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Ligand 2-hydroxypentanoic acid

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

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

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.15

DL-2-hydroxyvalerate + O2 = 2-oxovalerate + H2O2

389685, 389691, 389693, 389698, 389700, 389699, 389675

-

Substrate in Enzyme-catalyzed Reactions (13 results)

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Show Substrate (13 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.337

2-hydroxyvalerate + NAD+ = 2-oxovalerate + NADH + H+

726750

-

1.1.1.345

2-hydroxypentanoate + NAD+ = 2-oxopentanoate + NADH + H+

731727

-

1.1.3.15

2-hydroxyvalerate + O2 = ?

440423

-

1.1.3.15

DL-2-hydroxyvalerate + 2,6-dichlorophenolindophenol = 2-oxovalerate + reduced 2,6-dichlorophenolindophenol

389701

-

1.1.3.15

DL-2-hydroxyvalerate + O2 = 2-oxovalerate + H2O2

389685, 389691, 389693, 389698, 389700, 389699, 389675

-

1.1.3.15

3 entries

1.1.3.2

2-hydroxypentanoate + O2 = 2-oxopentanoate + H2O2

745260

-

1.1.99.2

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

389902

-

1.1.99.31

(R,S)-2-hydroxyvalerate + acceptor = 2-oxovalerate + reduced acceptor

678122

-

1.1.99.31

2-hydroxyvalerate + acceptor = 2-oxovalerate + reduced acceptor

667565, 667577

-

1.1.99.31

2 entries

1.13.12.4

2-hydroxyvalerate + O2 = ?

440413

-

1.4.3.2

alpha-hydroxyvaleric acid + H2O + O2 = 2-oxopentanoic acid + NH3 + H2O2

391802

-

2.8.3.9

DL-2-hydroxypentanoate + acetoacetyl-CoA = 2-hydroxypentanoyl-CoA + acetoacetate

643838

-

6.3.2.4

ATP + D-Ala + 2-hydroxypentanoate = ADP + phosphate + D-Ala-D-2-hydroxypentanoate

1249

-

Product in Enzyme-catalyzed Reactions (12 results)

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Show Product (12 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

2-oxopentanoate + NADH + H+ = 2-hydroxypentanoate + NAD+

0

-

1.1.1.169

2-oxoisovalerate + NADPH = 2-hydroxyvalerate + NADP+

0

-

1.1.1.27

2-oxopentanoate + NADH = 2-hydroxypentanoate + NAD+

0

-

1.1.1.27

2-oxovalerate + NADH + H+ = 2-hydroxyvalerate + NAD+

0

-

1.1.1.27

2-oxovalerate + NADH = 2-hydroxyvalerate + NAD+

0

-

1.1.1.28

2-ketovalerate + NADH = 2-hydroxyvalerate + NAD+

0

-

1.1.1.28

2-oxovalerate + NADH + H+ = 2-hydroxyvalerate + NAD+

0

-

1.1.1.27

3 entries

1.1.1.28

2 entries

1.1.1.337

2-oxovalerate + NADH + H+ = 2-hydroxyvalerate + NAD+

0

-

1.1.1.345

2-oxopentanoate + NADH + H+ = 2-hydroxypentanoate + NAD+

0

-

1.1.3.4

1,2-pentanediol + O2 = 2-hydroxypentanoate + H2O2

0

-

1.1.3.41

1,2-pentanediol + O2 = 2-hydroxypentanoic acid + H2O2

0

-

1.14.11.17

valeric acid + 2-oxoglutarate + O2 = 2-hydroxyvaleric acid + succinate + CO2

0

-

Inhibitor in Enzyme-catalyzed Reactions (2 results)

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Show Inhibitors (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.379

10 mM, 67.4% inhibition

730341

-

1.1.3.15

marked inhibition above 50 mM

389693

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (6 results)

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Show Turnover Number (6 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.345

24

-

pH 7.0, temperature not specified in the publication

731727

1.1.3.2

1.25

-

wild-type, pH 7.0, 25°C

745260

1.1.3.2

51.7

-

mutant A95G, pH 7.0, 25°C

745260

1.1.99.31

0.27

-

pH 7.5, 20°C, mutant enzyme G81A

667577

1.1.99.31

0.36

-

pH 7.5, 20°C, wild-type enzyme

667577

1.1.99.31

0.5

-

pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach

667565

1.1.3.2

2 entries

1.1.99.31

3 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

1.1.1.337

1.8

-

pH 8.0, 30°C

726750

1.1.1.345

3.3

-

pH 7.0, temperature not specified in the publication

731727

1.1.3.15

0.25

-

pH 7.5

389685

1.1.3.15

0.35

-

pH 7.0

389685

1.1.3.15

0.6

-

-

389693

1.1.3.15

5.5

-

-

440423

1.1.3.15

10

-

A95G mutant

440423

1.1.3.15

13

-

-

389691

1.1.3.2

5.5

-

wild-type, pH 7.0, 25°C

745260

1.1.3.2

10

-

mutant A95G, pH 7.0, 25°C

745260

1.1.99.31

3.2

-

pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach

667565

1.1.99.31

6.4

-

pH 7.5, 20°C, mutant enzyme G81A

667577

1.1.99.31

15.3

-

in 0.1 M potassium phosphate buffer, pH 7.5 at 20°C

678122

1.1.99.31

15.3

-

pH 7.5, 20°C, wild-type enzyme

667577

1.1.3.15

6 entries

1.1.3.2

2 entries

1.1.99.31

4 entries

2.8.3.9

21

-

pH 7.5, 25°C

643838

6.3.2.4

8.3

-

-

1249

References & Links

Literature References (21)

