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  • InChIKey
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• • In Vivo Substrate
  • In Vivo Product
  • Substrate
  • Product
  • Cofactor
  • Activator
  • Inhibitor
  • Metals and Ions
  • 3D Structure (PDB)
• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
  • K_M Value
  • K_i Value
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Ligand H2

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

coenzyme M biosynthesis, hydrogen production, methanogenesis from CO2, nitrate assimilation, sulfate reduction

KEGG

Carbohydrate digestion and absorption, Protein digestion and absorption, Two-component system

MetaCyc

coenzyme B/coenzyme M regeneration I (methanophenazine-dependent), coenzyme B/coenzyme M regeneration IV (H2-dependent), hydrogen oxidation I (aerobic), hydrogen oxidation II (aerobic, NAD), hydrogen oxidation III (anaerobic, NADP), hydrogen production I, hydrogen production II, hydrogen production III, hydrogen production IV, hydrogen production V, hydrogen production VI, hydrogen production VIII, hydrogen to dimethyl sulfoxide electron transfer, hydrogen to fumarate electron transfer, hydrogen to trimethylamine N-oxide electron transfer, L-glutamate degradation VII (to butanoate), methanogenesis from H2 and CO2, mixed acid fermentation, nitrogen fixation I (ferredoxin), nitrogen fixation II (flavodoxin), reductive acetyl coenzyme A pathway II (autotrophic methanogens), sulfur reduction I, sulfur reduction II (via polysulfide), superpathway of fermentation (Chlamydomonas reinhardtii) more

Show all BRENDA pathways known for H2

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (24 results)

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Show Natural Substrate (24 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.12.1.2

H2 + oxidized methyl viologen = H+ + reduced methyl viologen

655638

-

1.12.1.2

H2 + NAD+ = H+ + NADH

439633, 656298, 742695, 742373, 742858, 743797, 656734, 654821, 742575, 439692, 439694, 654388, 654562, 655638, 654285, 655890, 655307, 672067

-

1.12.1.3

H2 + oxidized ferredoxin = H+ + reduced ferredoxin

439691

-

1.12.1.3

H2 + NADP+ = H+ + NADPH

704606, 439687, 687409

-

1.12.1.2

2 entries

1.12.1.3

2 entries

1.12.1.4

H2 + NAD+ + oxidized ferredoxin = H+ + NADH + reduced ferredoxin

741931

-

1.12.2.1

H2 + ferricytochrome c3 = H+ + ferrocytochrome c3

674919, 742006, 742696, 654899, 675360

-

1.12.7.2

H2 + oxidized ferredoxin = H+ + reduced ferredoxin

439643, 439665, 439672, 439632, 439669, 439671, 439675, 439679, 439682, 439677, 712301, 439654, 439650

-

1.12.7.2

H2 + oxidized ferredoxin = reduced ferredoxin + H+

660222, 742859, 742784, 742698, 659110

-

1.12.7.2

H2 + oxidized ferredoxin Pet F = reduced ferredoxin Pet F + H+

742279

-

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

-

1.12.98.1

H2 + oxidized methyl viologen = reduced methyl viologen

727399

-

1.12.98.1

H2 + oxidized coenzyme F420 = reduced coenzyme F420

742368, 743086, 395099, 727399

-

1.12.7.2

3 entries

1.12.98.1

3 entries

1.12.98.2

5,10-methenyltetrahydromethanopterin + H2 = 5,10-methylenetetrahydromethanopterin + H+

657579, 658635, 658966, 658978, 696971

-

1.12.98.3

H2 + 2-(2,3-dihydropentaprenyloxy)phenazine = 2-dihydropentaprenyloxyphenazine

440299, 741956, 440300, 727829

-

1.12.99.6

H2 + acceptor = H+ + reduced acceptor

713374, 712029, 439644, 439637, 439645, 439638, 439627, 439643, 439632, 671432

-

1.12.99.6

H2 + acceptor = acceptor-H2

658987, 657739

-

1.12.99.6

H2 + acceptor = acceptorH2

658082, 659887

-

1.12.99.6

H2 + acceptor = reduced acceptor

742652

-

1.12.99.6

H2 + methylene blue = reduced methylene blue

742265

-

1.12.99.6

H2 + NADPH = NADP + H+

743732

-

1.12.99.6

6 entries

1.21.99.5

tetrachloroethene + 2 H2 = cis-1,2-dichloroethene + 2 chloride + 2 H+

657605

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2 = coenzyme B + coenzyme M

655400, 655398, 655396, 655825

-

1.8.98.5

H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB = reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+

