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Ligand ferrocenium hexafluorophosphate

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

1.3.8.11

cyclohexane-1-carbonyl-CoA + ferricenium hexafluorophosphate = cyclohex-1-ene-1-carbonyl-CoA + ferrocenium hexafluorophosphate

725285

-

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

1.3.8.11

cyclohexane-1-carbonyl-CoA + ferricenium hexafluorophosphate = cyclohex-1-ene-1-carbonyl-CoA + ferrocenium hexafluorophosphate

0

-

Substrate in Enzyme-catalyzed Reactions (42 results)

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Show Substrate (42 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.10

D-galactose + ferricenium hexafluorophosphate = 2-dehydro-D-galactose + ferrocenium hexafluorophosphate

699076

-

1.1.3.10

D-glucose + ferricenium hexafluorophosphate = 2-dehydro-D-glucose + ferrocenium hexafluorophosphate

699076

-

1.1.3.10

D-glucose + ferricenium hexafluorophosphate = ?

724062

-

1.1.3.10

ferricenium hexafluorophosphate + O2 = ? + H2O2

699081

-

1.1.3.10

D-galactose + ferrocenium hexafluorophosphate = 2-dehydro-D-galactose + ferrocene

711984

-

1.1.3.10

D-glucose + ferrocenium hexafluorophosphate = 2-dehydro-D-glucose + ferrocene

711984

-

1.1.3.10

6 entries

1.1.5.9

D-glucose + ferricenium hexafluorophosphate = D-glucono-1,5-lactone + ferrocenium hexafluorophosphate

725906

-

1.1.99.18

cellulose + ferrocenium hexafluorophosphate = cellobiono-1,5-lactone + ferricenium hexafluorophosphate

724019

-

1.1.99.29

beta-lactose + ferricenium hexafluorophosphate = ?

686685

-

1.1.99.29

D-arabinose + ferricenium hexafluorophosphate = ?

686685

-

1.1.99.29

D-maltose + ferricenium hexafluorophosphate = ?

686685

-

1.1.99.29

D-maltotriose + ferricenium hexafluorophosphate = ?

686685

-

1.1.99.29

D-xylose + ferricenium hexafluorophosphate = ?

686685

-

1.1.99.29

gentiobiose + ferricenium hexafluorophosphate = ?

686685

-

1.17.99.8

(+)-p-menth-1-ene + H2O + ferrocenium hexafluorophosphate = [(4S)-4-(propan-2-yl)cyclohex-1-en-1-yl]methanol + reduced ferrocenium hexafluorophosphate

754177

-

1.17.99.8

(R)-(-)-alpha-phellandrene + ferrocenium hexafluorophosphate = ? + reduced ferrocenium hexafluorophosphate

754177

-

1.17.99.8

(R)-limonene + H2O + ferrocenium hexafluorophosphate = (+)-perillyl alcohol + reduced ferrocenium hexafluorophosphate

754177

-

1.17.99.8

(S)-limonene + H2O + ferrocenium hexafluorophosphate = (-)-perillyl alcohol + reduced ferrocenium hexafluorophosphate

754177

-

1.17.99.8

alpha-terpinene + ferrocenium hexafluorophosphate = ? + reduced ferrocenium hexafluorophosphate

754177

-

1.17.99.8

limonene + H2O + ferrocenium hexafluorophosphate = perillyl alcohol + reduced ferrocenium hexafluorophosphate

754177

-

1.17.99.8

terpinolene + ferrocenium hexafluorophosphate = ? + reduced ferrocenium hexafluorophosphate

754177

-

1.3.8.10

cyclohex-1,5-diene-1-carbonyl-CoA + ferricenium hexafluorophosphate = benzoyl-CoA + ferrocenium hexafluorophosphate

742783

-

1.3.8.10

cyclohex-1-ene-1-carbonyl-CoA + ferricenium hexafluorophosphate = cyclohex-1,5-diene-1-carbonyl-CoA + ferrocenium hexafluorophosphate

725285, 742783

-

1.3.8.10

cyclohexa-1,5-diene-1-carbonyl-CoA + ferricenium hexafluorophosphate = benzoyl-CoA + ferrocenium hexafluorophosphate

725285

-

1.3.8.11

cyclohex-3-ene-1-carboxyl-CoA + ferricenium hexafluorophosphate = cyclohexa-1,3-diene-1-carboxyl-CoA + ferrocenium hexafluorophosphate

742783

-

1.3.8.11

cyclohexane-1-carbonyl-CoA + ferricenium hexafluorophosphate = cyclohex-1-ene-1-carbonyl-CoA + ferrocenium hexafluorophosphate

