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Ligand 2-methyl-3-oxopropanoic acid

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for 2-methyl-3-oxopropanoic acid

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.27

2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH

722211, 743075

-

1.2.1.27

2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH + H+

762976

-

1.2.1.27

2-methyl-3-oxopropanoate + CoA + NAD+ = propanoyl-CoA + CO2 + NADH

654105, 288055, 390218, 390219, 390220, 656987

-

1.2.1.27

methylmalonate-semialdehyde + CoA + NAD+ = propionyl-CoA + NADH + H+ + HCO3-

710894

-

1.2.1.27

4 entries

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

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Show Natural Product (6 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.31

(S)-3-hydroxyisobutyrate + NAD+ = 2-methyl-3-oxopropanoate + NADH + H+

0

-

1.1.1.31

3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH + H+

0

-

1.1.1.31

3-hydroxy-2-methylpropanoate + NADP+ = 2-methyl-3-oxopropanoate + NADPH + H+

0

-

1.1.1.31

D,L-3-hydroxyisobutyrate + NAD+ = 2-methyl-3-oxopropionate + NADH

0

-

1.1.1.31

4 entries

2.6.1.22

(S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate

0

-

2.6.1.40

(R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-oxopropanoate + L-alanine

644428

-

Substrate in Enzyme-catalyzed Reactions (6 results)

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Show Substrate (6 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.18

2-methyl-3-oxopropanoate + CoA + NAD+ = propanoyl-CoA + CO2 + NADH

288055

-

1.2.1.27

2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH

722211, 743075

-

1.2.1.27

2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH + H+

762976

-

1.2.1.27

2-methyl-3-oxopropanoate + CoA + NAD+ = propanoyl-CoA + CO2 + NADH

654105, 671852, 288055, 390223, 390218, 390219, 390220, 656987

-

1.2.1.27

methylmalonate semialdehyde + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH

725429, 725642, 722211, 725485

-

1.2.1.27

methylmalonate-semialdehyde + CoA + NAD+ = propionyl-CoA + NADH + H+ + HCO3-

710894

-

1.2.1.27

5 entries

Product in Enzyme-catalyzed Reactions (31 results)

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Show Product (31 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.276