744833, 744179

-

1.97.1.9

selenate + H2 = selenite + H2O

658902

-

In Vivo Product in Enzyme-catalyzed Reactions (18 results)

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Show Natural Product (18 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.12.1.2

H+ + NADH = H2 + NAD+

-

-

1.12.1.2

H+ + NADPH = H2 + NADP+

-

-

1.12.1.2

2 entries

1.12.1.4

NADH + H+ + reduced ferredoxin = H2 + NAD+ + oxidized ferredoxin

-

-

1.12.7.2

H+ + reduced ferredoxin = H2 + oxidized ferredoxin

-

-

1.12.7.2

2 H+ + reduced ferredoxin = H2 + oxidized ferredoxin

-

-

1.12.7.2

2 H+ + reduced polyferredoxin = H2 + oxidized polyferredoxin

-

-

1.18.6.1

8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate

440174, 440188

-

1.18.6.1

reduced ferredoxin + H+ + N2 + ATP + H2O = oxidized ferredoxin + H2 + NH3 + ADP + phosphate

-

-

1.18.6.1

N2 + 8 e- + 16 ATP + 8 H+ = 2 NH3 + H2 + 16 ADP + 16 phosphate

-

-

1.18.6.1

reduced ferredoxin + H+ + N2 + ATP = oxidized ferredoxin + H2 + NH3 + ADP + phosphate

-

-

1.18.6.1

N2 + 8 e- + 8 H+ + 16 ATP = 2 NH3 + H2 + 16 ADP + 16 phosphate

-

-

1.18.6.1

N2 + 10 H+ + 8 e- + 16 ATP = 2 NH4+ + H2 + 16 ADP + 16 phosphate

-

-

1.12.7.2

3 entries

1.18.6.1

6 entries

1.18.6.2

12 reduced ferredoxin + 12 H+ + N2 + 40 ATP + 40 H2O = 12 oxidized ferredoxin + 3 H2 + 2 NH3 + 40 ADP + 40 phosphate

-

-

1.19.6.1

reduced ferredoxin + H+ + N2 + ATP = oxidized ferredoxin + H2 + NH3 + ADP + phosphate

-

-

1.19.6.1

reduced flavodoxin + N2 + ATP + H2O = oxidized flavodoxin + H2 + NH3 + ADP + phosphate

-

-

1.19.6.1

reduced flavodoxin II + N2 + ATP + H2O = oxidized flavodoxin II + H2 + NH3 + ADP + phosphate

-

-

1.19.6.1

3 entries

1.2.7.4

CO + H2O = CO2 + H2

390485

-

1.8.98.5

reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+ = H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB

-

-

Substrate in Enzyme-catalyzed Reactions (143 results)

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Show Substrate (143 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.99.30

2-oxo-3,5-dienoates + H2 = ?

655314

-

1.1.99.30

2-oxo-3-(3,4-dihydroxyphenyl)-propionate + H2 = rosmarinic acid

655314

-

1.1.99.30

2-oxo-3-enoates + H2 = ?

