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  • InChIKey
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• • In Vivo Substrate
  • In Vivo Product
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  • Product
  • Cofactor
  • Activator
  • Inhibitor
  • Metals and Ions
  • 3D Structure (PDB)
• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
  • K_M Value
  • K_i Value
  • IC₅₀ Value
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• • References
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Ligand methylmalonyl-CoA

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

KEGG

Biosynthesis of 12-, 14- and 16-membered macrolides, Biosynthesis of secondary metabolites

MetaCyc

(S)-lactate fermentation to propanoate, acetate and hydrogen, 3-hydroxypropanoate cycle, 3-hydroxypropanoate/4-hydroxybutanate cycle, anaerobic energy metabolism (invertebrates, mitochondrial), conversion of succinate to propanoate, crotonyl-CoA/ethylmalonyl-CoA/hydroxybutyryl-CoA cycle (engineered), methylaspartate cycle, propanoyl CoA degradation I, pyruvate fermentation to propanoate I more

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (2 results)

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Show Natural Substrate (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.111

eicosanoyl-CoA + 4 methylmalonyl-CoA + 8 NADPH + 8 H+ = tetramethyl-branched mycocerosoyl-CoA + 4 CoA + 4 CO2 + 8 NADP+ + 4 H2O

486135, 486136, 486137, 486138, 486139

-

2.3.1.94

6 methylmalonyl-CoA + propionyl-CoA + 6 NADPH + 6 H+ = 6-deoxyerythronolide b + 7 CoA + 6 CO2 + H2O + 6 NADP+

487722

-

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

6.4.1.2

ATP + propionyl-CoA + HCO3- = ADP + phosphate + methylmalonyl-CoA

0

-

Substrate in Enzyme-catalyzed Reactions (46 results)

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Show Substrate (46 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.111

eicosanoyl-CoA + 4 methylmalonyl-CoA + 4 NADPH = 2,4,6,8-tetramethyloctacosanoyl-CoA + 4 CoA + 4 CO2 + 4 NADP+

486135

-

2.3.1.111

eicosanoyl-CoA + 4 methylmalonyl-CoA + 8 NADPH + 8 H+ = tetramethyl-branched mycocerosoyl-CoA + 4 CoA + 4 CO2 + 8 NADP+ + 4 H2O

486136, 486137, 486138, 486139, 486135

-

2.3.1.111

hexanoyl-CoA + methylmalonyl-CoA + NADPH = ?

486135

-

2.3.1.171

methylmalonyl-CoA + cyanidin 3-O-beta-D-glucoside = CoA + cyanidin 3-O-(6-O-methylmalonyl-beta-D-glucoside)

657110

-

2.3.1.171

methylmalonyl-CoA + pelargonidin 3-O-beta-D-glucoside = CoA + pelargonidin 3-O-(6-O-methylmalonyl-beta-D-glucoside)

656963, 656933

-

2.3.1.111

3 entries

2.3.1.171

2 entries

2.3.1.172

methylmalonyl-CoA + shisonin = CoA + methylmalonylshisonin

656032

-

2.3.1.187

methylmalonyl-CoA + dephospho-CoA = CoA + methylmalonyl-dephospho-CoA

686494, 686493

-

2.3.1.212

4-coumaroyl-CoA + (2RS)-methylmalonyl-CoA + H2O = 2 CoA + 1-(4-hydroxyphenyl)pent-1-en-3-one + 2 CO2

722314

-

2.3.1.212

N-methylanthraniloyl-CoA + (2RS)-methylmalonyl-CoA = 4-hydroxy-1,3-dimethyl-2(1H)-quinolone + ?

722314

-

2.3.1.212

3 (2RS)-methylmalonyl-CoA + H2O = 6-ethyl-4-hydroxy-3,5-dimethyl-2-pyrone + ?