725285, 742783

-

1.3.8.12

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

763257

-

1.3.8.12

succinyl-CoA + ferrocenium hexafluorophosphate = fumaryl-CoA + ferricenium hexafluorophosphate

763257

-

1.1.99.29

6 entries

1.17.99.8

7 entries

1.3.8.10

3 entries

1.3.8.11

2 entries

1.3.8.12

2 entries

1.3.8.3

(R)-2-benzylsuccinyl-CoA + ferricenium hexafluorophosphate = (E)-2-benzylidenesuccinyl-CoA + ferrocenium hexafluorophosphate

636487

-

1.3.8.6

glutaryl-CoA + ferricenium hexafluorophosphate = crotonyl-CoA + CO2 + ferrocenium hexafluorophosphate

686426

-

1.3.8.6

glutaconyl-CoA + ferrocenium hexafluorophosphate = crotonyl-CoA + CO2 + ferricenium hexafluorophosphate

391417, 685122

-

1.3.8.7

decanoyl-CoA + ferricenium hexafluorophosphate = 2-decenoyl-CoA + ferrocenium hexafluorophosphate

391367

-

1.3.8.7

furylpropionyl-CoA + ferricenium hexafluorophosphate = furylacryloyl-CoA + ferrocenium hexafluorophosphate

391367

-

1.3.8.7

hexanoyl-CoA + ferricenium hexafluorophosphate = trans-hex-2-enoyl-CoA + ferrocenium hexafluorophosphate

391367

-

1.3.8.7

indolepropionyl-CoA + ferricenium hexafluorophosphate = indoleacryloyl-CoA + ferrocenium hexafluorophosphate

391367, 391372

-

1.3.8.7

octanoyl-CoA + ferricenium hexafluorophosphate = 2-octenoyl-CoA + ferrocenium hexafluorophosphate

391313

-

1.3.8.7

phenylpropionyl-CoA + ferricenium hexafluorophosphate = ? + reduced ferricenium hexafluorophosphate

689014, 689196

-

1.3.8.7

[4-(dimethylamino)phenyl]propionyl-CoA + ferricenium hexafluorophosphate = 4-(dimethylamino)cinnamoyl-CoA + ferrocenium hexafluorophosphate

391367

-

1.3.8.7

decanoyl-CoA + ferrocenium hexafluorophosphate = trans-dec-2-enoyl-CoA + reduced ferrocenium hexafluorophosphate

391367

-

1.3.8.7

hexanoyl-CoA + ferrocenium hexafluorophosphate = trans-hex-2-enoyl-CoA + reduced ferrocenium hexafluorophosphate

391367

-

1.3.8.6

2 entries

1.3.8.7

9 entries

1.5.8.2

trimethylamine + H2O + ferricenium hexafluorophosphate = dimethylamine + formaldehyde + ferrocenium hexafluorophosphate

393888

-

1.5.8.4

N,N-dimethylglycine + ferricenium hexafluorophosphate + H2O = sarcosine + formaldehyde + reduced ferricenium hexafluorophosphate

699373

-

Product in Enzyme-catalyzed Reactions (21 results)

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Show Product (21 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.10

D-galactose + ferricenium hexafluorophosphate = 2-dehydro-D-galactose + ferrocenium hexafluorophosphate

0

-

1.1.3.10

D-glucose + ferricenium hexafluorophosphate = 2-dehydro-D-glucose + ferrocenium hexafluorophosphate

0

-

1.1.3.10

2 entries

1.1.5.9

D-glucose + ferricenium hexafluorophosphate = D-glucono-1,5-lactone + ferrocenium hexafluorophosphate

0

-

1.1.99.18

cellulose + ferrocenium hexafluorophosphate = cellobiono-1,5-lactone + ferricenium hexafluorophosphate

0

-

1.3.8.10

cyclohex-1,5-diene-1-carbonyl-CoA + ferricenium hexafluorophosphate = benzoyl-CoA + ferrocenium hexafluorophosphate

0

-

1.3.8.10

cyclohex-1-ene-1-carbonyl-CoA + ferricenium hexafluorophosphate = cyclohex-1,5-diene-1-carbonyl-CoA + ferrocenium hexafluorophosphate

0

-

1.3.8.10

cyclohexa-1,5-diene-1-carbonyl-CoA + ferricenium hexafluorophosphate = benzoyl-CoA + ferrocenium hexafluorophosphate

