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Ligand isovaleryl-CoA

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

leucine metabolism

KEGG

Valine, leucine and isoleucine degradation

MetaCyc

acylsucrose biosynthesis (Solanum habrochaites), acylsucrose biosynthesis (Solanum pennellii), diacylsucrose biosynthesis (Solanum), hyperforin and adhyperforin biosynthesis, L-leucine degradation I, L-leucine degradation V (oxidative Stickland reaction), lupulone and humulone biosynthesis, monoacylsucrose biosynthesis (Solanum), odd iso-branched-chain fatty acid biosynthesis, T-2 toxin biosynthesis, triacylsucrose biosynthesis (Solanum) more

Show all BRENDA pathways known for isovaleryl-CoA

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (10 results)

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Show Natural Substrate (10 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.3.8.4

isovaleryl-CoA + 2,6-dichlorophenolindophenol = ?

692393

-

1.3.8.4

isovaleryl-CoA + acceptor = 3-methylcrotonyl-CoA + reduced acceptor

391204, 391201, 391206, 391209, 391211, 391214, 391220, 655248, 391199, 391203, 391205, 391207, 391208, 391210, 391215, 391216, 391213, 391219, 391218, 391212, 391217, 391200, 391202

-

1.3.8.4

isovaleryl-CoA + electron transfer protein = 3-methylcrotonoyl-CoA + reduced electron transfer protein

656288

-

1.3.8.4

isovaleryl-CoA + electron transfer protein = 3-methylcrotonyl-CoA + reduced electron transfer protein

654890, 656288

-

1.3.8.4

isovaleryl-CoA + electron-transfer flavoprotein = 3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein

724512

-

1.3.8.4

isovaleryl-CoA + FAD = 3-methylcrotonyl-CoA + FADH2

725099, 724826

-

1.3.8.4

6 entries

2.3.1.156

isovaleryl-CoA + malonyl-CoA = phloroisovalerophenone + CO2 + CoA

288683

-

2.3.1.180

isovaleryl-CoA + malonyl-[acyl-carrier protein] = 3-oxo-5-methylhexanoyl-[acyl-carrier protein] + CoA + CO2

703762

-

2.3.1.228

isovaleryl-CoA + S-adenosyl-L-methionine = CoA + S-methyl-5'-thioadenosine + N-isovaleryl-L-homoserine lactone

726371

-

2.3.1.300

3-methylbutanoyl-CoA + malonyl-[acyl-carrier protein] = ethyl-3-oxohexanoyl-[acyl-carrier-protein] + CoA + CO2

761371

-

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

1.2.4.4

2-oxoisocaproate + NAD+ + CoA = 3-methylbutanoyl-CoA + CO2 + NADH + H+

-

-

Substrate in Enzyme-catalyzed Reactions (39 results)

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Show Substrate (39 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.11.18

isovaleryl-CoA + 2-oxoglutarate + O2 = ?

658428, 674512

-

1.3.8.4

isovaleryl-CoA + 2,6-dichlorophenolindophenol = ?

692393

-

1.3.8.4

isovaleryl-CoA + acceptor = 3-methylcrotonyl-CoA + reduced acceptor

391204, 391201, 391206, 391209, 391211, 391214, 391220, 655248, 391199, 391203, 391205, 391207, 391208, 391210, 391215, 391216, 391213, 391219, 391218, 685654, 391212, 689020, 391217, 391200, 391202

-

1.3.8.4

isovaleryl-CoA + electron transfer protein = 3-methylcrotonoyl-CoA + reduced electron transfer protein

656288, 742009

-

1.3.8.4

isovaleryl-CoA + electron transfer protein = 3-methylcrotonyl-CoA + reduced electron transfer protein

654890, 656288

-

1.3.8.4

isovaleryl-CoA + electron-transfer flavoprotein = 3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein

391201, 724512

-

1.3.8.4

isovaleryl-CoA + FAD = 3-methylcrotonyl-CoA + FADH2

725099, 724826

-

1.3.8.4

isovaleryl-CoA + phenazine methosulfate = 3-methylcrotonyl-CoA + reduced phenazine methosulfate

391201, 655248, 391203

-

1.3.8.4

7 entries

1.3.8.5

isovaleryl-CoA + phenazine methosulfate = ?

