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Ligand coenzyme F420

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

coenzyme M biosynthesis, methanogenesis from CO2

KEGG

Biosynthesis of cofactors, Methane metabolism, Microbial metabolism in diverse environments

MetaCyc

2,4,6-trinitrophenol and 2,4-dinitrophenol degradation, 3PG-factor 420 biosynthesis, coenzyme B/coenzyme M regeneration I (methanophenazine-dependent), coenzyme B/coenzyme M regeneration III (coenzyme F420-dependent), factor 420 biosynthesis I (archaea), factor 420 biosynthesis II (mycobacteria), lactate biosynthesis (archaea), lincomycin A biosynthesis, methanogenesis from H2 and CO2, methoxylated aromatic compound degradation II, methyl-coenzyme M oxidation to CO2, reductive acetyl coenzyme A pathway II (autotrophic methanogens), sibiromycin biosynthesis, tetracycline and oxytetracycline biosynthesis more

Show all BRENDA pathways known for coenzyme F420

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (12 results)

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Show Natural Substrate (12 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.98.2

D-glucose 6-phosphate + oxidized coenzyme F420 = 6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420

723589, 739925, 740083

-

1.1.98.2

D-glucose 6-phosphate + oxidized coenzyme F420 = D-glucono-1,5-lactone 6-phosphate + reduced coenzyme F420

697967, 701052, 698547

-

1.12.98.1

H2 + coenzyme F420 = reduced coenzyme F420

659894, 246745, 395080, 395081, 395084, 395086, 395087, 395089, 395097, 395098, 395095, 395082, 395083, 395085, 395092, 395093, 395088, 395090, 395100, 395079, 395094, 687420

3zfs, 3D-view

1.12.98.1

H2 + oxidized coenzyme F420 = reduced coenzyme F420

764762, 742368, 743086, 395099, 727399, 763970

3zfs, 3D-view

1.1.98.2

2 entries

1.12.98.1

2 entries

1.17.98.3

formate + oxidized coenzyme F420 = CO2 + reduced coenzyme F420

726924, 740619, 727801, 726711, 727709

-

1.17.98.4

formate + oxidized coenzyme F420 = CO2 + reduced coenzyme F420

727803

-

1.3.1.24

biliverdin + coenzyme F420 + H+ = bilirubin + reduced coenzyme F420

741376

-

1.5.1.40

coenzyme F420 + NADPH + H+ = reduced coenzyme F420 + NADP+

711315

-

1.5.7.2

oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+ = reduced coenzyme F420 + 2 oxidized ferredoxin

724960

-

1.5.98.1

5,10-methylenetetrahydromethanopterin + oxidized coenzyme F420 = 5,10-methenyltetrahydromethanopterin + reduced coenzyme F420

742776, 742473, 288524, 654077, 728130

-

1.8.98.4

2 oxidized coenzyme F420 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 reduced coenzyme F420 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB

764762, 764753

-

1.8.98.4

oxidized coenzyme F420 + reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+ = reduced coenzyme F420 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB

743210

-

1.8.98.4

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (13 results)

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Show Natural Product (13 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.98.4

menaquinone + reduced coenzyme F420 = menaquinol + oxidized coenzyme F420

0

-

1.5.1.40

reduced coenzyme F420 + NADP+ = coenzyme F420 + NADPH + H+

0

-

1.5.1.40

reduced coenzyme F420 + NADP+ = oxidized coenzyme F420 + NADPH + H+

0

-

1.5.1.40

2 entries

1.5.3.22

2 reduced coenzyme F420 + O2 = 2 oxidized coenzyme F420 + 2 H2O

0

-

1.5.7.2

reduced coenzyme F420 + 2 oxidized ferredoxin = oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+

0

-

1.5.7.2

methanophenazine + reduced F420 + 2 H+ = reduced methanophenazine + oxidized F420

0

-

1.5.7.2

2 entries

1.5.98.1

5,10-methenyltetrahydromethanopterin + reduced coenzyme F420 = 5,10-methylenetetrahydromethanopterin + coenzyme F420

0

-

1.5.98.2

N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420 = 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420

288524, 288523, 288525, 288528

-

1.5.98.2

5,10-methylenetetrahydromethanopterin + reduced coenzyme F420 = 5-methyltetrahydromethanopterin + oxidized coenzyme F420

0

-

1.5.98.2

N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420 = 5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420

0

-

1.5.98.2

3 entries

1.5.98.3

reduced coenzyme F420 + methanophenazine = oxidized coenzyme F420 + dihydromethanophenazine

0

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + coenzyme F420H2 = coenzyme B + coenzyme M + coenzyme F420

0

-

1.8.98.3

sulfite + reduced coenzyme F420 = hydrogen sulfide + oxidized coenzyme F420

0

-

Substrate in Enzyme-catalyzed Reactions (34 results)

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Show Substrate (34 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.98.2

D-fructose 6-phosphate + oxidized coenzyme F420 = ? + reduced coenzyme F420

739925

-

1.1.98.2

D-fructose-6-phosphate + oxidized coenzyme F420 = ?