0

-

1.3.8.11

cyclohex-3-ene-1-carboxyl-CoA + ferricenium hexafluorophosphate = cyclohexa-1,3-diene-1-carboxyl-CoA + ferrocenium hexafluorophosphate

0

-

1.3.8.11

cyclohexane-1-carbonyl-CoA + ferricenium hexafluorophosphate = cyclohex-1-ene-1-carbonyl-CoA + ferrocenium hexafluorophosphate

0

-

1.3.8.12

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

0

-

1.3.8.12

succinyl-CoA + ferrocenium hexafluorophosphate = fumaryl-CoA + ferricenium hexafluorophosphate

0

-

1.3.8.10

3 entries

1.3.8.11

2 entries

1.3.8.12

2 entries

1.3.8.3

(R)-2-benzylsuccinyl-CoA + ferricenium hexafluorophosphate = (E)-2-benzylidenesuccinyl-CoA + ferrocenium hexafluorophosphate

636487

-

1.3.8.6

glutaconyl-CoA + ferrocenium hexafluorophosphate = crotonyl-CoA + CO2 + ferricenium hexafluorophosphate

0

-

1.3.8.6

glutaryl-CoA + ferricenium hexafluorophosphate = crotonyl-CoA + CO2 + ferrocenium hexafluorophosphate

0

-

1.3.8.7

decanoyl-CoA + ferricenium hexafluorophosphate = 2-decenoyl-CoA + ferrocenium hexafluorophosphate

0

-

1.3.8.7

furylpropionyl-CoA + ferricenium hexafluorophosphate = furylacryloyl-CoA + ferrocenium hexafluorophosphate

391367

-

1.3.8.7

hexanoyl-CoA + ferricenium hexafluorophosphate = trans-hex-2-enoyl-CoA + ferrocenium hexafluorophosphate

0

-

1.3.8.7

indolepropionyl-CoA + ferricenium hexafluorophosphate = indoleacryloyl-CoA + ferrocenium hexafluorophosphate

391367, 391372

-

1.3.8.7

octanoyl-CoA + ferricenium hexafluorophosphate = 2-octenoyl-CoA + ferrocenium hexafluorophosphate

391313

-

1.3.8.7

[4-(dimethylamino)phenyl]propionyl-CoA + ferricenium hexafluorophosphate = 4-(dimethylamino)cinnamoyl-CoA + ferrocenium hexafluorophosphate

391367

-

1.3.8.6

2 entries

1.3.8.7

6 entries

1.5.8.2

trimethylamine + H2O + ferricenium hexafluorophosphate = dimethylamine + formaldehyde + ferrocenium hexafluorophosphate

393888

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (20 results)

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Show Turnover Number (20 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.3.10

1.7

-

pH 8.0, 30°C, recombinant enzyme

724062

1.1.3.10

2.9

-

mutant enzyme F454A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

4.5

-

mutant enzyme F454P, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

5.4

-

mutant enzyme F454A/S455A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

6.6

-

wild type enzyme, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

7.3

-

mutant enzyme F454N, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

7.3

-

mutant enzyme Y456W, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

17

-

mutant enzyme H450Q, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

67

-

mutant enzyme F454P, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

74

-

mutant enzyme F454A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

110

-

mutant enzyme F454A/S455A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

158

-

pH 8.0, 30°C, recombinant enzyme

724062

1.1.3.10

210

-

wild type enzyme, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

228

-

substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5

699081

1.1.3.10

400

-

mutant enzyme Y456W, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

420

-

mutant enzyme F454N, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

470

-

mutant enzyme H450Q, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

549

-

substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 8.0

699081

1.1.3.10

18 entries

1.3.8.6

7.5

-

-

391417

1.3.8.7

18.3

-

medium chain acyl-CoA dehydrogenase from kidney

391313

K_M Value (33 results)

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Show KM Value (33 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.3.10

0.015

-

mutant enzyme F454A/S455A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

0.016

-

mutant enzyme F454A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

0.023

-

mutant enzyme F454P, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

0.025

-

mutant enzyme F454N, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

0.041

-

mutant enzyme Y456W, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

0.049

-

mutant enzyme H450Q, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

0.092

-

mutant enzyme V546C/T169G/L537W, at pH 6.5 and 30°C

699076

1.1.3.10

0.092

-

V546C/T169G/L537W mutant, substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5