391203

-

1.3.8.6

isovaleryl-CoA + acceptor = ? + reduced acceptor

391408

-

2.3.1.13

isovaleryl-CoA + glycine = CoA + N-isovalerylglycine

486272, 486270

-

2.3.1.156

isovaleryl-CoA + 3 malonyl-CoA = phloroisovalerophenone + 3 CO2 + 4 CoA

737031

-

2.3.1.156

isovaleryl-CoA + malonyl-CoA = phloroisovalerophenone + CO2 + CoA

706171, 288683, 288684

-

2.3.1.156

2 entries

2.3.1.168

isovaleryl-CoA + dihydrolipoamide = CoA + S-isovaleryldihydrolipoamide

644839, 644848, 644842

-

2.3.1.180

isovaleryl-CoA + malonyl-[acyl-carrier protein] = 3-oxo-5-methyl-hexanoyl-[acyl-carrier protein] + CoA + CO2

660466, 486939, 486937

-

2.3.1.180

isovaleryl-CoA + malonyl-[acyl-carrier protein] = 3-oxo-5-methylhexanoyl-[acyl-carrier protein] + CoA + CO2

703762

-

2.3.1.180

2 entries

2.3.1.186

isovaleryl-CoA + pseudotropine = CoA + O-isovalerylpseudotropine

682287

-

2.3.1.19

isopentanoyl-CoA + phosphate = isopentanoylphosphate + CoA

486470

-

2.3.1.19

isovaleryl-CoA + phosphate = CoA + isovaleryl phosphate

756087

-

2.3.1.19

isovaleryl-CoA + phosphate = isovaleryl phosphate + CoA

756087

-

2.3.1.19

3 entries

2.3.1.220

3 malonyl-CoA + isovaleryl-CoA = 4 CoA + phloroisovalerophenone + 3 CO2

487479

-

2.3.1.228

isovaleryl-CoA + S-adenosyl-L-methionine = CoA + S-methyl-5'-thioadenosine + N-isovaleryl-L-homoserine lactone

726371, 737133

-

2.3.1.233

isovaleryl-CoA = 4-hydroxy-6-isobutyl-2-pyrone + 4-hydroxy-6-(4'-methyl-2'-oxopentyl)-2-pyrone + CoA + CO2 + H2O

729961

-

2.3.1.300

3-methylbutanoyl-CoA + malonyl-[acyl-carrier protein] = ethyl-3-oxohexanoyl-[acyl-carrier-protein] + CoA + CO2

761371

-

2.3.1.300

isovaleryl-CoA + malonyl-[acyl-carrier protein] = ? + CoA + CO2

761373, 761098, 762418

-

2.3.1.300

2 entries

2.3.1.39

isovaleryl-CoA + an [acyl-carrier protein] = CoA + isovaleryl-[acyl carrier protein]

755871

-

2.3.1.47

isovaleryl-CoA + L-arginine = N-[(4S)-4-amino-7-methyl-5-oxooctyl]guanidine + CO2 + CoA

758497

-

2.3.1.7

isovaleryl-CoA + carnitine = isovalerylcarnitine + CoASH

487407

-

2.3.1.71

isovaleryl-CoA + glycine = CoA + N-isovalerylglycine

486269, 487440, 487441, 486265

-

2.3.1.74

isovaleryl-CoA + malonyl-CoA = ?

672501

-

2.3.1.74

malonyl-CoA + isovaleryl-CoA = ?

487480, 676378

-

2.3.1.74

2 entries

2.3.1.85

3-methylbutanoyl-CoA + an [acyl-carrier protein] = CoA + 3-methylbutanoyl-[acyl-carrier protein]

755686

-

2.3.1.93

3-methylbutyryl-CoA + 13-hydroxylupanine = CoA + 13-(3-methylbutyryl)oxylupanine

487720

-

2.3.1.95

isovaleryl-CoA + malonyl-CoA = bisnoryangonin-type and p-coumaroyltriacetic acid lactone-type pyrones + CoA + CO2

487730

-

3.1.2.20

isovaleryl-CoA + H2O = CoA + isovalerate

690932

-

5.4.99.13

isovaleryl-CoA = pivalyl-CoA

748193, 748200

-

5.4.99.64

isovaleryl-CoA = ?