698547

-

1.1.98.2

D-glucosamine 6-phosphate + oxidized coenzyme F420 = ?

739925

-

1.1.98.2

D-glucose 6-phosphate + oxidized coenzyme F420 = 6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420

723589, 739925, 740083

-

1.1.98.2

D-glucose 6-phosphate + oxidized coenzyme F420 = D-glucono-1,5-lactone 6-phosphate + reduced coenzyme F420

697967, 701052, 698547

-

1.1.98.2

D-mannose 6-phosphate + oxidized coenzyme F420 = 6-phospho-D-mannono-1,5-lactone + reduced coenzyme F420

739925

-

1.1.98.2

D-mannose-6-phosphate + oxidized coenzyme F420 = ?

698547

-

1.1.98.5

(R)-2-butanol + oxidized coenzyme F420 = 2-butanone + reduced coenzyme F420

724899

-

1.1.98.5

(S)-2-butanol + oxidized coenzyme F420 = 2-butanone + reduced coenzyme F420

724899

-

1.1.98.5

2-pentanol + oxidized coenzyme F420 = 2-pentanone + reduced coenzyme F420

724899

-

1.1.98.5

2-propanol + oxidized coenzyme F420 = 2-propanone + reduced coenzyme F420

724899

-

1.1.98.5

2-propanol + oxidized coenzyme F420 = propanone + reduced coenzyme F420

724134

-

1.1.98.5

cyclopentanol + oxidized coenzyme F420 = cyclopentanone + reduced coenzyme F420

724899

-

1.12.98.1

H2 + coenzyme F420 = reduced coenzyme F420

246745, 659894, 395081, 395084, 395086, 395087, 395089, 395097, 395098, 395095, 395082, 395083, 395085, 395092, 395093, 687420, 395088, 395090, 395100, 395079, 395094, 395080

3zfs, 3D-view

1.12.98.1

H2 + oxidized coenzyme F420 = reduced coenzyme F420

764762, 742368, 743086, 395099, 727399, 763970

3zfs, 3D-view

1.1.98.2

7 entries

1.1.98.5

6 entries

1.12.98.1

2 entries

1.17.98.3

formate + oxidized coenzyme F420 = CO2 + reduced coenzyme F420

726924, 727712, 727714, 727717, 740619, 727801, 727709, 726711, 727711

-

1.17.98.4

formate + oxidized coenzyme F420 = CO2 + reduced coenzyme F420

727803

-

1.2.7.4

CO + H2O + coenzyme F420 = CO2 + reduced coenzyme F420

390456, 390473

-

1.3.1.24

biliverdin + coenzyme F420 + H+ = bilirubin + reduced coenzyme F420

741376

-

1.3.98.4

tetracycline + oxidized coenzyme F420 = 5a,11a-dehydrotetracycline + reduced coenzyme F420

738462

-

1.5.1.40

coenzyme F420 + NADPH + H+ = reduced coenzyme F420 + NADP+

711315, 395091

-

1.5.1.40

oxidized coenzyme F420 + NADPH + H+ = reduced coenzyme F420 + NADP+

724986

-

1.5.1.40

2 entries

1.5.7.2

oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+ = reduced coenzyme F420 + 2 oxidized ferredoxin

724960, 743210

-

1.5.98.1

5,10-methylenetetrahydromethanopterin + oxidized coenzyme F420 = 5,10-methenyltetrahydromethanopterin + reduced coenzyme F420

288524, 13757, 13748, 13747, 687420, 742776, 727408, 727375, 742473, 13750, 13752, 13753, 288527, 486086, 13749, 13755, 654077, 486097, 728130

-

1.5.98.3

oxidized coenzyme F420 + reduced 2,3-dimethyl-1,4-naphthoquinone = reduced coenzyme F420 + oxidized 2,3-dimethyl-1,4-naphthoquinone

742504

-

1.5.98.3

oxidized coenzyme F420 + reduced 2-bromophenazine = reduced coenzyme F420 + oxidized 2-bromophenazine

742504

-

1.5.98.3

oxidized coenzyme F420 + reduced 2-hydroxyphenazine = reduced coenzyme F420 + oxidized 2-hydroxyphenazine

742504

-

1.5.98.3

oxidized coenzyme F420 + reduced ferredoxin = reduced coenzyme F420 + oxidized ferredoxin

742483

-

1.5.98.3

oxidized coenzyme F420 + reduced methyl viologen = reduced coenzyme F420 + oxidized methyl viologen

742504

-

1.5.98.3

oxidized coenzyme F420 + reduced phenazine = reduced coenzyme F420 + oxidized phenazine