655314

-

1.1.99.30

phenylpyruvate + H2 = (2R)-phenyllactate

655314

-

1.12.1.2

H2 + acceptor = H+ + reduced acceptor

672279, 706499

-

1.12.1.2

H2 + NADP+ = H+ + NADPH

672282

-

1.12.1.2

H2 + oxidized methyl viologen = H+ + reduced methyl viologen

439711, 439699, 654388, 439702, 687403, 655307, 656734, 654285, 655638, 744926, 654821

-

1.12.1.2

H2 + NAD+ = H+ + NADH

439692, 439694, 439695, 439696, 439697, 439700, 439704, 439705, 439706, 439707, 439709, 439710, 439711, 439712, 439633, 656298, 672067, 675493, 726344, 654562, 655890, 674165, 654388, 439703, 439713, 742695, 655307, 742373, 742858, 743797, 685324, 656734, 654821, 654285, 655638, 742575, 439699, 439702, 439708, 439701, 439693, 439698, 654782, 672282, 726282

-

1.12.1.2

H2 + oxidized benzyl viologen = H+ + reduced benzyl viologen

439633, 439699, 655890, 656298, 654388, 439713, 439702

-

1.12.1.2

H2 + oxidized methylene blue = H+ + reduced methylene blue

439711, 654388, 439702

-

1.12.1.2

H2 + ferricyanide = H+ + ferrocyanide

654782, 439711

-

1.12.1.2

H2 + ferrocyanide = H+ + ferricyanide

655890

-

1.12.1.2

H2 + NAD(P)+ = H+ + NAD(P)H

654821

-

1.12.1.2

H2 + oxidized dithionite = H+ + reduced dithionite

654821

-

1.12.1.2

H2 = H+ + e-

654782

-

1.12.1.2

H2 + oxidized benzyl viologen = reduced benzyl viologen + H+

655890, 672282

-

1.12.1.2

H2 + oxidized methyl viologen = reduced methyl viologen + H+

672282

-

1.12.1.3

H2 + oxidized ferredoxin = H+ + reduced ferredoxin

439691

-

1.12.1.3

H2 + NADP+ = H+ + NADPH

704606, 439687, 439688, 659019, 439690, 439691, 439686, 687409

-

1.12.1.3

H2 + oxidized methyl viologen = H+ + reduced methyl viologen

687409, 659019, 439687

-

1.12.1.3

H2 + NAD+ = H+ + NADH

659019

-

1.12.1.3

H2 + oxidized benzyl viologen = H+ + reduced benzyl viologen

687409, 659019

-

1.12.1.3

H2 + oxidized methylene blue = H+ + reduced methylene blue

659019

-

1.12.1.3

H2 + 2,6-dichlorophenolindophenol = H+ + ?

659019

-

1.12.1.4

NAD+ + 2 oxidized ferredoxin + 2 H2 = NADH + 3 H+ + 2 reduced ferredoxin

740625, 740618

-

1.12.1.4

NAD+ + 2 oxidized methyl viologen + 2 H2 = NADH + 3 H+ + 2 reduced methyl viologen

740618

-

1.12.1.4

H2 + NAD+ + oxidized ferredoxin = H+ + NADH + reduced ferredoxin

741931

-

1.12.1.5

H2 + NADP+ = H+ + NADPH

439641

-

1.12.1.5

H2 + NAD+ = H+ + NADH

439641

-

1.12.2.1

H2 + ferricytochrome c3 = H+ + ferrocytochrome c3

395570, 395559, 395567, 395573, 654261, 657318, 395560, 395561, 395562, 395563, 395566, 395571, 395574, 674919, 684509, 686734, 688655, 742006, 395564, 395565, 689932, 395569, 395572, 742696, 395568, 654899, 675360, 672118, 711266, 724456

-

1.12.2.1

H2 + ferricytochrome c = H+ + ferrocytochrome c

672118, 674919, 395568

-

1.12.2.1

H2 + benzyl viologen = H+ + reduced benzyl viologen

395560

-

1.12.2.1

H2 + methylene blue = H+ + reduced methylene blue

395568, 395560, 690013

-

1.12.2.1

H2 + ferredoxin = H+ + reduced ferredoxin

395559

-

1.12.2.1

H2 + rubredoxin = H+ + reduced rubredoxin

395559

-

1.12.2.1

H2 + methyl viologen = H+ + reduced methyl viologen

395565

-

1.12.2.1

H2 + acceptor = H+ + reduced acceptor

701780

-

1.12.2.1

H2 + oxidized methyl viologen = H+ + reduced methyl viologen

701586

-

1.12.2.1

H2 + ferricytochrome Hmc = H+ + ferrocytochrome Hmc

654899

-

1.12.2.1

H2 + ammonium pertechnetate = ?