738677

-

5.4.99.64

isovaleryl-CoA = pentanoyl-CoA

738677

-

5.4.99.64

2 entries

6.2.1.13

ADP + phosphate + isovaleryl-CoA = ATP + isovalerate + CoA

744820

-

Product in Enzyme-catalyzed Reactions (15 results)

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Show Product (15 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.25

4-methyl-2-oxopentanoate + CoA + NAD+ = 3-methyl-butanoyl-CoA + CO2 + NADH

-

-

1.2.4.4

2-oxoisocaproate + NAD+ + CoA = 3-methylbutanoyl-CoA + CO2 + NADH + H+

-

-

1.2.4.4

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

, 349084, 349076

-

1.2.7.7

2-ketoisohexanoate + CoA + benzyl viologen = isopentanoyl-CoA + CO2 + reduced benzyl viologen

-

-

1.2.7.7

2-ketoisocaproate + CoA + oxidized ferredoxin = S-(3-methylbutanoyl)-CoA + CO2 + reduced ferredoxin

-

-

1.2.4.4

2 entries

1.2.7.7

2 entries

1.2.7.8

2-ketoisocaproate + CoA + oxidized ferredoxin = CO2 + reduced ferredoxin + isovaleryl-CoA

-

-

1.3.1.8

3-methyl-crotonyl-CoA + NADPH = 3-methylbutanoyl-CoA + NADP+

-

-

2.3.1.7

isovalerylcarnitine + CoASH = isovaleryl-CoA + carnitine

-

-

2.8.3.1

acetyl-CoA + isovalerate = acetate + isovaleryl-CoA

-

-

2.8.3.9

isopentanoate + acetoacetyl-CoA = isopentanoyl-CoA + acetoacetate

-

-

6.2.1.13

ATP + isopentanioate + CoA = ADP + phosphate + isovaleryl-CoA

-

-

6.2.1.13

ATP + isovalerate + CoA = ADP + phosphate + isovaleryl-CoA

-

-

6.2.1.13

2 entries

6.2.1.2

ATP + isopentanoate = AMP + diphosphate + isopentanoyl-CoA

-

-

6.2.1.44

ATP + 3-methylbutanoate + CoA = AMP + diphosphate + 3-methylbutanoyl-CoA

-

-

6.2.1.B11

ATP + isovalerate + CoA = ADP + phosphate + isovaleryl-CoA

-

-

Inhibitor in Enzyme-catalyzed Reactions (8 results)

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Show Inhibitors (8 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.2.4.4

-

349045

-

1.2.4.4

competitive with CoA

349062

-

1.2.4.4

-

349079

-

1.2.4.4

0.2 mM. 56% inhibition

349057, 349063

-

1.2.4.4

4 entries

2.3.1.1

about 50% residual activity at 2.5 mM

735706

-

2.7.11.4

-

349056, 640579

-

3.1.3.16

-

134616, 134617

-

3.1.3.52

-

134655

-

3D Structure of Enzyme-Ligand-Complex (PDB) (1 result)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (1 entry)

EC NUMBER

ENZYME 3D STRUCTURE

5.4.99.2

5cjv, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (33 results)

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Show Turnover Number (33 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.3.8.4