742504

-

1.5.98.3

oxidized coenzyme F420 + reduced tetramethyl-4-benzoquinone = reduced coenzyme F420 + oxidized tetramethyl-4-benzoquinone

742504

-

1.5.98.3

7 entries

1.8.98.1

coenzyme B + coenzyme M + reduced ferredoxin + H+ + coenzyme F420 = coenzyme B-coenzyme M disulfide + ferredoxin + H2 + reduced coenzyme F420

743210

-

1.8.98.4

2 oxidized coenzyme F420 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 reduced coenzyme F420 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB

764762, 764753

-

1.8.98.4

oxidized coenzyme F420 + reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+ = reduced coenzyme F420 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB

743210

-

1.8.98.4

2 entries

Product in Enzyme-catalyzed Reactions (43 results)

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Show Product (43 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.98.4

1,4-naphthoquinone + reduced coenzyme F420 = 1,4-naphthoquinol + oxidized coenzyme F420

0

-

1.1.98.4

2,3-dimethoxy-5-methyl-1,4-benzoquinone + reduced coenzyme F420 = 2,3-dimethoxy-5-methyl-1,4-benzoquinol + oxidized coenzyme F420

0

-

1.1.98.4

2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone + reduced coenzyme F420 = 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol + oxidized coenzyme F420

0

-

1.1.98.4

2,3-dimethyl-1,4-naphthoquinone + reduced coenzyme F420 = 2,3-dimethyl-1,4-naphthoquinol + oxidized coenzyme F420

0

-

1.1.98.4

2-hydroxy-1,4-naphthoquinone + reduced coenzyme F420 = 2-hydroxy-1,4-naphthoquinol + oxidized coenzyme F420

0

-

1.1.98.4

2-methyl-1,4-naphthoquinone + reduced coenzyme F420 = 2-methyl-1,4-naphthoquinol + oxidized coenzyme F420

0

-

1.1.98.4

menaquinone + reduced coenzyme F420 = menaquinol + oxidized coenzyme F420

0

-

1.1.98.4

oxidized methyl viologen + reduced coenzyme F420 = reduced methyl viologen + oxidized coenzyme F420

0

-

1.1.98.4

tetramethyl-4-benzoquinone + reduced coenzyme F420 = tetramethyl-1,4-benzoquinol + oxidized coenzyme F420

0

-

1.1.98.5

1-phenylpropan-1-one + reduced coenzyme F420 = (S)-1-phenylpropan-1-ol + oxidized coenzyme F420

0

-

1.1.98.5

2-butanone + reduced coenzyme F420 = 2-butanol + oxidized coenzyme F420

0

-

1.1.98.5

2-pentanone + reduced coenzyme F420 = 2-pentanol + oxidized coenzyme F420

0

-

1.1.98.5

4-methylpentan-2-one + reduced coenzyme F420 = (S)-4-methylpentan-2-ol + oxidized coenzyme F420

0

-

1.1.98.5

acetophenone + reduced coenzyme F420 = (S)-1-phenylethanol + oxidized coenzyme F420

0

-

1.1.98.5

cyclopentanone + reduced coenzyme F420 = cyclopentanol + oxidized coenzyme F420

0

-

1.1.98.5

methoxyacetone + reduced coenzyme F420 = (2S)-1-methoxypropan-2-ol + oxidized coenzyme F420

0

-

1.1.98.5

octan-3-one + reduced coenzyme F420 = (S)-3-octanol + oxidized coenzyme F420

0

-

1.1.98.5

pentan-2-one + reduced coenzyme F420 = (S)-2-pentanol + oxidized coenzyme F420

0

-

1.1.98.5

propanone + reduced coenzyme F420 = 2-propanol + oxidized coenzyme F420

0

-

1.1.98.4

9 entries

1.1.98.5

10 entries

1.1.99.B7

2,3-dimethyl-1,4-naphthoquinone + reduced coenzyme F420 = 2,3-dimethyl-1,4-naphthoquinol + oxidized coenzyme F420

0

-

1.5.1.40

reduced coenzyme F420 + NADP+ = coenzyme F420 + NADPH + H+

0

-

1.5.1.40

reduced coenzyme F420 + 1-aminoethylnicotinamide = oxidized coenzyme F420 + ?

0

-

1.5.1.40

reduced coenzyme F420 + 1-benzyl-3-acetylpyridine = oxidized coenzyme F420 + ?

0

-

1.5.1.40

reduced coenzyme F420 + 1-benzylnicotinamide = oxidized coenzyme F420 + ?

0

-

1.5.1.40

reduced coenzyme F420 + 1-ethylnicotinamide = oxidized coenzyme F420 + ?

0

-

1.5.1.40

reduced coenzyme F420 + 1-hydroxyethylnicotinamide = oxidized coenzyme F420 + ?

0

-

1.5.1.40

reduced coenzyme F420 + 1-hydroxypropylnicotinamide = oxidized coenzyme F420 + ?