686422

-

1.12.2.1

ferricytochrome c3 + 2 H2 = ferrocytochrome c3 + 4 H+

701586

-

1.12.2.1

H2 + oxidized acceptor = H+ + reduced acceptor

704287

-

1.12.2.1

H2 + oxidized dichloroindophenol = H+ + ?

701586

-

1.12.2.1

H2 + potassium ferricyanide = H+ + ?

701586

-

1.12.2.1

H2 + methylviologen-dication = H+ + methylviologen

742696

-

1.12.5.1

H2 + 2,3-dimethyl-1,4-naphthoquinone = reduced 2,3-dimethyl-1,4-naphthoquinone

676044, 394192, 394193

-

1.12.5.1

H2 + benzyl viologen = reduced benzyl viologen

394192, 394193, 676044

-

1.12.5.1

H2 + menaquinone = menaquinol

676044

-

1.12.7.2

H2 + oxidized ferredoxin = H+ + reduced ferredoxin

439643, 685620, 685627, 439665, 439672, 439632, 439669, 439671, 439675, 439679, 439682, 439677, 712281, 712301, 712307, 439654, 688848, 439650, 686267, 684643

-

1.12.7.2

H2 + electron acceptor = H+ + reduced electron acceptor

439668, 439651, 439660, 439643, 439663, 439632, 439669, 439670, 439679, 439681, 439682, 439684, 439671, 439659, 439672, 439665, 439650, 439641, 439652, 439675, 439678, 439674, 439677

-

1.12.7.2

(SeO3)2- + H2 + ? = Se + H2O + ?

439661

-

1.12.7.2

(TeO3)2- + H2 + ? = Te + H2O + ?

439661

-

1.12.7.2

H2 + oxidized methyl viologen = H+ + reduced methyl viologen

684643, 686267, 686793, 712301, 688848

-

1.12.7.2

H2 + oxidized ferredoxin = reduced ferredoxin + H+

659110, 660222, 742859, 742784, 742698

-

1.12.7.2

H2 + ferredoxin + oxidized metronidazole = H+ + ferredoxin + reduced metronidazole

673529, 656734

-

1.12.7.2

H2 + oxidized benzyl viologen = reduced benzyl viologen + H+

673529

-

1.12.7.2

H2 + oxidized CAC3527 ferredoxin = H+ + reduced CAC3527 ferredoxin

686267

-

1.12.7.2

H2 + oxidized ferredoxin CAC0587 = H+ + reduced ferredoxin CAC0587

686793

-

1.12.7.2

H2 + oxidized flavodoxin CAC0587 = H+ + reduced flavodoxin CAC0587

686793

-

1.12.7.2

H2 + oxidized ferredoxin = reduced ferredoxin + 2 H+

705334

-

1.12.7.2

H2 + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H+

730867

-

1.12.7.2

H2 + oxidized ferredoxin Pet F = reduced ferredoxin Pet F + H+

742279

-

1.12.7.2

H2 + methyl viologen = reduced methyl viologen + H+

742859, 742698

-

1.12.7.2

H2 + oxidized spinach ferredoxin = reduced spinach ferredoxin + H+

742698

-

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

-

1.12.98.1

H2 + coenzyme F0 = reduced coenzyme F0

395097, 395086, 395089, 395093, 395080

-

1.12.98.1

H2 + methyl viologen = ?

395089, 395080, 395098, 395095, 395082, 395085, 395093, 395097, 395088

-

1.12.98.1

H2 + benzyl viologen = ?