D-3-hydroxyisobutyrate + NADP+ = 2-methyl-3-oxopropanoic acid + NADPH

0

-

1.1.1.276

L-3-hydroxyisobutyrate + NADP+ = 2-methyl-3-oxopropanoic acid + NADPH

0

-

1.1.1.31

(R)-3-hydroxyisobutyrate + NAD+ = 2-methyl-3-oxopropanoate + NADH + H+

0

-

1.1.1.31

(S)-3-hydroxyisobutyrate + NAD+ = 2-methyl-3-oxopropanoate + NADH + H+

0

-

1.1.1.31

(S)-3-hydroxyisobutyrate + NADP+ = 2-methyl-3-oxopropanoate + NADPH + H+

0

-

1.1.1.31

(S)-beta-hydroxyisobutyrate + NADP+ = 2-methyl-3-oxopropanoate + NADPH + H+

0

-

1.1.1.31

3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH + H+

0

-

1.1.1.31

3-hydroxy-2-methylpropanoate + NADP+ = 2-methyl-3-oxopropanoate + NADPH + H+

0

-

1.1.1.31

D,L-3-hydroxyisobutyrate + NAD+ = 2-methyl-3-oxopropionate + NADH

0

-

1.1.1.31

L-3-hydroxyisobutyrate + NAD+ = 3-oxoisobutyrate + NADH

0

-

1.1.1.31

(R)-3-hydroxyisobutyrate + NAD+ = methylmalonate semialdehyde + NADH + H+

0

-

1.1.1.31

(S)-3-hydroxyisobutyrate + NAD+ = methylmalonate semialdehyde + NADH + H+

0

-

1.1.1.31

3-hydroxyisobutyrate + NAD+ = methylmalonate semialdehyde + NADH + H+

0

-

1.1.1.31

D-3-hydroxyisobutyrate + NAD+ = methylmalonate semialdehyde + NADH + H+

0

-

1.1.1.31

DL-3-hydroxyisobutyrate + NAD+ = methylmalonate semialdehyde + NADH + H+

0

-

1.1.1.31

L-3-hydroxyisobutyrate + NAD+ = methylmalonate semialdehyde + NADH + H+

0

-

1.1.1.31

3-hydroxyisobutyric acid + NAD+ = methylmalonic semialdehyde + NADH

0

-

1.1.1.59

(R)-3-hydroxyisobutyrate + NAD+ = 3-oxoisobutyrate + NADH + H+

0

-

1.1.1.59

(S)-3-hydroxyisobutyrate + NAD+ = 3-oxoisobutyrate + NADH + H+

0

-

1.1.1.59

3-hydroxyisobutyrate + NAD+ = methylmalonate semialdehyde + NADH + H+

0

-

2.6.1.18

pyruvate + DL-3-aminoisobutanoate = L-alanine + 3-oxoisobutanoate

288059

-

2.6.1.18

DL-aminoisobutanoate + propionaldehyde = oxoisobutanoate + 1-aminopropane

0

-

1.1.1.276

2 entries

1.1.1.31

15 entries

1.1.1.59

3 entries

2.6.1.18

2 entries

2.6.1.19

3-aminoisobutanoate + 2-oxoglutarate = L-glutamate + 3-oxoisobutanoate

0

-

2.6.1.2

2-oxoglutarate + DL-3-aminoisobutanoate = glutamate + 3-oxoisobutanoate

636727

-

2.6.1.22

(S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate

636963, 636962, 0

-

2.6.1.40

(R)-3-amino-2-methylpropanoate + 2-oxo-n-butanoate = 2-methyl-3-oxopropanoate + 2-amino-n-butanoate

0

-

2.6.1.40

(R)-3-amino-2-methylpropanoate + 2-oxo-n-pentanoate = 2-methyl-3-oxopropanoate + norvaline

0

-

2.6.1.40

(R)-3-amino-2-methylpropanoate + glyoxylate = 2-methyl-3-oxopropanoate + glycine

0

-

2.6.1.40

(R)-3-amino-2-methylpropanoate + oxaloacetate = 2-methyl-3-oxopropanoate + L-aspartate

0

-

2.6.1.40

(R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-oxopropanoate + L-alanine

644428, 644426, 644430

-

2.6.1.40

5 entries

2.6.1.55

DL-3-aminoisobutyrate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate

636678, 636677, 636679

-

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

1.2.1.27

0.003

-

pH 8.2, 30°C

722211

1.2.1.27

0.003

-

30°C, pH 8.2

722211

1.2.1.27

1.1

-

50 mM potassium phosphate pH 8.2, 30°C, 0.5 mM 2-methyl-3-oxopropanoate, 12 mM NAD+, 0.5 mM CoA