699076

1.1.3.10

0.1

-

wild type enzyme, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

0.14

-

mutant enzyme F454P, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

0.15

-

mutant enzyme V546C/E542K, at pH 6.5 and 30°C

699076

1.1.3.10

0.15

-

V546C/E542K mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5

699076

1.1.3.10

0.15

-

mutant enzyme F454A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

0.22

-

mutant enzyme V546C/T169G/L537W, at pH 6.5 and 30°C

699076

1.1.3.10

0.22

-

V546C/T169G/L537W mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5

699076

1.1.3.10

0.24

-

mutant enzyme Y456W, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

0.28

-

mutant enzyme F454A/S455A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

0.29

-

substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 8.0

699081

1.1.3.10

0.31

-

mutant enzyme V546C/T169G, at pH 6.5 and 30°C

699076

1.1.3.10

0.31

-

V546C/T169G mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5

699076

1.1.3.10

0.33

-

substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5

699081

1.1.3.10

0.35

-

mutant enzyme F454N, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

0.38

-

mutant enzyme H450Q, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

0.4

-

wild type enzyme, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

711984

1.1.3.10

0.5

-

mutant enzyme V546C/T169G, at pH 6.5 and 30°C

699076

1.1.3.10

0.5

-

V546C/T169G mutant, substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5

699076

1.1.3.10

0.67

-

pH 8.0, 30°C, recombinant enzyme

724062

1.1.3.10

1.06

-

V546C/E542K mutant, substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the chromogen, 30°C, pH 6.5

699076

1.1.3.10

1.12

-

pH 8.0, 30°C, recombinant enzyme

724062

1.1.3.10

29 entries

1.1.99.29

0.12

-

at 30°C with 25 mM glucose as susbtrate

686685

1.3.8.7

0.0099

-

substrate indolepropionyl-CoA

391367

1.3.8.7

0.055

-

-

391313

1.3.8.7

0.069

-

substrate octanoyl-CoA

391367

1.3.8.7

3 entries

References & Links

Literature References (22)

top print hide

Show Reference (22 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

391313

2363500

An acyl-coenzyme A dehydrogenase assay utilizing the ferricenium ion

1990

Lehmann, T.C.; Hale, D.E.; Bhala, A.; Thorpe, C.

Anal. Biochem.

186

280-284

391367

7578106

Recombinant human liver medium-chain acyl-CoA dehydrogenase: purification, characterization, and the mechanism of interactions with functionally diverse C8-CoA molecules

1995

Peterson, K.L.; Sergienko, E.E.; Wu, Y.; Kumar, N.R.; Strauss, A.W.; Oleson, A.E.; Muhonen, W.W.; Shabb, J.B.; Srivastava, D.K.

Biochemistry

34

14942-14953

391372

9521671

Energetics of two-step binding of a chromophoric reaction product, trans-3-indoleacryloyl-CoA, to medium-chain acyl-coenzyme-A dehydrogenase

1998

Qin, L.; Srivastava, D.K.

Biochemistry

37

3499-3508

391417

10985795

Proton abstraction reaction, steady-state kinetics, and oxidation-reduction potential of human glutaryl-CoA dehydrogenase

2000

Dwyer, T.M.; Rao, K.S.; Goodman, S.I.; Frerman, F.E.

Biochemistry

39

11488-11499

393888

8188674

Assembly of redox centers in the trimethylamine dehydrogenase of bacterium W3A1. Properties of the wild-type enzyme and a C30A mutant expressed from a cloned gene in Escherichia coli

1994

Scrutton, N.S.; Packman, L.C.; Mathews, F.S.; Rohlfs, R.J.; Hille, R.

J. Biol. Chem.

269

13942-13950

636487

12420174

(R)-Benzylsuccinyl-CoA dehydrogenase of Thauera aromatica, an enzyme of the anaerobic toluene catabolic pathway

2002

Leutwein, C.; Heider, J.

Arch. Microbiol.

178

517-524

685122

18020372

The effect of a Glu370Asp mutation in glutaryl-CoA dehydrogenase on proton transfer to the dienolate intermediate

2007

Rao, K.S.; Fu, Z.; Albro, M.; Narayanan, B.; Baddam, S.; Lee, H.J.; Kim, J.J.; Frerman, F.E.

Biochemistry

46

14468-14477

686426

18177371

Identification and analysis of a glutaryl-CoA dehydrogenase-encoding gene and its cognate transcriptional regulator from Azoarcus sp. CIB

2008

Blazquez, B.; Carmona, M.; Garcia, J.L.; Diaz, E.

Environ. Microbiol.