722314

-

2.3.1.212

4-coumaroyl-CoA + methylmalonyl-CoA + H2O = 2 CoA + 1-(4-hydroxyphenyl)pent-1-en-3-one + 2 CO2

723327

-

2.3.1.212

anthraniloyl-CoA + methylmalonyl-CoA + H2O = ?

723330

-

2.3.1.212

N-methylanthraniloyl-CoA + methylmalonyl-CoA + H2O = ?

723330

-

2.3.1.226

methylmalonyl-CoA + (2S,5S)-5-carboxymethylproline + CO2 = CoA + (2S,5S,6R)-6-methyl-5-carboxymethylproline

723252

-

2.3.1.226

methylmalonyl-CoA + (2S,5S)-5-carboxymethylproline + CO2 = CoA + (2S,5S,6S)-6-methyl-5-carboxymethylproline

723252

-

2.3.1.226

methylmalonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O = CoA + (2S,5S)-6-methyl-5-carboxymethylproline + CO2

721595, 722643

-

2.3.1.226

methylmalonyl-CoA + L-2-aminoadipate semialdehyde = CoA + (2S,6S,7R)-7-methyl-carboxymethylpipecolic acid

723252

-

2.3.1.226

methylmalonyl-CoA + L-2-aminoadipate semialdehyde = CoA + (2S,6S,7S)-7-methyl-carboxymethylpipecolic acid

723252

-

2.3.1.212

6 entries

2.3.1.226

5 entries

2.3.1.233

acetoacetyl-CoA + methylmalonyl-CoA = 3,6-dimethyl-4-hydroxy-2-pyrone + CoA + CO2 + H2O

729961

-

2.3.1.39

methylmalonyl-CoA + acyl-carrier protein = CoA + methylmalonyl-[acyl-carrier protein]

686493, 4866

-

2.3.1.39

methylmalonyl-CoA + an [acyl-carrier protein] = CoA + a methalmalonyl-[acyl-carrier protein]

755871

-

2.3.1.39

methylmalonyl-CoA + an [acyl-carrier protein] = CoA + a methylmalonyl-[acyl carrier protein]

755871

-

2.3.1.39

3 entries

2.3.1.71

methylmalonyl-CoA + glycine = CoA + N-methylmalonylglycine

486265

-

2.3.1.74

(2RS)-methylmalonyl-CoA + n-hexanoyl-CoA = triketide lactone + 6-ethyl-4-hydroxy-3,5-dimethyl-2-pyrone

758097

-

2.3.1.74

4-coumaroyl-CoA + (2RS)-methylmalonyl-CoA = 1-(4-hydroxyphenyl)pent-1-en-3-one

758097

-

2.3.1.74

cinnamoyl diketide-N-methylanthraniloyl-CoA + (2RS)-methylmalonyl-CoA = styrylpyrone

758097

-

2.3.1.74

benzoyl-CoA + methylmalonyl-CoA = 4-hydroxy-3,5-dimethyl-6-phenyl-pyran-2-one + 4-hydroxy-3,5-dimethyl-6-(1-methyl-2-oxo-2-phenyl-ethyl)-pyran-2-one + CoA + CO2

663006

-

2.3.1.74

hexanoyl-CoA + methylmalonyl-CoA = 4-hydroxy-3,5-dimethyl-6-pentyl-pyran-2-one + CoA + CO2

663006

-

2.3.1.74

5 entries

2.3.1.81

methylmalonyl-CoA + neomycin B = CoA + N3-methylmalonylneomycin B

703205

-

2.3.1.85

methylmalonyl-CoA + an [acyl-carrier protein] = CoA + a methylmalonyl-[acyl-carrier protein]

755686

-

2.3.1.94

6 methylmalonyl-CoA + propionyl-CoA + 6 NADPH + 6 H+ = 6-deoxyerythronolide b + 7 CoA + 6 CO2 + H2O + 6 NADP+

487722

-

2.3.1.B32

methylmalonyl-CoA + an [acyl-carrier protein] = CoA + a methylmalonyl-[acyl-carrier protein]