671852

1.2.1.27

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

1.2.1.18

0.0053

-

-

288055

1.2.1.27

0.0025

-

-

390223

1.2.1.27

0.0053

-

-

288055

1.2.1.27

0.006

-

R124L mutant enzyme, steady-state conditions, pH 8.2 and 30°C

725429

1.2.1.27

0.019

-

-

390219

1.2.1.27

0.021

-

V229G/H226P/G225 insertion, pH 8.2 and 30°C

725485

1.2.1.27

0.022

-

G225 insertion, pH 8.2 and 30°C

725485

1.2.1.27

0.023

-

R301L mutant enzyme, steady-state conditions, pH 8.2 and 30°C

725429

1.2.1.27

0.024

-

-

390218

1.2.1.27

0.027

-

V229G/G225 insertion, pH 8.2 and 30°C

725485

1.2.1.27

0.028

-

V229G/H226P, pH 8.2 and 30°C

725485

1.2.1.27

0.054

-

V229G, pH 8.2 and 30°C

725485

1.2.1.27

0.06

-

50 mM KP04 pH 8.2, 30°C, 0.5 mM 2-methyl-3-oxopropanoate, 12 mM NAD+, 0.5 mM CoA

671852

1.2.1.27

0.06

-

wild type MSDH, pH 8.2 and 30°C

725485

1.2.1.27

0.06

-

wild type MSDH, steady-state conditions, pH 8.2 and 30°C

725429

1.2.1.27

0.215

-

V229G/Y252L/V253I/G225 insertion, pH 8.2 and 30°C

725485

1.2.1.27

15 entries

References & Links

Literature References (25)

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Show Reference (25 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

288055

2768248

Purification and characterization of methylmalonate-semialdehyde dehydrogenase from rat liver. Identity to malonate-semialdehyde dehydrogenase

1989

Goodwin, G.W.; Rougraff, P.M.; Davis, E.J.; Harris, R.A.

J. Biol. Chem.

264

14965-14971

288059

13712439

Enzymatic studies on the metabolism of beta-alanine

1961

Hayaishi, O.; Nishizuka, Y.; Tatibana, M.; Takeshita, M.; Kuno, S.

J. Biol. Chem.

236

781-790

390218

3149395

Purification of methylmalonate-semialdehyde dehydrogenase from Pseudomonas aeruginosa PAO

1988

Hatter, K.; Sokatch, J.R.

Methods Enzymol.

166

389-393

390219

4314598

Properties of purified methylmalonate semialdehyde dehydrogenase of Pseudomonas aeruginosa

1970

Bannerjee, D.; Sanders, L.E.; Sokatch, J.R.

J. Biol. Chem.

245

1828-1835

390220

4297649

Oxidation of methylmalonate semialdehyde to propionyl coenzyme A in Pseudomonas aeruginosa grown on valine

1968

Sokatch, J.R.; Sanders, L.E.; Marshall, V.P.

J. Biol. Chem.

243

2500-2506

390223

10989432

Mammalian methylmalonate-semialdehyde dehydrogenase

2000

Kedishvili, N.Y.; Goodwin, G.W.; Popov, K.M.; Harris, R.A.

Methods Enzymol.

324

207-218

636677

5012173

Crystalline taurine: alpha-ketoglutarate aminotransferase from Achromobacter superficialis

1972

Toyama, S.; Misono, H.; Soda, K.

Biochem. Biophys. Res. Commun.

46

1374-1379

636678

3003495

Taurine-glutamate transaminase

1985

Yonaha, K.; Toyama, S.; Soda, K.

Methods Enzymol.

113

102-108

636679

629994

Properties of taurine: alpha-ketoglutarate aminotransferase of Achromobacter superficialis. Inactivation and reactivation of enzyme

1978

Toyama, S.; Misono, H.; Soda, K.

Biochim. Biophys. Acta

523

75-81

636727

6816789

Purification and properties of beta-alanine aminotransferase from rabbit liver

1982

Tamaki, N.; Aoyama, H.; Kubo, K.; Ikeda, T.; Hama, T.

J. Biochem.

92

1009-1017

636962

5641913

beta-Aminoisobutyrate-alpha-ketoglutarate transaminase in relation to beta-aminoisobutyric aciduria

1968

Kakimoto, Y.; Kanazawa, A.; Taniguchi, K.; Sano, I.

Biochim. Biophys. Acta

156

374-380

636963

3113494

Identity of beta-alanine-oxo-glutarate aminotransferase and L-beta-aminoisobutyrate aminotransferase in rat liver

1987

Tamaki, N.; Fujimoto, S.; Mizota, C.; Kikugawa, M.