0

-

1.5.1.40

reduced coenzyme F420 + 1-propylnicotinamide = oxidized coenzyme F420 + ?

0

-

1.5.1.40

reduced coenzyme F420 + NADP+ = oxidized coenzyme F420 + NADPH + H+

0

-

1.5.1.40

9 entries

1.5.3.22

2 reduced coenzyme F420 + O2 = 2 oxidized coenzyme F420 + 2 H2O

0

-

1.5.7.2

reduced coenzyme F420 + 2 oxidized ferredoxin = oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+

0

-

1.5.7.2

methanophenazine + reduced F420 + 2 H+ = reduced methanophenazine + oxidized F420

0

-

1.5.7.2

2 entries

1.5.98.1

5,10-methenyltetrahydromethanopterin + reduced coenzyme F420 = 5,10-methylenetetrahydromethanopterin + coenzyme F420

0

-

1.5.98.2

N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420 = 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420

288524, 288523, 288525, 288528, 288529, 288531, 288527, 288526, 288530, 0

-

1.5.98.2

5,10-methylenetetrahydromethanopterin + reduced coenzyme F420 = 5-methyltetrahydromethanopterin + oxidized coenzyme F420

0

-

1.5.98.2

N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420 = 5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420

0

-

1.5.98.3

reduced coenzyme F420 + methanophenazine = oxidized coenzyme F420 + dihydromethanophenazine

0

-

1.5.98.3

reduced coenzyme F420 + oxidized 2-hydroxyphenazine = oxidized coenzyme F420 + reduced 2-hydroxyphenazine

0

-

1.5.98.3

reduced coenzyme F420 + oxidized metronidazole = oxidized coenzyme F420 + reduced metronidazole

0

-

1.5.98.2

3 entries

1.5.98.3

3 entries

1.8.1.2

sulfite + reduced F420 = sulfide + oxidized F420

0

-

1.8.7.1

sulfite + reduced coenzyme F420 = sulfide + oxidized coenzyme F420

0

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + coenzyme F420H2 = coenzyme B + coenzyme M + coenzyme F420

0

-

1.8.98.3

sulfite + reduced coenzyme F420 = hydrogen sulfide + oxidized coenzyme F420

0

-

Enzyme Cofactor/Cosubstrate (16 results)

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Show Cofactor (16 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.98.2

-

697967, 698547, 701052, 740083

-

1.1.98.2

a 5-deazaflavin derivative

723589

-

1.1.98.2

the enzyme is strictly dependent on F420 as coenzyme

739925

-

1.1.98.2

3 entries

1.12.98.1

-

742368, 743086

3zfs, 3D-view

1.12.98.2

-

696971

-

1.12.98.3

the reaction is dependent on the cofactor F420

727829

-

1.17.98.3

-

740619

-

1.3.1.24

-

741376

-

1.5.98.1

-

687420, 742776, 696301, 742473

-

1.5.98.1

dependent on

486097, 654120

-

1.5.98.1

dependent on, binding site structure

654077

-

1.5.98.1

required

288524, 13749, 13750, 13752, 13753, 13757, 13748, 288527, 486086, 13755, 13747

-

1.5.98.1

4 entries

1.5.98.2

-

687420

-

1.8.98.1

-

654386, 743210

-

1.8.98.4

-

764753

-

1.8.98.4

reduced F420 is a direct electron donor in the carbon dioxide reduction pathway and also serves as the electron donor for the proposed HdrABC-catalyzed electron bifurcation reaction in which reduced ferredoxin (also required for carbon dioxide reduction) is generated with simultaneous reduction of CoM-S-S-CoB

764762

-

1.8.98.4

2 entries

Activator in Enzyme-catalyzed Reactions (3 results)

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Show Activating Compound (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.8.1.2

-

674504

-

1.8.7.1

-

674504

-

2.8.4.1

enzyme system is stimulated

393257

-

3D Structure of Enzyme-Ligand-Complex (PDB) (5 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (5 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.12.98.1

3zfs, 3D-view

1.5.99.11

1z69, 3D-view

1.5.99.9

3iqe, 3D-view

6.3.2.31

4xoq, 3D-view

6.3.2.34

4xoq, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (17 results)

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Show Turnover Number (17 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.98.2