10

474-482

686685

17227387

Properties of pyranose dehydrogenase purified from the litter-degrading fungus Agaricus xanthoderma

2007

Kujawa, M.; Volc, J.; Halada, P.; Sedmera, P.; Divne, C.; Sygmund, C.; Leitner, C.; Peterbauer, C.; Haltrich, D.

FEBS J.

274

879-894

689014

17540595

Equine biochemical multiple acyl-CoA dehydrogenase deficiency (MADD) as a cause of rhabdomyolysis

2007

Westermann, C.M.; de Sain-van der Velden, M.G.; van der Kolk, J.H.; Berger, R.; Wijnberg, I.D.; Koeman, J.P.; Wanders, R.J.; Lenstra, J.A.; Testerink, N.; Vaandrager, A.B.; Vianey-Saban, C.; Acquaviva-Bourdain, C.; Dorland, L.

Mol. Genet. Metab.

91

362-369

689196

18406615

Acquired multiple acyl-CoA dehydrogenase deficiency in 10 horses with atypical myopathy

2008

Westermann, C.M.; Dorland, L.; Votion, D.M.; de Sain-van der Velden, M.G.; Wijnberg, I.D.; Wanders, R.J.; Spliet, W.G.; Testerink, N.; Berger, R.; Ruiter, J.P.; van der Kolk, J.H.

Neuromuscul. Disord.

18

355-364

699076

19095017

Engineering of pyranose 2-oxidase: improvement for biofuel cell and food applications through semi-rational protein design

2009

Spadiut, O.; Pisanelli, I.; Maischberger, T.; Peterbauer, C.; Gorton, L.; Chaiyen, P.; Haltrich, D.

J. Biotechnol.

139

250-257

699081

19501263

Pyranose 2-oxidase from Phanerochaete chrysosporium--expression in E. coli and biochemical characterization

2009

Pisanelli, I.; Kujawa, M.; Spadiut, O.; Kittl, R.; Halada, P.; Volc, J.; Mozuch, M.D.; Kersten, P.; Haltrich, D.; Peterbauer, C.

J. Biotechnol.

142

97-106

699373

18937046

Molecular basis of dimethylglycine dehydrogenase deficiency associated with pathogenic variant H109R

2008

McAndrew, R.P.; Vockley, J.; Kim, J.J.

J. Inherit. Metab. Dis.

31

761-768

711984

20528921

Importance of the gating segment in the substrate-recognition loop of pyranose 2-oxidase

2010

Spadiut, O.; Tan, T.C.; Pisanelli, I.; Haltrich, D.; Divne, C.

FEBS J.

277

2892-2909

724019

22729546

Characterization of the two Neurospora crassa cellobiose dehydrogenases and their connection to oxidative cellulose degradation

2012

Sygmund, C.; Kracher, D.; Scheiblbrandner, S.; Zahma, K.; Felice, A.K.; Harreither, W.; Kittl, R.; Ludwig, R.

Appl. Environ. Microbiol.

78

6161-6171

724062

21968652

Heterologous expression and biochemical characterization of novel pyranose 2-oxidases from the ascomycetes Aspergillus nidulans and Aspergillus oryzae

2012

Pisanelli, I.; Wuehrer, P.; Reyes-Dominguez, Y.; Spadiut, O.; Haltrich, D.; Peterbauer, C.

Appl. Microbiol. Biotechnol.

93

1157-1166

725285

23667239

Cyclohexanecarboxyl-coenzyme a (CoA) and cyclohex-1-ene-1-carboxyl-CoA dehydrogenases, two enzymes involved in the fermentation of benzoate and crotonate in Syntrophus aciditrophicus

2013

Kung, J.; Seifert, J.; von Bergen, M.; Bolla, M.

J. Bacteriol.

195

3193-3200

725906

21903757

Reduction of quinones and phenoxy radicals by extracellular glucose dehydrogenase from Glomerella cingulata suggests a role in plant pathogenicity

2011

Sygmund, C.; Klausberger, M.; Felice, A.K.; Ludwig, R.

Microbiology

157

3203-3212

742783

25112478

Enzymes involved in a novel anaerobic cyclohexane carboxylic acid degradation pathway

2014

Kung, J.W.; Meier, A.K.; Mergelsberg, M.; Boll, M.

J. Bacteriol.

196

3667-3674

754177

29716998

Limonene dehydrogenase hydroxylates the allylic methyl group of cyclic monoterpenes in the anaerobic terpene degradation by Castellaniella defragrans

2018

Puentes-Cala, E.; Liebeke, M.; Markert, S.; Harder, J.

J. Biol. Chem.

293

9520-9529

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

Links to other databases for ferrocenium hexafluorophosphate

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