395087, 395100

-

1.12.98.1

H2 + oxidized methyl viologen = reduced methyl viologen

727399

-

1.12.98.1

H2 + oxidized benzyl viologen = reduced benzyl viologen

395099

-

1.12.98.1

H2 + oxidized coenzyme F420 = reduced coenzyme F420

742368, 743086, 395099, 727399

-

1.12.98.1

H2 + oxidized coenzyme F0 = reduced coenzyme F20

395099

-

1.1.99.30

4 entries

1.12.1.2

13 entries

1.12.1.3

7 entries

1.12.1.4

3 entries

1.12.1.5

2 entries

1.12.2.1

16 entries

1.12.5.1

3 entries

1.12.7.2

16 entries

1.12.98.1

8 entries

1.12.98.2

5,10-methenyltetrahydromethanopterin + H2 = 5,10-methylenetetrahydromethanopterin + H+

657579, 658635, 658966, 658978, 696971

-

1.12.98.3

H2 + oxidized methyl viologen = reduced methyl viologen

440297

-

1.12.98.3

H2 + 2-(2,3-dihydropentaprenyloxy)phenazine = 2-dihydropentaprenyloxyphenazine

440300, 440299, 741956, 439643, 727829

-

1.12.98.3

H2 + 2-hydroxyphenazine = dihydro-2-hydroxyphenazine

440300, 440299

-

1.12.98.4

sulfur + H2 = H2S

659878

-

1.12.98.4

polysulfide + H2 = H2S

674514

-

1.12.98.4

S + H2 = H2S

674514

-

1.12.98.4

tetrathionate + H2 = ? + H+

674514

-

1.12.98.4

H2 + benzyl viologen = H2S + reduced benzyl viologen

439641

-

1.12.98.4

H2 + methyl viologen = H2S + reduced methyl viologen

722289, 439641

-

1.12.98.4

H2 + NADP+ = H2S + NADPH + H+

722289

-

1.12.98.4

H2 + polysulfide(n) = H2S + polysulfide(n-1)

439664, 439641

-

1.12.98.3

3 entries

1.12.98.4

8 entries

1.12.98.B1

H2 + sulfur = H2S

722508

-

1.12.99.6

H2 + benzyl viologen = reduced benzyl viologen

742788

-

1.12.99.6

H2 + benzyl viologen = H+ + reduced benzyl viologen

710951

-

1.12.99.6

H2 + methyl viologen = H+ + reduced methyl viologen

725206, 711516

-

1.12.99.6

H2 + acceptor = H+ + reduced acceptor

439630, 439644, 439633, 674448, 686733, 711862, 439637, 439628, 684463, 713374, 712029, 439638, 671937, 713368, 439645, 439641, 439627, 439643, 439649, 439647, 439631, 439635, 439640, 439648, 439634, 439632, 439636, 439642, 439646, 439629, 671432, 710927

-

1.12.99.6

H2 + S = H2S

439641

-

1.12.99.6

H2 + oxidized methyl viologen = H+ + reduced methyl viologen

706442, 684608, 726704, 704309, 688848, 704744, 703746

-

1.12.99.6

H2 + oxidized benzyl viologen = H+ + reduced benzyl viologen

439648, 686732, 702218, 702707, 703746

-

1.12.99.6

H2 + oxidized methylene blue = H+ + reduced methylene blue

711516, 704518, 703746

-

1.12.99.6

H2 + acceptor = acceptor-H2

684608, 658987, 657739, 659041

-

1.12.99.6

H2 + acceptor = acceptorH2

658082, 659887

-

1.12.99.6

H2 + 2,3-dimethyl-1,4-naphthoquinone = 2,3-dimethyl-naphthoquinol

659355

-

1.12.99.6

H2 + anthraquinone 2,6-disulfonic acid = anthraquinol 2,6-disulfonic acid

657605

-

1.12.99.6

H2 + Cr6+ = Cr3+ + H+

657622

-

1.12.99.6

H2 + oxidized 2,3-dimethylnaphthoquinone = 2,3-dimethylnaphthoquinol

659878

-

1.12.99.6

H2 + oxidized benzyl viologen = reduced benzyl viologen

658082

-

1.12.99.6

H2 + oxidized benzyl viologen = reduced benzyl viologen + H+

658082, 659355, 657605, 659878, 658138, 672638

-

1.12.99.6

H2 + oxidized diquat = reduced diquat + H+

657605

-

1.12.99.6

H2 + oxidized ethyl viologen = reduced ethyl viologen + H+

657605

-

1.12.99.6

H2 + oxidized methyl viologen = reduced methyl viologen + H+

657778, 672729, 658972, 657622, 657605, 659878, 659310, 659520, 658138

-

1.12.99.6

H2 + oxidized metranidazole = H+ + reduced metranidazol

659523

-

1.12.99.6

H2 + oxidized phenazine methosulfate = reduced phenazine methosulfate + H+

657605

-

1.12.99.6

H2 + 2,4,6-trinitrotoluene = ?