735679

-

2.8.3.13

methylmalonyl-CoA + 3-hydroxy-3-methylglutarate = methylmalonate + 3-hydroxy-3-methylglutaryl-CoA

643834

-

2.8.3.13

methylmalonyl-CoA + adipate = methylmalonate + adipyl-CoA

643834

-

2.8.3.13

methylmalonyl-CoA + glutarate = methylmalonate + glutaryl-CoA

643834

-

2.8.3.13

methylmalonyl-CoA + malonate = methylmalonate + malonyl-CoA

643834

-

2.8.3.13

methylmalonyl-CoA + succinate = methylmalonate + succinyl-CoA

643834

-

2.8.3.13

5 entries

2.8.3.3

methylmalonyl-CoA + malonate = malonyl-CoA + methylmalonate

4864

-

3.1.2.17

DL-methylmalonyl-CoA + H2O = CoA + methylmalonate

643853

-

3.1.2.20

methylmalonyl-CoA + H2O = CoA + methylmalonate

690932, 698975, 707486

-

4.1.1.9

methylmalonyl-CoA = propionyl-CoA + CO2

4864, 4849, 4847, 4856, 4852, 651816

-

4.1.1.94

methylmalonyl-CoA = propanoyl-CoA + CO2

717859

-

5.1.99.1

DL-methylmalonyl-CoA = ?

2434, 2442

-

5.1.99.1

methylmalonyl-CoA = ?

649408

-

5.1.99.1

2 entries

5.4.99.2

methylmalonyl-CoA = succinyl-CoA

649513, 661149, 662325

-

5.4.99.64

methylmalonyl-CoA = succinyl-CoA

738677

-

Product in Enzyme-catalyzed Reactions (9 results)

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Show Product (9 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.1.85

acryloyl-CoA + CO2 + NADPH + H+ = methylmalonyl-CoA + NADP+

0

-

2.8.3.13

3-hydroxy-3-methylglutaryl-CoA + methylmalonate = 3-hydroxy-3-methylglutarate + methylmalonyl-CoA

643834

-

2.8.3.13

adipyl-CoA + methylmalonate = adipate + methylmalonyl-CoA

643834

-

2.8.3.13

glutaryl-CoA + methylmalonate = glutarate + methylmalonyl-CoA

643834

-

2.8.3.13

malonyl-CoA + methylmalonate = malonate + methylmalonyl-CoA

643834

-

2.8.3.13

succinyl-CoA + methylmalonate = succinate + methylmalonyl-CoA

643834

-

6.4.1.2

ATP + propionyl-CoA + HCO3- = ADP + methylmalonyl-CoA + phosphate

0

-

6.4.1.2

ATP + propionyl-CoA + HCO3- = ADP + phosphate + methylmalonyl-CoA

0, 37580, 651169

-

2.8.3.13

5 entries

6.4.1.2

2 entries

6.4.1.3

ATP + propanoyl-CoA + HCO3- = ADP + phosphate + methylmalonyl-CoA

1863, 1867, 1868, 1876, 1880, 1881, 1870, 1873, 1878, 1865, 1866, 1869, 1875, 1872, 1874, 1871, 1864, 1877, 0, 1879

-

Inhibitor in Enzyme-catalyzed Reactions (17 results)

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Show Inhibitors (17 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.36

-

286615

-

1.3.1.8

i.e. tiglyl-CoA

390850

-

2.3.1.1

about 40% residual activity at 2.5 mM

735706

-

2.3.1.21

CPT I

486532

-

2.3.1.21

inhibits sheep liver CPT I, no inhibition of rat liver and guinea-pig liver mitochondrial CPT I

