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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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Ligand (S)-methylmalonyl-CoA

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

CO2 fixation in Crenarchaeota, methylaspartate cycle, propionate fermentation

KEGG

Biosynthesis of 12-, 14- and 16-membered macrolides, Biosynthesis of secondary metabolites, Carbon fixation pathways in prokaryotes, Carbon metabolism, Glyoxylate and dicarboxylate metabolism, Microbial metabolism in diverse environments, Propanoate metabolism, Valine, leucine and isoleucine degradation more

MetaCyc

(S)-lactate fermentation to propanoate, acetate and hydrogen, 3-hydroxypropanoate cycle, 3-hydroxypropanoate/4-hydroxybutanate cycle, anaerobic energy metabolism (invertebrates, mitochondrial), ansatrienin biosynthesis, aureothin biosynthesis, beta-D-mannosyl phosphomycoketide biosynthesis, candicidin biosynthesis, chaxamycin biosynthesis, conversion of succinate to propanoate, crotonyl-CoA/ethylmalonyl-CoA/hydroxybutyryl-CoA cycle (engineered), dimycocerosyl phthiocerol biosynthesis, dimycocerosyl triglycosyl phenolphthiocerol biosynthesis, erythromycin D biosynthesis, methylaspartate cycle, methymycin, neomethymycin and novamethymycin biosynthesis, mycinamicin biosynthesis, mycobacterial sulfolipid biosynthesis, naphthomycin biosynthesis, narbomycin, pikromycin and novapikromycin biosynthesis, nystatin biosynthesis, oleandomycin biosynthesis, phenolphthiocerol biosynthesis, phthiocerol biosynthesis, polyacyltrehalose biosynthesis, propanoyl CoA degradation I, pyruvate fermentation to propanoate I, rifamycin B biosynthesis, rosamicin biosynthesis, spectinabilin biosynthesis, spinosyn A biosynthesis, streptovaricin biosynthesis, tylosin biosynthesis more

Show all BRENDA pathways known for (S)-methylmalonyl-CoA

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (14 results)

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Show Natural Substrate (14 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.3.1

(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate

689897, 676760, 756213, 737181, 674054

-

2.3.1.239

malonyl-CoA + 5 (2S)-methylmalonyl-CoA + 5 NADPH + 5 H+ = 10-deoxymethynolide + 6 CoA + 6 CO2 + 5 NADP+ + 2 H2O

729193

-

2.3.1.240

malonyl-CoA + 6 (2S)-methylmalonyl-CoA + 5 NADPH + 5 H+ = narbonolide + 7 CoA + 7 CO2 + 5 NADP+ + 2 H2O

729193

-

2.3.1.287

7 (S)-methylmalonyl-CoA + palmitoyl-[(hydroxy)phthioceranic acid synthase] + 14 NADPH + 14 H+ = 7 CO2 + C37-phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 14 NADP+ + 7 CoA + 7 H2O

751682

-

2.3.1.287

8 (S)-methylmalonyl-CoA + palmitoyl-[(hydroxy)phthioceranic acid synthase] + 16 NADPH + 16 H+ = 8 CoA + C40-phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 16 NADP+ + 8 CO2 + 8 H2O

751682

-

2.3.1.292

3 malonyl-CoA + 2 (S)-methylmalonyl-CoA + 17-(4-hydroxyphenyl)heptadecanoyl-[(phenol)carboxyphthiodiolenone synthase] + 5 NADPH = C35-(phenol)carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase] + 5 CoA + 5 NADP+ + 5 CO2 + 2 H2O

754715, 754743

-

2.3.1.292

3 malonyl-CoA + 2 (S)-methylmalonyl-CoA + 19-(4-hydroxyphenyl)-nonadecanoyl-[(phenol)carboxyphthiodiolenone synthase] + 5 NADPH = C37-(phenol)carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase] + 5 CoA + 5 NADP+ + 5 CO2 + 2 H2O

754715, 754743

-

2.3.1.292

3 malonyl-CoA + 2 (S)-methylmalonyl-CoA + docosanoyl-[(phenol)carboxyphthiodiolenone synthase] + 5 NADPH = C34-carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase] + 5 CoA + 5 NADP+ + 5 CO2 + 2 H2O

754715, 754743

-

2.3.1.292

3 malonyl-CoA + 2 (S)-methylmalonyl-CoA + icosanoyl-[(phenol)carboxyphthiodiolenone synthase] + 5 NADPH = C32-carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase] + 5 CoA + 5 NADP+ + 5 CO2 + 2 H2O