0.001

-

mutant enzyme W44A, at pH 7.0 and 22°C

740083

1.1.98.2

0.002

-

mutant enzyme H40A, at pH 7.0 and 22°C

740083

1.1.98.2

0.02

-

mutant enzyme E109Q, at pH 7.0 and 22°C

740083

1.1.98.2

0.06

-

mutant enzyme W44Y, at pH 7.0 and 22°C

740083

1.1.98.2

1.4

-

wild type enzyme, at pH 7.0 and 22°C

740083

1.1.98.2

3.2

-

mutant enzyme W44F, at pH 7.0 and 22°C

740083

1.1.98.2

6 entries

1.1.98.5

85

-

pH 5.8, 37°C

724899

1.12.98.1

17.5

-

-

395088

1.12.98.1

353

-

37°C, pH 7.5

727399

1.12.98.1

725

-

pH 7.2

395080

1.12.98.1

2050

-

-

395089

1.5.1.40

0.7

-

with F420 precursor, FO, pH 6.5, 22°C, recombinant mutant I135G

741811

1.5.1.40

1.6

-

with F420 precursor, FO, pH 6.5, 22°C, recombinant mutant I135A

741811

1.5.1.40

1.8

-

with F420 precursor, FO, pH 6.5, 22°C, recombinant mutant I135V

741811

1.5.1.40

5.27

-

pH 6.5, 22°C, recombinant enzyme

741921

1.5.1.40

5.3

-

with F420 precursor, FO, pH 6.5, 22°C, recombinant wild-type enzyme

741811

1.5.1.40

17.22

-

pH 6.0, 22°C

711315

1.12.98.1

4 entries

1.5.1.40

6 entries

K_M Value (40 results)

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Show KM Value (40 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.98.2

0.0009

-

mutant enzyme W44A, at pH 7.0 and 22°C

740083

1.1.98.2

0.0026

-

wild type enzyme, at pH 7.0 and 22°C

740083

1.1.98.2

0.004

-

pH 7.0, 40°C

698547

1.1.98.2

0.0042

-

mutant enzyme W44Y, at pH 7.0 and 22°C

740083

1.1.98.2

0.0054

-

mutant enzyme W44F, at pH 7.0 and 22°C

740083

1.1.98.2

0.0056

-

mutant enzyme E109Q, at pH 7.0 and 22°C

740083

1.1.98.2

0.008

-

mutant enzyme H40A, at pH 7.0 and 22°C

740083

1.1.98.2

7 entries

1.1.98.5

0.018

-

pH 5.8, 37°C

724899

1.12.98.1

0.016

-

-

395088

1.12.98.1

0.019

-

pH 7.2

395080

1.12.98.1

0.025

-

37°C, pH 7.5

727399

1.12.98.1

0.036

-

-

395089

1.12.98.1

0.037

-

-

395093

1.12.98.1

5 entries

1.17.98.3

0.006

-

pH 7.5, temperature not specified in the publication

727711

1.5.1.40

0.0034

-

pH 6.0, 22°C

711315

1.5.1.40

0.0036

-

with F420 precursor, FO, pH 6.5, 22°C, recombinant mutant I135A

741811

1.5.1.40

0.0036

-

with F420 precursor, FO, pH 6.5, 22°C, recombinant mutant I135G

741811

1.5.1.40

0.0037

-

with F420 precursor, FO, pH 6.5, 22°C, recombinant mutant I135V

741811

1.5.1.40

0.004

-

with F420 precursor, FO, pH 6.5, 22°C, recombinant wild-type enzyme

741811

1.5.1.40

0.01

-

pH 5.5, 65°C

724135

1.5.1.40

0.0625

-

pH and temperature not specified in the publication

727263

1.5.1.40

0.1

-

pH 6.0, 30°C

724136

1.5.1.40

0.3

-

pH 6.0, temperature not specified in the publication

724986

1.5.1.40

2

-

pH 6.0, 25°C, recombinant enzyme

742904

1.5.1.40

4

-

pH 6.5, 22°C, recombinant enzyme

741921

1.5.7.2

0.002

-

pH 7.0, temperature not specified in the publication

724960

1.5.7.2

0.0064

-

21°C, pH not specified in the publication

743210

1.5.98.1

0.004

-

-

13748

1.5.98.1

0.005

-

pH 6.0, 20°C

727375

1.5.98.1

0.013

-

-

486086

1.5.98.1

0.013

-

-

486097

1.5.98.1

0.018

-

-

288524

1.5.98.1

0.02

-

-

13755

1.5.98.1

0.02

-

native enzyme, pH 6.0, 65°C, N2-atmosphere

486097

1.5.98.1

0.025

-

-

486097

1.5.98.1

0.03

-

1 M (NH4)2SO4, at 65°C

696301

1.5.98.1

0.04

-

recombinant enzyme expressed in Escherichia coli, pH and temperature not specified in the publication

727408

1.5.98.1

0.065

-

-

13752

1.5.98.1

0.065

-

-

486097

1.5.98.1

0.08

-

enzyme from Methanopyrus kandleri, pH and temperature not specified in the publication

727408

1.5.1.40

11 entries

1.5.7.2

2 entries

1.5.98.1

13 entries

References & Links

Literature References (96)

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Show Reference (96 entries)

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AUTHORS

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1991

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Methyl-coenzyme M reductase and other enzymes involved in methanogenesis from carbon dioxide and hydrogen in the extreme thermophile Methanopyrus kandleri

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1993

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Coenzyme F420-dependent N5,N10-methylenetetrahydromethanopterin reductase (Mer) from Methanobacterium thermoautotrophicum strain Marburg. Cloning, sequencing, transcriptional analysis, and functional expression in Escherichia coli of the mer gene

1995

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Paramagnetic centers in the nickel-containig, deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum

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Two hydrogenases with distinct electron-carrier specificity and subunit composition in Methanobacterium formicicum

1983

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1984

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395084

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Electron microscopy of nickel-containing methanogenic enzymes: methyl reductase and F420-reducing hydrogenase

1987

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1987

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8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 1. Purification and characterization

1987

Fox, J.A.; Livingston, D.J.; Orme-Johnson, W.H.; Walsh, C.T.