486552

-

2.3.1.21

partial proteolysis of CPT I slightly diminishes the inhibitory effect

486572

-

2.3.1.21

3 entries

2.3.1.39

inhibition of MCT1 at 0.1 mM

486887

-

2.7.11.4

-

349056, 640583

-

2.7.11.4

40% inhibition at 0.2 mM

640579

-

3.1.2.4

competitive

94558

-

3.1.2.4

competitive inhibition

653127

-

4.1.1.9

-

4847, 4849, 4850, 4851, 4852, 4854, 4856

-

4.1.1.9

competitive

4846

-

2.7.11.4

2 entries

3.1.2.4

2 entries

4.1.1.9

2 entries

5.4.99.2

reversible mixed-type inhibition

3513

-

6.4.1.2

0.5 mM, 79% inhibition of acetyl-CoA carboxylase

725234

-

6.4.1.2

60% inhibition at 0.5 mM; 79% inhibition at 0.5 mM

745205

-

6.4.1.2

2 entries

6.4.1.3

0.5 mM, 60% inhibition of propionyl-CoA carboxylase

725234

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (11 results)

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Show Turnover Number (11 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.3.1.39

5

-

mutant enzyme R117A, pH and temperature not specified in the publication

755871

2.3.1.39

1000

-

wild type enzyme, pH and temperature not specified in the publication

755871

2.3.1.39

1000

-

wild-type enzyme, pH and temperature not specified in the publication

755871

2.3.1.39

3 entries

2.3.1.85

4

-

didomain construct, pH not specified in the publication, 25°C

755686

2.3.1.B32

0.033

-

pH 7.6, temperature not specified in the publication

735679

3.1.2.20

0.083

-

wild-type protein, pH7.5, 25°C

707486

3.1.2.20

1.1

-

absorbance of 5-thio-2-nitrobenzoate formed by reaction of 5,5'-dithiobis(2-nitrobenzoic acid) is measured

690932

4.1.1.94

1.61

-

pH 7.1, 30°C, recombinant enzyme in absence of ATP-Mg2-

717859

4.1.1.94

1.81

-

pH 7.1, 30°C, recombinant enzyme in presence of 5 mM ATP-Mg2-

717859

5.1.99.1

240

-

-

649408

5.1.99.1

4170

-

-

2434, 2442

3.1.2.20

2 entries

4.1.1.94

2 entries

5.1.99.1

2 entries

K_M Value (24 results)

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Show KM Value (24 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.3.1.187