754715, 754743

-

2.3.1.287

2 entries

2.3.1.292

4 entries

2.3.1.295

a medium-chain acyl-CoA + 5 malonyl-CoA + 5 (S)-methylmalonyl-CoA + 22 NADPH + 22 H+ = a mycoketide-CoA + 10 CO2 + 10 CoA + 22 NADP+ + 11 H2O

754298, 755058

-

2.3.1.94

propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH + 6 H+ = 6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+

701714, 702545, 702843, 705513, 705525, 706566, 706754, 702385

-

3.1.2.17

(S)-methylmalonyl-CoA + H2O = methylmalonate + CoA

643853

-

5.1.99.1

(S)-methylmalonyl-CoA = (R)-methylmalonyl-CoA

726729

-

7.2.4.3

(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2] = propanoyl-CoA + CO2 + Na+[side 2]

4549, 4550, 4548, 4553, 4545, 4546, 4547

-

In Vivo Product in Enzyme-catalyzed Reactions (3 results)

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Show Natural Product (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.3.1

propionyl-CoA + oxaloacetate = (S)-methylmalonyl-CoA + pyruvate

485816

-

5.1.99.1

(R)-methylmalonyl-CoA = (S)-methylmalonyl-CoA

0

-

6.4.1.3

ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA

651169, 651638, 653148, 649502, 651406, 652691, 653242, 653246, 653247, 651459

-

Substrate in Enzyme-catalyzed Reactions (34 results)

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Show Substrate (34 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.3.1

(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate

689897, 676760, 756213, 737181, 674054

-

2.3.1.239

(E)-(2S,4R,8R,9R)-S-2-acetamidoethyl 9-hydroxy-2,4,8-trimethyl-5-oxoundec-6-enethioate + (2S)-methylmalonyl-CoA + NADPH + H+ = 10-deoxymethynolide + ?

729574, 729878

-

2.3.1.239

malonyl-CoA + 5 (2S)-methylmalonyl-CoA + 5 NADPH + 5 H+ = 10-deoxymethynolide + 6 CoA + 6 CO2 + 5 NADP+ + 2 H2O

729193

-

2.3.1.240

(E)-(2S,4R,8R,9R)-S-2-acetamidoethyl 9-hydroxy-2,4,8-trimethyl-5-oxoundec-6-enethioate + (2S)-methylmalonyl-CoA + NADPH + H+ = narbonolide + ?

729878

-

2.3.1.240

hexaketide N-acetyl cysteamine thioester + (2S)-methylmalonyl-CoA + NADPH + H+ = narbonolide + ?

729878

-

2.3.1.240

malonyl-CoA + 6 (2S)-methylmalonyl-CoA + 5 NADPH + 5 H+ = narbonolide + 7 CoA + 7 CO2 + 5 NADP+ + 2 H2O

729193

-

2.3.1.287

7 (S)-methylmalonyl-CoA + palmitoyl-[(hydroxy)phthioceranic acid synthase] + 14 NADPH + 14 H+ = 7 CO2 + C37-phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 14 NADP+ + 7 CoA + 7 H2O

751682

-

2.3.1.287

8 (S)-methylmalonyl-CoA + palmitoyl-[(hydroxy)phthioceranic acid synthase] + 16 NADPH + 16 H+ = 8 CoA + C40-phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 16 NADP+ + 8 CO2 + 8 H2O

751682

-

2.3.1.239

2 entries

2.3.1.240

3 entries

2.3.1.287

2 entries

2.3.1.289

4-nitrobenzoyl-CoA + malonyl-CoA + 4 (S)-methylmalonyl-CoA + 4 NADPH + 4 H+ = demethylluteothin + 5 CO2 + 6 CoA + 4 NADP+ + 3 H2O

753269, 755024

-

2.3.1.290

4-nitrobenzoyl-CoA + malonyl-CoA + 6 (S)-methylmalonyl-CoA + 6 NADPH + 4 H+ = demethyldeoxyspectinabilin + 7 CO2 + 8 CoA + 6 NADP+ + 5 H2O

754694, 753270

-

2.3.1.292

3 malonyl-CoA + 2 (S)-methylmalonyl-CoA + 17-(4-hydroxyphenyl)heptadecanoyl-[(phenol)carboxyphthiodiolenone synthase] + 5 NADPH = C35-(phenol)carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase] + 5 CoA + 5 NADP+ + 5 CO2 + 2 H2O

754715, 754743

-

2.3.1.292

3 malonyl-CoA + 2 (S)-methylmalonyl-CoA + 19-(4-hydroxyphenyl)-nonadecanoyl-[(phenol)carboxyphthiodiolenone synthase] + 5 NADPH = C37-(phenol)carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase] + 5 CoA + 5 NADP+ + 5 CO2 + 2 H2O