Biochemistry

26

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395087

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Properties of the particulate enzyme F420-reducing hydrogenase isolated from Methanospirillum hungatei

1987

Sprott, G.D.; Shaw, K.M.; Beveridge, T.J.

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33

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Purification and characterization of an 8-hydroxy-5-deazaflavin-reducing hydrogenase from the archaebacterium Methanococcus voltae

1987

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1987

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1988

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Spectrophotometric identification of 8-hydroxy-5-deazaflavin. NADPH oxidoreductase activity in Streptomyces producing tetracyclines

1989

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Immunogold localization of coenzyme F420-reducing format dehydrogenase and coenzyme F420-reducing hydrogenase in Methanobacterium formicicum

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Cloning, sequence determination, and expression of the genes encoding the subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum delta H

1990

Alex, L.A.; Reeve, J.N.; Orme-Johnson, W.H.; Walsh, C.T.

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29

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395095

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Partial purification and characterization of two hydrogenases from the extreme thermophile Methanococcus jannaschii

1990

Shah, N.N.; Clark, D.S.

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56

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395097

27316897

Some properties of F420-reducing hydrogenase of Methanobacterium thermoformicicum strain SF-4

1993

Tachibana, A.; Tanaka, T.; Taniguchi, M.; Oi, S.

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57

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395098

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Structural aspects and immunolocalization of the F420-reducing and non-F420-reducing hydrogenases from Methanobacterium thermoautotrophicum Marburg

1994

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395099

8521835

Biochemical characterization of the 8-hydroxy-5-deazaflavin-reactive hydrogenase from Methanosarcina barkeri Fusaro

1995

Michel, R.; Massanz, C.; Kostka, S.; Richter, M.; Fiebig, K.

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2000

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267

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486086

8481089

Formylmethanofuran:tetrahydromethanopterin formyltransferase and N5,N10-methylenetetrahydromethanopterin dehydrogenase from the sulfate-reducing Archaeoglobus fulgidus: similarities with the enzymes from methanogenic Archaea

1993

Schwörer, B.; Breitung, J.; Klein, A.R.; Stetter, K.O.; Thauer, R.K.

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225-232

486097

11265475

Tetrahydromethanopterin-specific enzymes from Methanopyrus kandleri

2001

Shima, S.; Thauer, R.K.

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331

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654077

12925803

Coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase from Methanopyrus kandleri: the selenomethionine-labelled and non-labelled enzyme crystallized in two different forms

2003

Hagemeier, C.H.; Shima, S.; Warkentin, E.; Thauer, R.K.; Ermler, U.

Acta Crystallogr. Sect. D

59

1653-1655

654120

15681872

The structure of F420-dependent methylenetetrahydromethanopterin dehydrogenase: a crystallographic 'superstructure' of the selenomethionine-labelled protein crystal structure

2005

Warkentin, E.; Hagemeier, C.H.; Shima, S.; Thauer, R.K.; Ermler, U.

Acta Crystallogr. Sect. D

61

198-202

654386

9914308

Membrane-bound F420H2-dependent heterodisulfide reduction in Methanococcus voltae

1999

Brodersen, J.; Gottschalk, G.; Deppenmeier, U.

Arch. Microbiol.

171

115-121

659894

15870477

Hydrogen concentrations in methane-forming cells probed by the ratios of reduced and oxidized coenzyme F420

2005

de Poorter, L.M.; Geerts, W.J.; Keltjens, J.T.

Microbiology

151

1697-1705

674504

16048999

A new type of sulfite reductase, a novel coenzyme F420-dependent enzyme, from the methanarchaeon Methanocaldococcus jannaschii

2005

Johnson, E.F.; Mukhopadhyay, B.

J. Biol. Chem.

280

38776-38786

687420

18487331

Roles of coenzyme F420-reducing hydrogenases and hydrogen- and F420-dependent methylenetetrahydromethanopterin dehydrogenases in reduction of F420 and production of hydrogen during methanogenesis

2008

Hendrickson, E.L.; Leigh, J.A.

J. Bacteriol.

190

4818-4821

696301

19761261

Structural basis of the hydride transfer mechanism in F(420)-dependent methylenetetrahydromethanopterin dehydrogenase

2009

Ceh, K.; Demmer, U.; Warkentin, E.; Moll, J.; Thauer, R.K.; Shima, S.; Ermler, U.