0.01

-

-

686494

2.3.1.187

0.016

-

pH 7.0

686493

2.3.1.39

0.016

-

pH 7.5, 37°C

686493

2.3.1.39

0.33

-

mutant enzyme R117A, pH and temperature not specified in the publication

755871

2.3.1.39

0.58

-

wild type enzyme, pH and temperature not specified in the publication

755871

2.3.1.39

0.58

-

wild-type enzyme, pH and temperature not specified in the publication

755871

2.3.1.187

2 entries

2.3.1.39

4 entries

2.3.1.71

360

-

-

486265

2.3.1.85

0.00062

-

didomain construct, pH not specified in the publication, 25°C

755686

2.3.1.B32

0.002

-

pH 7.6, temperature not specified in the publication

735679

2.8.3.13

0.65

-

pH 7.8, 30°C, cosubstrate malonate

643834

2.8.3.13

0.72

-

pH 7.8, 30°C, cosubstrate glutarate or adipate

643834

2.8.3.13

0.74

-

pH 7.8, 30°C, cosubstrate 3-hydroxy-3-methylglutarate

643834

2.8.3.13

0.87

-

pH 7.8, 30°C, cosubstrate succinate

643834

2.8.3.13

4 entries

3.1.2.17

1.4

-

pH 6.0, 30°C

643853

3.1.2.20

0.17

-

pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay

690932

3.1.2.20

0.21

-

wild-type protein, pH7.5, 25°C

707486

4.1.1.94

0.0031

-

pH 7.1, 30°C, recombinant enzyme in absence of ATP-Mg2-

717859

4.1.1.94

0.0151

-

pH 7.1, 30°C, recombinant enzyme in presence of 5 mM ATP-Mg2-

717859

5.1.99.1

0.079

-

-

649408

5.1.99.1

0.1

-

-

2434, 2442

5.4.99.2

0.11

-

37°C, pH 7, in presence of 3 mM NH4+

649513

5.4.99.2

0.13

-

37°C, pH 7, without NH4+

649513

5.4.99.2

0.133

-

wild type, 37°C

661149

5.4.99.2

0.357

-

mutant Y89F, 37°C

661149

3.1.2.20

2 entries

4.1.1.94

2 entries

5.1.99.1

2 entries

5.4.99.2

4 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

3.1.2.4

2.26

-

recombinant enzyme, pH 8.0, 30°C

653127

References & Links

Literature References (86)

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Show Reference (86 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

1863

3555348

Sequence homology around the biotin-binding site of human propionyl-CoA carboxylase and pyruvate carboxylase

1987

Lamhonwah, A.M.; Quan, F.; Gravel, R.A.

Arch. Biochem. Biophys.

254

631-636

1864

-

Propionyl-CoA carboxylase in Nocardia mediterranei

1984

Gygax, D.; Stalder, R.; Nuesch, J.

FEMS Microbiol. Lett.

23

211-216

1865

6705792

Propionyl-coenzyme A carboxylase of Mycobacterium smegmatis

1984

Haase, F.C.; Beegen, H.; Allen, S.H.G.

Eur. J. Biochem.

140

147-151

1866

7118926

The subunit structure and function of the propionyl coenzyme A carboxylase of Mycobacterium smegmatis

1982

Haase, F.C.; Henrikson, K.P.; Treble, D.H.; Allen, S.H.G.

J. Biol. Chem.

257

11994-11999

1867

7396525

Purification of human liver propionyl-CoA carboxylase by carbon tetrachloride extraction and monomeric avidin affinity chromatography

1980

Gravel, R.A.; Lam, F.K.; Mahuran, D.; Kronis, A.

Arch. Biochem. Biophys.

201

669-673

1868

6765947

Isolation and characterization of propionyl-CoA carboxylase from normal human liver. Evidence for a protomeric tetramer of nonidentical subunits

1980

Kalousek, F.; Darigo, M.D.; Rosenberg, L.E.

J. Biol. Chem.

255

60-65

1869

447686

Purification and subunit structure of propionyl coenzyme A carboxylase of Mycobacterium smegmatis

1979

Henrikson, K.P.; Allen, S.H.G.

J. Biol. Chem.

254

5888-5891

1870

16170895

Bovine kidney 3-methylcrotonyl-CoA and propionyl-CoA carboxylase: each enzyme contains nonidentical subunits

1979

Lau, E.P.; Cochran, B.C.; Munson, L.; Fall, R.R.

Proc. Natl. Acad. Sci. USA

76

214-218

1871

8091

Multiple acyl-coenzyme A carboxylases in Pseudomonas citronellolis

1976

Hector, M.L.; fall, R.R.

Biochemistry

15

3465-3472

1872

4147495

Acetyl-CoA and propionyl-CoA carboxylation by Mycobacterium phlei. Partial purification and some properties of the enzyme

1973

Erfle, J.D.

Biochim. Biophys. Acta

316

143-155

1873

13752080

Metabolism of propionic acid in animal tissues. VIII. Crystalline propionyl carboxylase

1961

Kaziro, Y.; Ochoa, S.; Warner, R.C.; Chen, J.Y.

J. Biol. Chem.

236

1917-1923

1874

9371458

Propionyl coenzyme A carboxylase is required for development of Myxococcus xanthus

1997

Kimura, Y.; Sato, R.; Mimura, K.; Sato, M.

J. Bacteriol.

179

7098-7102

1875

2321957

Plants contain multiple biotin enzymes: discovery of 3-methylcrotonyl-CoA carboxylase, propionyl-CoA carboxylase and pyruvate carboxylase in the plant kingdom

1990

Wurtele, E.S.; Nikolau, B.J.

Arch. Biochem. Biophys.