754715, 754743

-

2.3.1.292

3 malonyl-CoA + 2 (S)-methylmalonyl-CoA + docosanoyl-[(phenol)carboxyphthiodiolenone synthase] + 5 NADPH = C34-carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase] + 5 CoA + 5 NADP+ + 5 CO2 + 2 H2O

754715, 754743

-

2.3.1.292

3 malonyl-CoA + 2 (S)-methylmalonyl-CoA + icosanoyl-[(phenol)carboxyphthiodiolenone synthase] + 5 NADPH = C32-carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase] + 5 CoA + 5 NADP+ + 5 CO2 + 2 H2O

754715, 754743

-

2.3.1.295

9-hydroxy-decanoyl N-acetyl-cysteamine thioester + 5 malonyl-CoA + 5 (S)-methylmalonyl-CoA + 22 NADPH + 22 H+ = ?

755058

-

2.3.1.295

a medium-chain acyl-CoA + 5 malonyl-CoA + 5 (S)-methylmalonyl-CoA + 22 NADPH + 22 H+ = a mycoketide-CoA + 10 CO2 + 10 CoA + 22 NADP+ + 11 H2O

754298, 755058

-

2.3.1.295

decanoyl N-acetyl-cysteamine thioester + 5 malonyl-CoA + 5 (S)-methylmalonyl-CoA + 22 NADPH + 22 H+ = ?

755058

-

2.3.1.295

dodecanoyl N-acetyl-cysteamine thioester + 5 malonyl-CoA + 5 (S)-methylmalonyl-CoA + 22 NADPH + 22 H+ = ?

755058

-

2.3.1.295

hexadecanoyl N-acetyl-cysteamine thioester + 5 malonyl-CoA + 5 (S)-methylmalonyl-CoA + 22 NADPH + 22 H+ = ?

755058

-

2.3.1.295

hexanoyl N-acetyl-cysteamine thioester + 5 malonyl-CoA + 5 (S)-methylmalonyl-CoA + 22 NADPH + 22 H+ = ?

755058

-

2.3.1.295

octadecanoyl N-acetyl-cysteamine thioester + 5 malonyl-CoA + 5 (S)-methylmalonyl-CoA + 22 NADPH + 22 H+ = ?

755058

-

2.3.1.295

octanoyl N-acetyl-cysteamine thioester + 5 malonyl-CoA + 5 (S)-methylmalonyl-CoA + 22 NADPH + 22 H+ = ?

755058

-

2.3.1.295

propionyl N-acetyl-cysteamine thioester + 5 malonyl-CoA + 5 (S)-methylmalonyl-CoA + 22 NADPH + 22 H+ = ?

755058

-

2.3.1.295

tetradecanoyl N-acetyl-cysteamine thioester + 5 malonyl-CoA + 5 (S)-methylmalonyl-CoA + 22 NADPH + 22 H+ = ?

755058

-

2.3.1.94

propanoyl-CoA + (2S)-methylmalonyl-CoA + NADPH = (3R,4S,5R,6R)-6-ethyl-4-hydroxy-3,5-dimethyloxan-2-one + ?

756037

-

2.3.1.94

propanoyl-CoA + 5 (2S)-methylmalonyl-CoA + (2S)-ethylmalonyl-CoA + 6 NADPH + 6 H+ = (3R,4S,5R,6R)-6-ethyl-4-hydroxy-3,5-dimethyltetrahydro-2H-pyran-2-one + ?

736307

-

2.3.1.94

propanoyl-CoA + 5 (2S)-methylmalonyl-CoA + (2S)-ethylmalonyl-CoA + 6 NADPH + 6 H+ = (3R,5R,6S)-6-[(2S,3R)-3-hydroxypentan-2-yl]-3,5-dimethyldihydro-2H-pyran-2,4(3H)-dione + ?

736307

-

2.3.1.94

propanoyl-CoA + 5 (2S)-methylmalonyl-CoA + (2S)-ethylmalonyl-CoA + 6 NADPH + 6 H+ = 8-ethyl-8-desmethyl-6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+

736307

-

2.3.1.94

propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH + 6 H+ = 6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+

701714, 702545, 702843, 705513, 705525, 706566, 706754, 702385, 735679, 736307

-

2.3.1.292

4 entries

2.3.1.295

10 entries

2.3.1.94

5 entries

3.1.2.17

(S)-methylmalonyl-CoA + H2O = methylmalonate + CoA

643853, 643854

-

3.1.2.4

(S)-methylmalonyl-CoA + H2O = CoA + methylmalonate

94558

-

5.1.99.1

(S)-methylmalonyl-CoA = (R)-methylmalonyl-CoA

693174, 726729

-

5.4.99.2

(S)-methylmalonyl-CoA = succinyl-CoA

677443

-

7.2.4.3

(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2] = propanoyl-CoA + CO2 + Na+[side 2]