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Show Reference (21 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

1249

7957913

Purification and characterization of the VanB ligase associated with type B vancomycin resistance in Enterococcus faecalis V583

1994

Meziane-Cherif, D.; Badet-Denisot, M.A.; Evers, S.; Courvalin, P.; Badet, B.

FEBS Lett.

354

140-142

389675

11038060

A novel glycolate oxidase requiring flavin mononucleotide as the cofactor in the Prasinophycean alga Mesostigma viride

2000

Iwamoto, K.; Ikawa, T.

Plant Cell Physiol.

41

988-991

389685

3061453

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

1988

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

Biochemistry

27

7365-7371

389691

1148170

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

1975

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

Biochemistry

14

2588-2596

389693

4750770

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

1973

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

Biochim. Biophys. Acta

321

54-63

389698

5686300

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

1968

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

Biochim. Biophys. Acta

167

9-22

389699

5972358

Oxidation of L-alpha-hydroxy acids by Tetrahymena pyriformis

1966

Eichel, H.J.

Biochim. Biophys. Acta

128

183-186

389700

5946631

Crystalline mammalian L-amino acid oxidase from rat kidney mitochondria

1966

Nakano, M.; Danowski, T.S.

J. Biol. Chem.

241

2075-2083

389701

14492912

L-alpha-Hydroxy acid oxidases of hog renal cortex

1962

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

J. Biol. Chem.

237

2001-2010

389902

-

Purification and characterization of a-hydroxyglutarate dehydrogenase from Alcaligenes sp.

1985

Suzuki, T.; Uozomi, T.; Beppu, T.

Agric. Biol. Chem.

49

2939-2947

391802

4962138

Crystalline L-amino-acid oxidase from the soluble fraction of rat-kidney cells

1967

Nakano, M.; Tsutsumi, Y.; Danowski, T.S.

Biochim. Biophys. Acta

139

40-48

440413

-

Lactate oxygenase of Mycobacterium phlei

1975

Takemori, S.; Katagiri, M.

Methods Enzymol.

41B

329-333

440423

8910450

Conversion of L-lactate oxidase to a long chain alpha-hydroxyacid oxidase by site-directed mutagenesis of alanine 95 to glycine

1996

Yorita, K.; Aki, K.; Ohkuma-Soyejima, T.; Kokubo, T.; Misaki, H.; Massey, V.

J. Biol. Chem.

271

28300-28305

643838

624727

Butyryl-CoA:acetoacetate CoA-transferase from a lysine-fermenting Clostridium

1978

Barker, H.A.; Jemg, I.M.; Neff, N.; Robertson, J.M.; Tam, F.K.; Hosaka, S.

J. Biol. Chem.

253

1219-1225

667565

10493804

A highly active, soluble mutant of the membrane-associated (S)-mandelate dehydrogenase from Pseudomonas putida

1999

Xu, Y.; Mitra, B.

Biochemistry

38

12367-12376

667577

15311930

Role of glycine 81 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate specificity and oxidase activity

2004

Dewanti, A.R.; Xu, Y.; Mitra, B.

Biochemistry

43

10692-10700

678122

10231535

(S)-Mandelate dehydrogenase from Pseudomonas putida: mechanistic studies with alternate substrates and pH and kinetic isotope effects

1999

Lehoux, I.E.; Mitra, B.

Biochemistry

38

5836-5848

726750

-

L-2-Hydroxyisocaproate dehydrogenase - A new enzyme from Lactobacillus confusus for the stereospecific reduction of 2-ketocarboxylic acids

1984

Schütte, W.; Hummel, W.; Kula, M.R.

Appl. Microbiol. Biotechnol.

19

167-176

730341

-

Purification and characterization of D(-)-mandelate dehydrogenase from Rhodotorula graminis

1989

Baker, D.P.; Fewson, C.A.

Microbiology

135

2035-2044

731727

-

Potential of R-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei for stereospecific reductions

1992

Kallwass, H.K.W.

Enzyme Microb. Technol.

14

28-35

745260

8910450

Conversion of L-lactate oxidase to a long chain alpha-hydroxyacid oxidase by site-directed mutagenesis of alanine 95 to glycine

1996

Yorita, K.; Aki, K.; Ohkuma-Soyejima, T.; Kokubo, T.; Misaki, H.; Massey, V.

J. Biol. Chem.

271

28300-28305

Links to other databases for 2-hydroxypentanoic acid

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ChEBI

PubChem