278

179-186

1876

2740237

Human mitochondrial propionyl-CoA carboxylase: localization of the N-terminus of the pro-and mature alpha chains in the deduced primary sequence of a full-length cDNA

1989

Lamhonwah, A.M.; Mahuran, D.; Gravel, R.A.

Nucleic Acids Res.

17

4396

1877

8868440

Propionyl-CoA carboxylase from Streptomyces coelicolor A3(2): cloning of the gene encoding the biotin-containing subunit

1996

Bramwell, H.; Hunter, I.S.; Coggins, J.R.; Nimmo, H.G.

Microbiology

142

649-655

1878

1769208

Comparative analysis of propionyl-CoA carboxylase from liver and mammary gland of mid-lactation cow

1991

Garrastazu, C.; Iniesta, M.P.; Aranguez, M.I.; Amil, M.R.

Comp. Biochem. Physiol. B

99

613-617

1879

9082912

Autotrophic carbon dioxide fixation in Acidianus brierleyi

1997

Ishii, M.; Miyake, T.; Satoh, T.; Sugiyama, H.; Oshima, Y.; Kodama, T.; Igarashi, Y.

Arch. Microbiol.

166

368-371

1880

8434582

Cloning of functional alpha propionyl CoA carboxylase and correction of enzyme deficiency in pccA fibroblasts

1993

Stankovic, J.; Ledley, F.D.

Am. J. Hum. Genet.

52

144-151

1881

8852656

Chaperonin-mediated assembly of wild-type and mutant subunits of human propionyl-CoA carboxylase expressed in Escherichia coli

1996

Kelson, T.L.; Ohura, T.; Kraus, J.P.

Hum. Mol. Genet.

5

331-337

2434

2862845

Isolation and characterization of DL-methylmalonyl-coenzyme A racemase from rat liver

1985

Stabler, S.P.; Marcell, P.D.; Allen, R.H.

Arch. Biochem. Biophys.

241

252-264

2442

3071715

DL-Methylmalonyl-CoA racemase from rat liver

1988

Stabler, S.P.; Allen, R.H.

Methods Enzymol.

166

400-406

3513

7989334

Inhibition of the human methylmalonyl-CoA mutase by various CoA-esters

1994

Taoka, S.; Padmakumar, R.; Lai, M.; Liu, H.; Banerjee, R.

J. Biol. Chem.

269

31630-31634

4846

4152381

Malonate metabolism in rat brain mitochondria

1974

Koeppen, A.H.; Mitzen, E.J.; Ammoumi, A.A.

Biochemistry

13

3589-3595

4847

827976

Purification and properties of malonyl-coenzyme A decarboxylase, a regulatory enzyme from the uropygial gland of goose

1976

Buckner, J.S.; Kolattukudy, P.E.; Poulose, A.J.

Arch. Biochem. Biophys.

177

539-551

4849

101148

Purification and properties of malonyl-CoA decarboxylase from rat liver mitochondria and its immunological comparison with the enzymes from rat brain, heart, and mammary gland

1978

Kim, Y.S.; Kolattukudy, P.E.

Arch. Biochem. Biophys.

190

234-246

4850

102255

Malonyl-CoA decarboxylase from the uropygial gland of waterfowl: purification, properties, immunological comparison, and role in regulating the synthesis of multimethyl-branched fatty acids

1978

Kim, Y.S.; Kolattukudy, P.E.

Arch. Biochem. Biophys.

190

585-597

4851

718970

Malonyl-CoA decarboxylase from the mammary gland of lactating rat. Purification, properties and subcellular localization

1978

Kim, Y.S.; Kolattukudy, P.E.

Biochim. Biophys. Acta

531

187-196

4852

114118

Malonyl-CoA decarboxylase from Mycobacterium tuberculosis and Pseudomonas fluorescence

1979

Kim, Y.S.; Kolattukudy, P.E.; Boos, A.

Arch. Biochem. Biophys.

196

543-551

4854

6792462

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