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Ligand 2-Hydroxy-3-butynoate

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Substrate (4 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.15

DL-2-hydroxy-3-butynoate + O2 = 2-oxo-3-butynoate + H2O2

389692

-

1.1.99.31

2-hydroxy-3-butynoate + acceptor = 2-oxo-3-butynoate + reduced acceptor

667565, 667577, 678122

-

1.13.12.4

2-hydroxy-3-butynoate + O2 = ?

440412

-

1.13.12.4

DL-2-hydroxy-3-butynoate + O2 = ?

440412, 440421

-

1.13.12.4

2 entries

Product in Enzyme-catalyzed Reactions (2 results)

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Show Product (2 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.15

DL-2-hydroxy-3-butynoate + O2 = 2-oxo-3-butynoate + H2O2

389692

-

1.1.99.31

2-hydroxy-3-butynoate + acceptor = 2-oxo-3-butynoate + reduced acceptor

0

-

Inhibitor in Enzyme-catalyzed Reactions (6 results)

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Show Inhibitors (6 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.15

inhibition of transhydrogenation reaction

389685

-

1.1.3.15

irreversible inactivation after 25 turnovers, covalent addition to the coenzyme

389692

-

1.1.3.15

2 entries

1.1.5.12

inactivation

740643

-

1.1.99.31

irreversible inactivation

678122

-

1.13.12.4

irreversible inactivator due to a covalent modification of the bound FMN

440412, 440421

-

1.13.12.4

suicide substrate

440397

-

1.13.12.4

2 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (3 results)

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Show Turnover Number (3 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.99.31

3.9

-

pH 7.5, 20°C, wild-type enzyme

667577

1.1.99.31

6.6

-

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

14.8

-

pH 7.5, 20°C, mutant enzyme G81A

667577

1.1.99.31

3 entries

K_M Value (7 results)

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Show KM Value (7 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.3.15

4

-

-

389692

1.1.99.31

4.3

-

pH 7.5, 20°C, mutant enzyme G81A

667577

1.1.99.31

17.2

-

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

22

-

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

678122

1.1.99.31

22

-

pH 7.5, 20°C, wild-type enzyme

667577

1.13.12.4

1.41

-

-

440412

1.13.12.4

2

-

-

440421

1.1.99.31

4 entries

1.13.12.4

2 entries

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.99.31

36

-

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

678122

References & Links

Literature References (9)

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Show Reference (9 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

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

389692

1148211

Mechanistic studies on the rat kidney flavoenzyme L-alpha-hydroxy acid oxidase

1975

Cromartie, T.H.; Walsh, C.

Biochemistry

14

3482-3490

440397

8663383

Site-directed mutagenesis of glycine 99 to alanine in L-lactate monooxygenase from Mycobacterium smegmatis

1996

Sun, W.; Williams, C.H., Jr.; Massey, V.

J. Biol. Chem.

271

17226-17233

440412

1268195

Kinetic studies on the inactivation of L-lactate oxidase by [the acetylenic suicide substrate] 2-hydroxy-3-butynoate

1976

Ghisla, S.; Ogata, H.; Massey, V.; Schonbrunn, A.; Abeles, R.H.; Walsh, C.T.

Biochemistry

15

1791-1797

440421

5057095

Inactivation of a flavoprotein, lactate oxidase, by an acetylenic substrate

1972

Walsh, C.T.; Schonbrunn, A.; Lockridge, O.; Massey, V.; Abeles, R.H.

J. Biol. Chem.

247

6004-6006

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

740643

4582730

Mechanisms of active transport in isolated bacterial membrane vesicles

1973

Kohn, L.; Kaback, H.

J. Biol. Chem.

248

7012-7017

Links to other databases for 2-Hydroxy-3-butynoate

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Show Links (1 entry)

ChEBI

PubChem

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