Biochim. Biophys. Acta

925

238-240

644426

2158891

Purification, characterization and inhibition of D-3-aminoisobutyrate aminotransferase from the rat liver

1990

Tamaki, N.; Kaneko, M.; Mizota, C.; Kikugawa, M.; Fujimoto, S.

Eur. J. Biochem.

189

39-45

644428

5773299

D-beta-Aminoisobutyrate:pyruvate aminotransferase in mammalian liver and excretion of beta-aminoisobutyrate by man

1969

Kakimoto, Y.; Taniguchi, K.; Sano, I.

J. Biol. Chem.

244

335-340

644430

2306461

Purification and characterization of D-3-aminoisobutyrate-pyruvate aminotransferase from rat liver

1990

Ueno, S.I.; Morino, H.; Sano, A.; Kakimoto, Y.

Biochim. Biophys. Acta

1033

169-175

654105

15272169

Expression, purification, crystallization and preliminary X-ray diffraction data of methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis

2004

Dubourg, H.; Stines-Chaumeil, C.; Didierjean, C.; Talfournier, F.; Rahuel-Clermont, S.; Branlant, G.; Aubry, A.

Acta Crystallogr. Sect. D

60

1435-1437

656987

15045523

Methylmalonate-semialdehyde dehydrogenase is induced in auxin-stimulated and zinc-stimulated root formation in rice

2004

Oguchi, K.; Tanaka, N.; Komatsu, S.; Akao, S.

Plant Cell Rep.

22

848-858

671852

16332250

Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis

2006

Stines-Chaumeil, C.; Talfournier, F.; Branlant, G.

Biochem. J.

395

107-115

710894

20696867

The development of ciprofloxacin resistance in Pseudomonas aeruginosa involves multiple response stages and multiple proteins

2010

Su, H.C.; Ramkissoon, K.; Doolittle, J.; Clark, M.; Khatun, J.; Secrest, A.; Wolfgang, M.C.; Giddings, M.C.

Antimicrob. Agents Chemother.

54

4626-4635

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

725429

21515690

Methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis: substrate specificity and coenzyme A binding

2011

Talfournier, F.; Stines-Chaumeil, C.; Branlant, G.

J. Biol. Chem.

286

21971-21981

725485

22782904

Adenine binding mode is a key factor in triggering the early release of NADH in coenzyme A-dependent methylmalonate semialdehyde dehydrogenase

2012

Bchini, R.; Dubourg-Gerecke, H.; Rahuel-Clermont, S.; Aubry, A.; Branlant, G.; Didierjean, C.; Talfournier, F.

J. Biol. Chem.

287

31095-31103

725642

21863277

3-Hydroxyisobutyrate aciduria and mutations in the ALDH6A1 gene coding for methylmalonate semialdehyde dehydrogenase

2012

Sass, J.O.; Walter, M.; Shield, J.P.; Atherton, A.M.; Garg, U.; Scott, D.; Woods, C.G.; Smith, L.D.

J. Inherit. Metab. Dis.

35

437-442

743075

26832667

Crystal structure and modeling of the tetrahedral intermediate state of methylmalonate-semialdehyde dehydrogenase (MMSDH) from Oceanimonas doudoroffii

2016

Do, H.; Lee, C.W.; Lee, S.G.; Kang, H.; Park, C.M.; Kim, H.J.; Park, H.; Park, H.; Lee, J.H.

J. Microbiol.

54

114-121

762976

28799697

Methylmalonate-semialdehyde dehydrogenase mediated metabolite homeostasis essentially regulate conidiation, polarized germination and pathogenesis in Magnaporthe oryzae

2017

Norvienyeku, J.; Zhong, Z.; Lin, L.; Dang, X.; Chen, M.; Lin, X.; Zhang, H.; Anjago, W.M.; Lin, L.; Abdul, W.; Wang, Z.

Environ. Microbiol.

19

4256-4277

Links to other databases for 2-methyl-3-oxopropanoic acid

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