0.17

-

mutant IVD G375E, pH 7.4, 37°C

724512

1.3.8.4

0.283

-

purified V342A mutant, electron acceptor: dichlorophenol indophenol

391212

1.3.8.4

0.32

-

mutabt IVD E254G/G375E, pH 7.4, 37°C

724512

1.3.8.4

0.733

-

purified R382L mutant, electron acceptor: dichlorophenol indophenol

391212

1.3.8.4

0.817

-

purified V342A mutant, electron acceptor: electron-transferring flavoprotein

391212

1.3.8.4

0.98

-

per tetramer, recombinant enzyme, 32°C

656288

1.3.8.4

1.5

-

wild-type enzyme, pH 7.4, 37°C

724512

1.3.8.4

2

-

purified R382L mutant, electron acceptor: electron-transferring flavoprotein

391212

1.3.8.4

2.2

-

purified A282V mutant, electron acceptor: electron-transferring flavoprotein

391212

1.3.8.4

2.37

-

using recombinant enzyme, electron acceptor: electron-transferring flavoprotein

391218

1.3.8.4

2.82

-

purified A282V mutant, electron acceptor: dichlorophenol indophenol

391212

1.3.8.4

8.8

-

purified wild-type enzyme, electron acceptor: electron-transferring flavoprotein

391212

1.3.8.4

10

-

purified wild-type enzyme, electron acceptor: dichlorophenol indophenol

391212

2.3.1.180

0.018

-

10°C

703762

2.3.1.180

0.12

-

30°C

703762

2.3.1.180

15.5

30.5

pH 7.0, 30°C, recombinant enzyme

660466

2.3.1.19

1043.4

-

pH 7.5, 23°C

756087

2.3.1.19

1043.4

-

pH 7.5, 25°C

756087

1.3.8.4

13 entries

2.3.1.180

3 entries

2.3.1.19

2 entries

2.3.1.228

0.021

-

pH 7.3, temperature not specified in the publication

737133

2.3.1.300

0.018

-

pH 7, 10°C

761098

2.3.1.300

0.12

-

pH 7, 30°C

761098

2.3.1.300

2 entries

2.3.1.85

7.2

-

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

755686

3.1.2.20

30

-

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

690932

5.4.99.13

0.0036

-

recombinant mutant F598I, pH 7.5, 37°C

748193

5.4.99.13

0.0084

-

recombinant mutant F598L, pH 7.5, 37°C

748193

5.4.99.13

0.014

-

recombinant engineered PCM mutant, pH 7.5, 37°C

748193

5.4.99.13

0.015

-

recombinant mutant F598V, pH 7.5, 37°C

748193

5.4.99.13

0.022

-

recombinant mutant F598A, pH 7.5, 37°C

748193

5.4.99.13

0.023

-

recombinant engineered PCM-F mutant, pH 7.5, 37°C

748193

5.4.99.13

0.062

-

recombinant wild-type enzyme, pH 7.5, 37°C

748193

5.4.99.64

0.009

-

pH 6.6, 30°C, mutant enzyme I90A (mutation in subunit HcmA)

738677

5.4.99.64

0.0093

-

pH 6.6, 30°C, mutant enzyme I90V (mutation in subunit HcmA)

738677

5.4.99.64

0.011

-

pH 6.6, 30°C, wild-type enzyme

738677

5.4.99.13

7 entries

5.4.99.64

3 entries

K_M Value (61 results)

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Show KM Value (61 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.8.4

0.001

-

pH 8.0, 30°C, calculated per monomer

742009

1.3.8.4

0.0013

-

per tetramer, recombinant enzyme, 32°C

656288

1.3.8.4

0.0015

-

wild-type

391220

1.3.8.4

0.0023

-

pH 7.5, 30°C, recombinant enzyme

692393

1.3.8.4

0.0025

-

-

391218

1.3.8.4

0.0028

-

purified enzyme V342A

391212

1.3.8.4

0.0028

-

purified V342A mutant, electron acceptor: electron-transferring flavoprotein

391212

1.3.8.4

0.0029

-

wild-type enzyme, pH 7.4, 37°C

724512

1.3.8.4

0.0031

-

mutabt IVD E254G/G375E, pH 7.4, 37°C

724512

1.3.8.4

0.0031

-

purified wild-type enzyme, electron acceptor: electron-transferring flavoprotein

391212

1.3.8.4

0.0038

-

mutant IVD G375E, pH 7.4, 37°C

724512

1.3.8.4

0.0042

-

purified enzyme

391215

1.3.8.4

0.0045

-

purified R382L mutant, electron acceptor: dichlorophenol indophenol

391212

1.3.8.4

0.006

-

partially purified enzyme

391215

1.3.8.4

0.0063

-

sonic supernatant

391204

1.3.8.4

0.0069

-

purified R382L mutant, electron acceptor: electron-transferring flavoprotein

391212

1.3.8.4

0.0113

-

-

391204

1.3.8.4

0.0113

-

purified enzyme in the absence of electron transfer agents

391204

1.3.8.4

0.013

-

whole sonicate

391204

1.3.8.4

0.0132

-

-

391204

1.3.8.4

0.0132

-

purified enzyme with electron-transferring flavoprotein and dichlorophenol indophenol, reaction terminated with KMnO4/HCl

