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Ligand 2-methylbutanoyl-CoA

Basic Ligand Information

Molecular Structure

Related pathways

Show all BRENDA pathways known for 2-methylbutanoyl-CoA

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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

1.3.8.5

2-methylbutanoyl-CoA + electron transfer flavoprotein = 2-methylbut-2-enoyl-CoA + reduced electron transfer flavoprotein

391203, 391254, 391252

-

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

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.25

3-methyl-2-oxopentanoate + CoA + NAD+ = 2-methylbutanoyl-CoA + CO2 + NADH

-

-

1.2.1.25

3-methyl-2-oxopentanoate + CoA + NAD+ = 2-methylbutanoyl-CoA + CO2 + NADH + H+

-

-

1.2.1.25

2 entries

Substrate in Enzyme-catalyzed Reactions (7 results)

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Show Substrate (7 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.8.1

2-methylbutanoyl-CoA + acceptor = 2-methyl-2-butenoyl-CoA + reduced acceptor

654618

-

1.3.8.4

2-methylbutanoyl-CoA + acceptor = 2-methylbut-2-enoyl-CoA + reduced acceptor

656288

-

1.3.8.5

2-methylbutanoyl-CoA + electron transfer flavoprotein = 2-methylbut-2-enoyl-CoA + reduced electron transfer flavoprotein

391203, 391254, 391252, 656288

-

1.3.8.5

2-methylbutanoyl-CoA + electron-transfer flavoprotein = (E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+

12302

-

2.3.1.19

2-methylbutanoyl-CoA + phosphate = 2-methylbutanoyl phosphate + CoA

756087

-

2.3.1.19

2-methylbutanoyl-CoA + phosphate = CoA + 2-methylbutanoyl phosphate

756087

-

1.3.8.5

2 entries

2.3.1.19

2 entries

2.3.1.300

2-methylbutanoyl-CoA + malonyl-[acyl-carrier protein] = 4-methyl-3-oxohexanoyl-[acyl-carrier-protein] + CoA + CO2

486937

-

Product in Enzyme-catalyzed Reactions (4 results)

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Show Product (4 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.25

3-methyl-2-oxopentanoate + CoA + NAD+ = 2-methylbutanoyl-CoA + CO2 + NADH

-

-

1.2.1.25

3-methyl-2-oxopentanoate + CoA + NAD+ = 2-methylbutanoyl-CoA + CO2 + NADH + H+

-

-

1.2.1.25

2 entries

1.2.7.7

2-keto-3-methylvalerate + CoA + oxidized ferredoxin = 2-methylbutanoyl-CoA + CO2 + reduced ferredoxin

-

-

1.3.1.8

2-methyl-trans-crotonyl-CoA + NADPH = 2-methylbutanoyl-CoA + NADP+

-

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (4 results)

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Show Turnover Number (4 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.3.8.1

6

-

32°C, pH 7.0

654618

1.3.8.5

1.77

-

per enzyme tetramer, recombinant enzyme, 32°C

656288

2.3.1.19

849.1

-

pH 7.5, 23°C

756087

2.3.1.19

849.1

-

pH 7.5, 25°C

756087

2.3.1.19

2 entries

K_M Value (5 results)

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Show KM Value (5 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.8.1

0.019

-

32°C, pH 7.0

654618

1.3.8.5

0.001

-

recombinant enzyme, 32°C

656288

1.3.8.5

0.018

-

-

12302

2.3.1.19

0.0481

-

pH 7.5, 23°C

756087

2.3.1.19

0.0481

-

pH 7.5, 25°C

756087

1.3.8.5

2 entries

2.3.1.19

2 entries

References & Links

Literature References (9)

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Show Reference (9 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

12302

3988734

Purification and characterization of the 2-methyl branched-chain acyl-CoA dehydrogenase, an enzyme involved in NADH-dependent enoyl-CoA reduction in anaerobic mitochondria of the nematode, Ascaris suum

1985

Komuniecki, R.; Fekete, S.; Thissen-Parra, J.

J. Biol. Chem.

260

4770-4777

391203

6401712

Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria. Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase

1983

Ikeda, Y.; Dabrowski, C.; Tanaka, K.

J. Biol. Chem.

258

1066-1076

391252

2853820

2-Methyl branched-chain acyl-CoA dehydrogenase from rat liver

1988

Ikeda, Y.; Tanaka, K.

Methods Enzymol.

166

360-373

391254

6874697

Purification and characterization of 2-methyl-branched chain acyl coenzyme a dehydrogenase, an enzyme involved in the isoleucine and valine metabolism, from rat liver mitochondria

1983

Ikeda, Y.; Tanaka, K.

J. Biol. Chem.

258

9477-9487

486937

10629181

beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis

2000

Choi, K.H.; Heath, R.J.; Rock, C.O.

J. Bacteriol.

182

365-370

654618

12220177

Purification and characterization of two polymorphic variants of short chain acyl-CoA dehydrogenase reveal reduction of catalytic activity and stability of the Gly185Ser enzyme

2002

Nguyen, T.V.; Riggs, C.; Babovic-Vuksanovic, D.; Kim, Y.S.; Carpenter, J.F.; Burghardt, T.P.; Gregersen, N.; Vockley, J.

Biochemistry

41

11126-11133

656288

15574432

Convergent evolution of a 2-methylbutyryl-CoA dehydrogenase from isovaleryl-CoA dehydrogenase in Solanum tuberosum

2005

Goetzman, E.S.; Mohsen, A.W.; Prasad, K.; Vockley, J.

J. Biol. Chem.

280

4873-4879

756087

27940001

Utilization of multiple substrates by butyrate kinase from Listeria monocytogenes

2017

Sirobhushanam, S.; Galva, C.; Saunders, L.P.; Sen, S.; Jayaswal, R.; Wilkinson, B.J.; Gatto, C.

Biochim. Biophys. Acta

1862

283-290

756087

27940001

Utilization of multiple substrates by butyrate kinase from Listeria monocytogenes

2017

Sirobhushanam, S.; Galva, C.; Saunders, L.P.; Sen, S.; Jayaswal, R.; Wilkinson, B.J.; Gatto, C.

Biochim. Biophys. Acta

1862

283-290

756087

2 entries

Links to other databases for 2-methylbutanoyl-CoA

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Show Links (1 entry)