4545, 4546, 4547, 4549, 4550, 4551, 4552, 4553, 4548, 4544

-

Product in Enzyme-catalyzed Reactions (10 results)

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Show Product (10 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.3.1

propionyl-CoA + oxaloacetate = (S)-methylmalonyl-CoA + pyruvate

485817, 485818, 485819, 485822, 4552, 485833, 485816, 485825, 485823, 485826, 485827, 485828, 485829, 485830, 485831, 485832, 485834

-

5.1.99.1

(2R)-methylmalonyl-CoA = (2S)-methylmalonyl-CoA

0

-

5.1.99.1

(R)-methylmalonyl-CoA = (S)-methylmalonyl-CoA

0, 653930, 649408

-

6.4.1.3

ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (2S)-methylmalonyl-CoA

0

-

6.4.1.3

propionyl-CoA + CO2 = (2S)-methylmalonyl-CoA

0

-

6.4.1.3

ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA

0, 651406, 651459, 652691, 653246, 653247, 653242, 649502, 653148, 651169, 651638

-

6.4.1.3

ATP + propionyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA

0

-

6.4.1.3

GTP + propanoyl-CoA + HCO3- = GDP + phosphate + (S)-methylmalonyl-CoA

651169

-

6.4.1.3

propionyl-CoA + CO2 = (S)-methylmalonyl-CoA

0

-

6.4.1.3

UTP + propanoyl-CoA + HCO3- = UDP + phosphate + (S)-methylmalonyl-CoA

651169

-

5.1.99.1

2 entries

6.4.1.3

7 entries

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.7.11.2

slight activation

642139

-

Inhibitor in Enzyme-catalyzed Reactions (2 results)

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Show Inhibitors (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.1.3.1

-

485816

-

7.2.4.3

substrate inhibition above 0.014 mM

4548

-

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

2.3.1.292

0.02

-

mutant enzyme S726F, at pH 7.0 and 30°C

754715

2.3.1.292

0.22

-

wild type enzyme, at pH 7.0 and 30°C

754715

2.3.1.292

2 entries

3.1.2.17

23.3

-

pH 6.0, 30°C

643853, 643854

K_M Value (8 results)

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Show KM Value (8 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.1.3.1

0.0077

-

-

485822, 485816

2.3.1.292

0.0701

-

wild type enzyme, at pH 7.0 and 30°C

754715

2.3.1.292

0.2386

-

mutant enzyme S726F, at pH 7.0 and 30°C

754715

2.3.1.292

2 entries

3.1.2.17

0.7

-

pH 6.0, 30°C

643853, 643854

5.1.99.1

0.08

-

-

693174

7.2.4.3

0.002

-

-

4548

7.2.4.3

0.007

-

at 20 mM NaCl

4545, 4547

7.2.4.3

0.012

-

-

4553

7.2.4.3

3 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

2.1.3.1

0.00004

-

-

485816

References & Links

Literature References (73)

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Show Reference (73 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

4544

3609308

Stereochemistry of the methylmalonyl-CoA decarboxylation reaction

1987

Hoffmann, A.; Dimroth, P.

FEBS Lett.

220

121-125

4545

-

Sodium pump methylmalonyl-CoA decarboxylase from Veillonella alcalescens

1986

Hilpert, W.; Dimroth, P.

Methods Enzymol.

125

540-546

4546

6692834

Reconstitution of Na+ transport from purified merthylmalonyl-CoA decarboxylase and phospholipid vesicles

1984

Hilpert, W.; Dimroth, P.

Eur. J. Biochem.

138

579-583

4547

6852015

Purification and characterization of a new sodium-transport decarboxylase

1983

Hilpert, W.; Dimroth, P.

Eur. J. Biochem.

132

579-587

4548

5686595

Methylmalonyl-CoA decarboxylase: partial purification and enzymatic properties

1968

Galivan, J.H.; Allen, S.H.G.

Arch. Biochem. Biophys.

126

838-847

4549

5646172

Methylmalonyl coenzyme A decarboxylase. Its role in succinate decarboxylation by Micrococcus lactilyticus

1968

Galivan, J.H.; Allen, S.H.G.

J. Biol. Chem.

243

1253-1261

4550

7070502

Conversion of the chemical energy of methylmalonyl-CoA decarboxylation into a Na+ gradient

1982

Hilpert, W.; Dimroth, P.