Biochemistry

48

10098-10105

696971

19671178

Comprehensive computational analysis of Hmd enzymes and paralogs in methanogenic Archaea

2009

Goldman, A.; Leigh, J.; Samudrala, R.

BMC Evol. Biol.

9

199-210

697967

8997717

Presence of F420-dependent glucose-6-phosphate dehydrogenase in Mycobacterium and Nocardia species, but absence from Streptomyces and Corynebacterium species and methanogenic archaea

1997

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698547

8631674

Purification of a novel coenzyme F420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis

1996

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Expression, purification and crystallization of native and selenomethionine labeled Mycobacterium tuberculosis FGD1 (Rv0407) using a Mycobacterium smegmatis expression system

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Characterization of an 8-hydroxy-5-deazaflavin:NADPH oxidoreductase from Streptomyces griseus

1989

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2012

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PLoS ONE

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724134

-

Expression of secondary alcohol dehydrogenase in methanogenic bacteria and purification of the F420-specific enzyme from Methanogenium thermophilum strain TCI

1989

Widdel, F.; Wolfe, R.S.

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152

322-328

724135

-

A F420-dependent NADP reductase in the extremely thermophilie sulfate-reducing Archaeoglobus fulgidus

1993

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160

199-205

724136

9325428

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1997

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724899

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Purification and properties of F420- and NADP(+)-dependent alcohol dehydrogenases of Methanogenium liminatans and Methanobacterium palustre, specific for secondary alcohols

1991

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200

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724960

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2011

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724986

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1998

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124-126

726711

18791018

Formate-dependent H2 production by the mesophilic methanogen Methanococcus maripaludis

2008

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Appl. Environ. Microbiol.

74

6584-6590

726924

3801411

Mechanistic studies of the coenzyme F420 reducing formate dehydrogenase from Methanobacterium formicicum

1986

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Biochemistry

25

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727263

11109487

Purification of the NADP+:F420 oxidoreductase of Methanosphaera stadtmanae

2000

Elias, D.A.; Juck, D.F.; Berry, K.A.; Sparling, R.

Can. J. Microbiol.

46

998-1003

727375

24707918

A reversed genetic approach reveals the coenzyme specificity and other catalytic properties of three enzymes putatively involved in anaerobic oxidation of methane with sulfate

2014

Kojima, H.; Moll, J.; Kahnt, J.; Fukui, M.; Shima, S.

Environ. Microbiol.

16

3431-3442

727399

2550229

Purification of the F420-reducing hydrogenase from Methanosarcina barkeri (strain Fusaro)

1989

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Eur. J. Biochem.

184

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727408

9151968

Overexpression of the coenzyme-F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase gene from the hyperthermophilic Methanopyrus kandleri

1997

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Eur. J. Biochem.

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727709

234935

Factor 420-dependent pyridine nucleotide-linked formate metabolism of Methanobacterium ruminantium

1975

Tzing, S.F.; Bryant, M.P.; Wolfe, R.S.

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121

192-196

727711

7061389

Properties of formate dehydrogenase in Methanobacterium formicicum

1982

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150

1-7

727712

6874636

FAD requirement for the reduction of coenzyme F420 by formate dehydrogenase from Methanobacterium formicicum

1983

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J. Bacteriol.

155

467-472

727714

3944055

Composition of the coenzyme F420-dependent formate dehydrogenase from Methanobacterium formicicum

1986

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J. Bacteriol.

165

405-411

727717

2661536

Reconstitution and properties of a coenzyme F420-mediated formate hydrogenlyase system in Methanobacterium formicicum

1989

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J. Bacteriol.

171

3854-3859

727801

7356649

Reconstitution of a formate-NADP+ oxidoreductase from formate dehydrogenase and a 5-deazaflavin-linked NADP+ reductase isolated from Methanococcus vannielii

1980

Jones, J.B.; Stadtman, T.C.

J. Biol. Chem.

255

1049-1053

727803

7451465

Selenium-dependent and selenium-independent formate dehydrogenases of Methanococcus vannielii. Separation of the two forms and characterization of the purified selenium-independent form

1981

Jones, J.B.; Stadtman, T.C.

J. Biol. Chem.

256

656-663

727829

10751389

The F420H2 dehydrogenase from Methanosarcina mazei is a Redox-driven proton pump closely related to NADH dehydrogenases

2000

Baumer, S.; Ide, T.; Jacobi, C.; Johann, A.; Gottschalk, G.; Deppenmeier, U.

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728130

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Coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase (Mtd) from Methanopyrus kandleri: a methanogenic enzyme with an unusual quarternary structure

2003

Hagemeier, C.H.; Shima, S.; Thauer, R.K.; Bourenkov, G.; Bartunik, H.D.; Ermler, U.

