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Ligand 3-hydroxy-3-methyl-2-oxobutanoic acid

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

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

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.86

2-acetolactate + NADPH + H+ = 3-hydroxy-3-methyl-2-oxobutyrate + NADP+

0

-

Substrate in Enzyme-catalyzed Reactions (6 results)

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Show Substrate (6 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.169

2-keto-3-hydroxyisovalerate + NADPH = ? + NADP+

286103

-

1.1.1.86

NADPH + 2-oxo-3-hydroxyisovalerate = NADP+ + alpha,beta-dihydroxyisovalerate

639169

-

1.1.1.86

3-hydroxy-3-methyl-2-ketobutyrate + NADP+ = ?

655530

-

1.1.1.86

3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+ = 2,3-dihydroxy-3-methyl-butanoate + NADP+

738989

-

1.1.1.86

3-hydroxy-3-methyl-2-oxobutanoate + NADPH + H+ = 2,3-dihydroxy-3-methylbutanoate + NADP+

738989

-

1.1.1.86

NADP+ + 3-hydroxy-3-methyl-2-oxobutanoate = NADPH + acetolactate

639177

-

1.1.1.86

5 entries

Product in Enzyme-catalyzed Reactions (5 results)

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Show Product (5 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.86

(2S)-2-acetolactate + NADPH + H+ = 3-hydroxy-3-methyl-2-oxobutyrate + NADP+

0

-

1.1.1.86

2-acetolactate + NADPH + H+ = 3-hydroxy-3-methyl-2-oxobutyrate + NADP+

0

-

1.1.1.86

2-acetolactate + NADPH = 3-hydroxy-3-methyl-2-oxobutyrate + NADP+

0

-

1.1.1.86

NADPH + 2-acetolactate = NADP+ + 3-hydroxy-3-methyl-2-oxobutyrate

0, 639175

-

1.1.1.86

4 entries

5.4.99.3

2-Acetolactate = 3-Hydroxy-3-methyl-2-oxobutanoate

3520

-

Inhibitor in Enzyme-catalyzed Reactions (2 results)

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Show Inhibitors (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.86

0.001 mM, 58% inhibition

639169

-

1.1.1.86

-

670482

-

1.1.1.86

2 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (12 results)

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Show Turnover Number (12 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.86

0.3

-

pH 8.0 25°C

738989

1.1.1.86

0.4

-

pH 8.0 25°C

738989

1.1.1.86

0.5

-

pH 8.0 25°C

738989

1.1.1.86

0.8

-

pH 8.0 25°C

738989

1.1.1.86

0.9

-

pH 8.0 25°C

738989

1.1.1.86

1.2

-

pH 8.0 25°C

738989

1.1.1.86

2.2

-

pH 8.0 25°C

738989

1.1.1.86

2.5

-

pH 8.0 25°C

738989

1.1.1.86

2.8

-

pH 8.0 25°C

738989

1.1.1.86

3.1

-

pH 8.0 25°C

738989

1.1.1.86

3.511

-

pH 8.0, 37°C

655530

1.1.1.86

5.2

-

pH 8.0 25°C

738989

1.1.1.86

12 entries

K_M Value (11 results)

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Show KM Value (11 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.169

8.55

-

-

286103

1.1.1.86

0.26

-

pH 8.0 25°C

738989

1.1.1.86

0.27

-

pH 8.0, 37°C, wild-type enzyme

655530

1.1.1.86

2.3

-

pH 8.0 25°C

738989

1.1.1.86

3

-

pH 8.0 25°C

738989

1.1.1.86

4

-

pH 8.0 25°C

738989

1.1.1.86

5

-

pH 8.0 25°C

738989

1.1.1.86

8

-

pH 8.0 25°C

738989

1.1.1.86

8.6

-

pH 8.0 25°C

738989

1.1.1.86

10

-

pH 8.0 25°C

738989

1.1.1.86

13

-

pH 8.0 25°C

738989

1.1.1.86

10 entries

References & Links

Literature References (8)

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Show Reference (8 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

3520

4384955

Biosynthesis of isoleucine and valine in Mycobacterium tuberculosis H37 Rv

1968

Allaudeen, H.S.; Ramakrishnan, T.

Arch. Biochem. Biophys.

125

199-209

286103

3042788

Ketopantoic acid reductase of Pseudomonas maltophilia 845. Purification, characterization, and role in pantothenate biosynthesis

1988

Shimizu, S.; Kataoka, M.; Ching-Ming Chung, M.; Yamada, H.

J. Biol. Chem.

263

12077-12084

639169

4388025

Purification and properties of the acetohydroxy acid isomeroreductase of Salmonella typhimurium

1969

Arfin, S.M.; Umbarger, H.E.

J. Biol. Chem.

244

1118-1127

639175

2653423

Mechanism of ketol acid reductoisomerase--steady-state analysis and metal ion requirement

1989

Chunduru, S.K.; Mrachko, G.T.; Calvo, K.C.

Biochemistry

28

486-493

639177

2189496

Oxalyl hydroxamates as reaction-intermediate analogues for ketol-acid reductoisomerase

1990

Aulabaugh, A.; Schloss, J.V.

Biochemistry

29

2824-2830

655530

15654896

Probing the mechanism of the bifunctional enzyme ketol-acid reductoisomerase by site-directed mutagenesis of the active site

2005

Tyagi, R.; Lee, Y.T.; Guddat, L.W.; Duggleby, R.G.

FEBS J.

272

593-602

670482

15751008

Synthesis, crystal structure and herbicidal activity of mimics of intermediates of the KARI reaction

2005

Wang, B.L.; Duggleby, R.G.; Li, Z.M.; Wang, J.G.; Li, Y.H.; Wang, S.H.; Song, H.B.

Pest Manag. Sci.

61

407-412

738989

25296650

Molecular annotation of ketol-acid reductoisomerases from Streptomyces reveals a novel amino acid biosynthesis interlock mediated by enzyme promiscuity

2015

Verdel-Aranda, K.; Lopez-Cortina, S.T.; Hodgson, D.A.; Barona-Gomez, F.

Microb. Biotechnol.

8

239-252

Links to other databases for 3-hydroxy-3-methyl-2-oxobutanoic acid

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Show Links (1 entry)

ChEBI

PubChem