391204

1.3.8.4

0.014

-

-

391201

1.3.8.4

0.0203

-

mutant R387K

391220

1.3.8.4

0.0208

-

-

391204

1.3.8.4

0.0208

-

purified enzyme with phenazine methosulfate and dichlorophenol indophenol, reaction terminated with KMnO4/HCl

391204

1.3.8.4

0.024

-

purified V342A mutant, electron acceptor: dichlorophenol indophenol

391212

1.3.8.4

0.027

-

purified A282V mutant, electron acceptor: electron-transferring flavoprotein

391212

1.3.8.4

0.0296

-

purified wild-type enzyme, electron acceptor: dichlorophenol indophenol

391212

1.3.8.4

0.033

-

with phenazine methosulfate as an artificial electron acceptor

391200, 391202

1.3.8.4

0.047

-

-

391216

1.3.8.4

0.05

-

-

391219

1.3.8.4

0.0756

-

mutant R387A

391220

1.3.8.4

0.125

-

pH 8.0, 37°C

724826

1.3.8.4

0.195

-

mutant R387Q

391220

1.3.8.4

0.41

-

purified A282V mutant, electron acceptor: dichlorophenol indophenol

391212

1.3.8.4

0.9

-

mutant R387E

391220

2.3.1.13

73.3

-

-

486272

2.3.1.13

124

-

-

486272

1.3.8.4

36 entries

2.3.1.13

2 entries

2.3.1.156

0.004

-

-

288684

2.3.1.168

0.05

-

pH 7.4, 37°C

644839

2.3.1.180

0.0053

-

30°C

703762

2.3.1.180

0.013

0.014

pH 7.0, 30°C, recombinant enzyme

660466

2.3.1.180

0.0169

-

10°C

703762

2.3.1.19

0.0532

-

pH 7.5, 23°C

756087

2.3.1.19

0.0532

-

pH 7.5, 25°C

756087

2.3.1.180

3 entries

2.3.1.19

2 entries

2.3.1.228

0.007

-

pH 7.3, temperature not specified in the publication

737133

2.3.1.300

0.0053

-

pH 7, 30°C

761098

2.3.1.300

0.0169

-

pH 7, 10°C

761098

2.3.1.300

2 entries

2.3.1.74

0.008

-

-

672501

2.3.1.85

0.00206

-

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

755686

3.1.2.20

0.014

-

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

690932

5.4.99.13

0.2

-

recombinant engineered PCM-F mutant, pH 7.5, 37°C

748193

5.4.99.13

0.37

-

recombinant engineered PCM mutant, pH 7.5, 37°C

748193

5.4.99.13

0.51

-

recombinant mutant F598A, pH 7.5, 37°C

748193

5.4.99.13

0.56

-

recombinant mutant F598L, pH 7.5, 37°C

748193

5.4.99.13

0.58

-

recombinant mutant F598I, pH 7.5, 37°C

748193

5.4.99.13

0.62

-

recombinant mutant F598V, pH 7.5, 37°C

748193

5.4.99.13

1.4

-

recombinant wild-type enzyme, pH 7.5, 37°C

748193

5.4.99.64

0.147

-

pH 6.6, 30°C, mutant enzyme I90A (mutation in subunit HcmA)

738677

5.4.99.64

0.288

-

pH 6.6, 30°C, wild-type enzyme

738677

5.4.99.64

0.329

-

pH 6.6, 30°C, mutant enzyme I90V (mutation in subunit HcmA)

738677

5.4.99.13

7 entries

5.4.99.64

3 entries

K_i Value (4 results)

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Show KI Value (4 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.2.4.4

0.0082

-

reaction with 3-methyl-2-oxobutanoate

349079

1.2.4.4

0.0101

-

reaction with DL-3-methyl-2-oxopentanoate

349079

1.2.4.4

0.0136

-

reaction with 4-methyl-2-oxopentanoate

349079

1.2.4.4

3 entries

2.3.1.1

1.9

-

at pH 8.5 and 30°C

735706

References & Links

Literature References (90)

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Show Reference (90 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

134616

-

Mitochondrial protein phosphatases

1987

Reed, L.J.; Damuni, Z.

Adv. Protein Phosphatases

4

59-76

134617

3031043

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