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1047-1057

738462

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Cosynthetic factor I, a factor involved in hydrogen-transfer in Streptomyces aureofaciens [4]

1960

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739925

27966048

Discovery and characterization of an F420-dependent glucose-6-phosphate dehydrogenase (Rh-FGD1) from Rhodococcus jostii RHA1

2016

Nguyen, Q.T.; Trinco, G.; Binda, C.; Mattevi, A.; Fraaije, M.W.

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740083

27603793

Investigating the reaction mechanism of F420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium tuberculosis: Kinetic analysis of the wild-type and mutant enzymes

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Oyugi, M.A.; Bashiri, G.; Baker, E.N.; Johnson-Winters, K.

Biochemistry

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740619

23335420

Effects of H2 and formate on growth yield and regulation of methanogenesis in Methanococcus maripaludis

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Costa, K.C.; Yoon, S.H.; Pan, M.; Burn, J.A.; Baliga, N.S.; Leigh, J.A.

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195

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741376

27364382

Rv2074 is a novel F420H2-dependent biliverdin reductase in Mycobacterium tuberculosis

2016

Ahmed, F.H.; Mohamed, A.E.; Carr, P.D.; Lee, B.M.; Condic-Jurkic, K.; O'Mara, M.L.; Jackson, C.J.

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741811

28955995

Effects of isoleucine 135 side chain length on the cofactor donor-acceptor distance within F420H2 NADP+ oxidoreductase A kinetic analysis

2017

Le, C.; Oyugi, M.; Joseph, E.; Nguyen, T.; Ullah, M.; Aubert, J.; Phan, T.; Tran, J.; Johnson-Winters, K.

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741921

26811861

Evidence of negative cooperativity and half-site reactivity within an F420-dependent enzyme kinetic analysis of F420H2 NADP+ oxidoreductase

2016

Joseph, E.; Le, C.Q.; Nguyen, T.; Oyugi, M.; Hossain, M.S.; Foss, F.W.; Johnson-Winters, K.

Biochemistry

55

1082-1090

742368

24569482

Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector

2014

Allegretti, M.; Mills, D.J.; McMullan, G.; Kuehlbrandt, W.; Vonck, J.

eLife

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742473

27347377

Lovastatin lactone may improve irritable bowel syndrome with constipation (IBS-C) by inhibiting enzymes in the archaeal methanogenesis pathway

2016

Muskal, S.M.; Sliman, J.; Kokai-Kun, J.; Pimentel, M.; Wacher, V.; Gottlieb, K.

F1000Res.

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606

742483

21306561

Re-evaluation of the function of the F420 dehydrogenase in electron transport of Methanosarcina mazei

2011

Welte, C.; Deppenmeier, U.

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278

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742504

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The F420H2 heterodisulfide oxidoreductase system from Methanosarcina species. 2-Hydroxyphenazine mediates electron transfer from F420H2 dehydrogenase to heterodisulfide reductase

1998

Baeumer, S.; Murakami, E.; Brodersen, J.; Gottschalk, G.; Ragsdale, S.; Deppenmeier, U.

FEBS Lett.

428

295-298

742776

23335420

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Costa, K.; Yoon, S.; Pan, M.; Burn, J.; Baliga, N.; Leigh, J.

J. Bacteriol.

195

1456-1462

742904

28411200

Isolation and characterization of a thermostable F420 NADPH oxidoreductase from Thermobifida fusca

2017

Kumar, H.; Nguyen, Q.T.; Binda, C.; Mattevi, A.; Fraaije, M.W.

J. Biol. Chem.

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743086

24887099

The F420-reducing [NiFe]-hydrogenase complex from Methanothermobacter marburgensis, the first X-ray structure of a group 3 family member

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Vitt, S.; Ma, K.; Warkentin, E.; Moll, J.; Pierik, A.J.; Shima, S.; Ermler, U.

J. Mol. Biol.

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2813-2826

743210

28174314

A ferredoxin- and F420H2-dependent, electron-bifurcating, heterodisulfide reductase with homologs in the domains Bacteria and Archaea

2017

Yan, Z.; Wang, M.; Ferry, J.G.

mBio

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763970

31924613

Direct electron transfer between the frhAGB-encoded hydrogenase and thioredoxin reductase in the nonmethanogenic archaeon Thermococcus onnurineus NA1

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Jung, H.-C.; Lim , J.K.; Yang, T.-J.; Kang, S.G.; Lee, H.S.

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Electron bifurcation and confurcation in methanogenesis and reverse methanogenesis

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Yan, Z.; Ferry, J.

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764762

30631315

Electron and proton flux for carbon dioxide reduction in Methanosarcina barkeri during direct interspecies electron transfer

2018

Holmes, D.; Rotaru, A.; Ueki, T.; Shrestha, P.; Ferry, J.; Lovley, D.

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3109

Links to other databases for coenzyme F420

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