from Pseudomonas saccharophila

1966

Stoolmiller, A.C.; Abeles, R.H.

J. Biol. Chem.

241

5764-5771

33852

-

Pentose metabolism in Rhizobium leguminosarum MNF300 and in cowpea Rhizobium NGR234

1986

Dilworth, M.J.; Arwas, R.; McKay, I.A.; Saroso, S.; Glenn, A.R.

J. Gen. Microbiol.

132

2733-2742

288125

-

Factors influencing growth on L-lysine by Pseudomonas

1971

Chang, Y.F.; Adams, E.

Methods Enzymol.

17B

166-171

288177

6024771

alpha-Ketoglutaric semialdehyde dehydrogenase of Pseudomonas. Properties of the purified enzyme induced by hydroxyproline and of the glucarate-induced and constitutive enzymes

1967

Adams, E.; Rosso, G.

J. Biol. Chem.

242

1802-1814

674654

16835232

A novel alpha-ketoglutaric semialdehyde dehydrogenase: evolutionary insight into an alternative pathway of bacterial L-arabinose metabolism

2006

Watanabe, S.; Kodaki, T.; Makino, K.

J. Biol. Chem.

281

28876-28888

693021

17202142

alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, D-galactarate, and hydroxy-L-proline. Molecular and metabolic convergent evolution

2007

Watanabe, S.; Yamada, M.; Ohtsu, I.; Makino, K.

J. Biol. Chem.

282

6685-6695

693064

18364348

New Insights into the Alternative D-Glucarate Degradation Pathway

2008

Aghaie, A.; Lechaplais, C.; Sirven, P.; Tricot, S.; Besnard-Gonnet, M.; Muselet, D.; de Berardinis, V.; Kreimeyer, A.; Gyapay, G.; Salanoubat, M.; Perret, A.

J. Biol. Chem.

283

15638-15646

715548

20736170

Metabolism of pentose sugars in the hyperthermophilic archaea Sulfolobus solfataricus and Sulfolobus acidocaldarius

2010

Nunn, C.E.; Johnsen, U.; Schoenheit, P.; Fuhrer, T.; Sauer, U.; Hough, D.W.; Danson, M.J.

J. Biol. Chem.

285

33701-33709

719837

16849334

Identification of the missing links in prokaryotic pentose oxidation pathways: evidence for enzyme recruitment

2006

Brouns, S.J.; Walther, J.; Snijders, A.P.; van de Werken, H.J.; Willemen, H.L.; Worm, P.; de Vos, M.G.; Andersson, A.; Lundgren, M.; Mazon, H.F.; van den Heuvel, R.H.; Nilsson, P.; Salmon, L.; de Vos, W.M.; Wright, P.C.; Bernander, R.; van der Oost, J.

J. Biol. Chem.

281

27378-27388

722211

23296511

Unraveling the function of paralogs of the aldehyde dehydrogenase super family from Sulfolobus solfataricus

2013

Esser, D.; Kouril, T.; Talfournier, F.; Polkowska, J.; Schrader, T.; Bräsen, C.; Siebers, B.

Extremophiles

17

205-216

763713

29214999

Engineering an aldehyde dehydrogenase toward its substrates, 3-hydroxypropanal and NAD+, for enhancing the production of 3-hydroxypropionic acid

2017

Park, Y.S.; Choi, U.J.; Nam, N.H.; Choi, S.J.; Nasir, A.; Lee, S.G.; Kim, K.J.; Jung, G.Y.; Choi, S.; Shim, J.Y.; Park, S.; Yoo, T.H.

Sci. Rep.

7

17155

763717

28393833

Structural insights into the production of 3-hydroxypropionic acid by aldehyde dehydrogenase from Azospirillum brasilense

2017

Son, H.F.; Park, S.; Yoo, T.H.; Jung, G.Y.; Kim, K.J.

Sci. Rep.

7

46005

Links to other databases for 2,5-dioxopentanoate

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Show Links (1 entry)

ChEBI

PubChem