Nature

296

584-585

4551

-

Morphological properties of proteoliposomes reconstituted with Na+ pump methylmalonyl-CoA decarboxylase from Veillonella alcalescens

1986

Rohde, M.; Däkena, P.; Mayer, F.; Dimroth, P.

FEBS Lett.

195

280-284

4552

2920730

The carboxyltransferase activity of the sodium-ion-translocating methylmalonyl-CoA decarboxylase of Veillonella alcalescens

1989

Hoffmann, A.; Hilpert, W.; Dimroth, P.

Eur. J. Biochem.

179

645-650

4553

9428714

Methylmalonyl-CoA decarboxylase from Propionibacterium modestum. Cloning and sequencing of the structural genes and purification of the enzyme complex

1997

Bott, M.; Pfister, K.; Burda, P.; Kalbermatter, O.; Woehlke, G.; Dimroth, P.

Eur. J. Biochem.

250

590-599

94558

8188708

Purification and partial characterization of 3-hydroxyisobutyryl-coenzyme A hydrolase of rat liver

1994

Shimomura, Y.; Murakami, T.; Fujitsuka, N.; Nakai, N.; Sato, Y.; Sugiyama, S.; Shimomura, N.; Irwin, J.; Hawes, J.W.; Harris, R.A.

J. Biol. Chem.

269

14248-14253

485816

-

Transcarboxylase

1972

Wood, H.G.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

6

83-115

485817

16590594

The role of transcarboxylase in propionic acid ermentation

1960

Swick, R.W.; Wood, H.G.

Proc. Natl. Acad. Sci. USA

46

28-41

485818

1112797

Purification of the subunits of transcarboxylase by affinity chromatography on avidin-sepharose

1975

Berger, M.; Wood, H.G.

J. Biol. Chem.

250

927-933

485819

40985

Amino acid sequence of the biotinyl subunit from transcarboxylase

1979

Maloy, W.L.; Bowien, B.U.; Zwolinski, G.K.; Kumar, K.G.; Wood, H.G.; Ericsson, L.H.; Walsh, K.A.

J. Biol. Chem.

254

11615-11622

485822

1526981

The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis

1992

Shenoy, B.C.; Xie, Y.; Park, V.L.; Kumar, G.K.; Beegen, H.; Wood, H.G.; Samols, D.

J. Biol. Chem.

267

18407-18412

485823

3790507

Biotin-dependent carboxylation catalyzed by transcarboxylase is a stepwise process [published erratum appears in Biochemistry 1987 Sep 8;26(18):5952]

1986

O'Keefe, S.J.; Knowles, J.R.

Biochemistry

25

6077-6084

485825

11841210

Characterization of the carboxylate delivery module of transcarboxylase: following spontaneous decarboxylation of the 1.3S-CO2- subunit by NMR and FTIR spectroscopies

2002

Rivera-Hainaj, R.E.; Pusztai-Carey, M.; Reddy, D.V.; Choowongkomon, K.; Soennichsen, F.D.; Carey, P.R.

Biochemistry

41

2191-2197

485826

12196011

Substrate binding induces a cooperative conformational change in the 12S subunit of transcarboxylase: raman crystallographic evidence

2002

Zheng, X.; Rivera-Hainaj, R.E.; Zheng, Y.; Pusztai-Carey, M.; Hall, P.R.; Yee, V.C.; Carey, P.R.

Biochemistry

41

10741-10746

485827

8420991

Dissection of the biotinyl subunit of transcarboxylase into regions essential for activity and assembly

1993

Shenoy, B.C.; Kumar, G.K.; Samols, D.

J. Biol. Chem.

268

2232-2238

485828

8425112

The nonbiotinylated form of the 1.3 S subunit of transcarboxylase binds to avidin (monomeric)-agarose: Purification and separation from the biotinylated 1.3 S subunit

1993

Shenoy, B.C.; Magner, W.J.; Kumar, G.K.; Phillips, N.F.B.; Haase, F.C.; Samols, D.

Protein Expr. Purif.

4

85-94

485829

8346913

The conserved methionines of the 1.3 S biotinyl subunit of transcarboxylase: effect of mutations on conformation and activity

1993

Shenoy, B.C.; Samols, D.; Kumar, G.K.

Arch. Biochem. Biophys.

304

359-366

485830

8344927

Effect of deletion from the carboxyl terminus of the 12 S subunit on activity of transcarboxylase

1993

Woo, S.B.; Shenoy, B.C.; Wood, H.G.; Magner, W.J.; Kumar, G.K.; Beegen, H.; Samols, D.

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Links to other databases for (S)-methylmalonyl-CoA

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