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Ligand (2S)-methylsuccinyl-CoA

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

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

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.8.12

(2S)-methylsuccinyl-CoA + electron-transfer flavoprotein = 2-methylfumaryl-CoA + reduced electron-transfer flavoprotein

763481, 763257, 730403

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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

5.4.99.63

(2R)-ethylmalonyl-CoA = (2S)-methylsuccinyl-CoA

0

-

Substrate in Enzyme-catalyzed Reactions (2 results)

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Show Substrate (2 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.8.12

(2S)-methylsuccinyl-CoA + electron-transfer flavoprotein = 2-methylfumaryl-CoA + reduced electron-transfer flavoprotein

763481, 763257, 730403

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1.3.8.12

(2S)-methylsuccinyl-CoA + ferrocenium hexafluorophosphate = mesaconyl-CoA + ferricenium hexafluorophosphate

763257

-

1.3.8.12

2 entries

Product in Enzyme-catalyzed Reactions (1 result)

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Show Product (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

5.4.99.63

(2R)-ethylmalonyl-CoA = (2S)-methylsuccinyl-CoA

0

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (6 results)

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Show Turnover Number (6 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.3.8.12

0.71

-

mutant enzyme A282F/F284A, at pH 7.5 and 30°C

763257

1.3.8.12

0.71

-

recombinant mutant A282F/F284A, pH 7.5, 30°C

763257

1.3.8.12

31.8

-

mutant enzyme A282V, at pH 7.5 and 30°C

763257

1.3.8.12

31.8

-

recombinant mutant A282V, pH 7.5, 30°C

763257

1.3.8.12

82.3

-

recombinant wild-type enzyme, pH 7.5, 30°C

763257

1.3.8.12

82.3

-

wild type enzyme, at pH 7.5 and 30°C

763257

1.3.8.12

6 entries

K_M Value (6 results)

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Show KM Value (6 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.8.12

0.064

-

mutant enzyme A282V, at pH 7.5 and 30°C

763257

1.3.8.12

0.064

-

recombinant mutant A282V, pH 7.5, 30°C

763257

1.3.8.12

0.08

-

recombinant wild-type enzyme, pH 7.5, 30°C

763257

1.3.8.12

0.08

-

wild type enzyme, at pH 7.5 and 30°C

763257

1.3.8.12

0.439

-

mutant enzyme A282F/F284A, at pH 7.5 and 30°C

763257

1.3.8.12

0.439

-

recombinant mutant A282F/F284A, pH 7.5, 30°C

763257

1.3.8.12

6 entries

References & Links

Literature References (3)

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Show Reference (3 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

730403

19703103

(2S)-Methylsuccinyl-CoA dehydrogenase closes the ethylmalonyl-CoA pathway for acetyl-CoA assimilation

2009

Erb, T.J.; Fuchs, G.; Alber, B.E.

Mol. Microbiol.

73

992-1008

763257

29275330

Structural basis for substrate specificity of methylsuccinyl-CoA dehydrogenase, an unusual member of the acyl-CoA dehydrogenase family

2018

Schwander, T.; McLean, R.; Zarzycki, J.; Erb, T.

J. Biol. Chem.

293

1702-1712

763481

29283425

Molecular basis for converting (2S)-methylsuccinyl-CoA dehydrogenase into an oxidase

2017

Burgener, S.; Schwander, T.; Romero, E.; Fraaije, M.W.; Erb, T.J.

Molecules

23

68

Links to other databases for (2S)-methylsuccinyl-CoA

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Show Links (1 entry)

ChEBI

PubChem

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