675221

-

1.12.99.6

H2 + oxidized methylene blue = reduced methylene blue + H+

674936

-

1.12.99.6

H2 + acceptor = H2-acceptor

687302, 684596

-

1.12.99.6

H2 + methenyltetrahydromethanopterin = H+ + methylenetetrahydromethanopterin

690060, 687827

-

1.12.99.6

H2 + oxidized amaranth = H+ + reduced amaranth

684651

-

1.12.99.6

H2 + oxidized benzyl viologen = H+ + reduceded benzyl viologen

685293

-

1.12.99.6

H2 + oxidized acceptor = H+ + reduced acceptor

704016, 701778, 704489, 702254, 704162

-

1.12.99.6

H2 + oxidized electron acceptor = H+ + reduced electron acceptor

702307, 704015, 704013, 704012, 687302

-

1.12.99.6

H2 + O2 = ?

713401, 710927

-

1.12.99.6

H2 + oxidized dichloroindophenol = H+ + reduced dichloroindophenol

711516

-

1.12.99.6

H2 + oxidized sodium hydrosulfite = H+ + reduced sodium hydrosulfite

711516

-

1.12.99.6

H2 + phenazine methosulfate = H+ + reduced phenazine methosulfate

711516

-

1.12.99.6

H2 + acceptor = reduced acceptor

742652

-

1.12.99.6

H2 + methylene blue = reduced methylene blue

742265

-

1.12.99.6

H2 + NADPH = NADP + H+

743732

-

1.12.99.6

H2 + 2,3,5-triphenyltetrazolium chloride = reduced 2,3,5-triphenyltetrazolium chloride

742788

-

1.12.99.6

H2 + fumarate = succinate

742788

-

1.12.99.6

38 entries

1.14.14.9

2-phenylbutyric acid + H2 = ?

438895

-

1.18.6.2

acetylene + H2 + ? = ethylene + ?

745388

-

1.2.1.B29

H2 + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster = NADPH + 3 H+ + 2 reduced ferredoxin [iron-sulfur] cluster

734087

-

1.2.1.B29

H2 + NADP+ + 2 oxidized methyl viologen = ? + NADPH + H+ + 2 reduced methyl viologen

734087

-

1.2.1.B29

2 entries

1.2.7.4

H2 + reduced methyl viologen = methyl viologen

655446

-

1.21.99.5

tetrachloroethene + 2 H2 = cis-1,2-dichloroethene + 2 chloride + 2 H+

657605

-

1.8.98.1

N-(7-[(2-sulfoethyl)dithio]heptanoyl)-3-O-phospho-L-threonine + H2 = coenzyme B + coenzyme M

655396, 655400, 655398, 655471, 655531, 655825, 654385, 639391

-

1.8.98.5

coenzyme B-coenzyme M disulfide + ferredoxin + 2 H2 = coenzyme B + coenzyme M + reduced ferredoxin2- + 2 H+

726376

-

1.8.98.5

coenzyme B-coenzyme M disulfide + metronidazole + 2 H2 = coenzyme B + coenzyme M + reduced metronidazole2- + 2 H+

726376

-

1.8.98.5

H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB = reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+

744833, 744179

-

1.8.98.5

H2 + oxidized methyl viologen + CoM-S-S-CoB = reduced methyl viologen + CoB + CoM + H+

744833, 744179

-

1.8.98.5

4 entries

1.9.3.1

reduced N,N,N',N'-tetramethyl-4-phenylenediamine + O2 + H2 = oxidized N,N,N',N'-tetramethyl-4-phenylenediamine + H2O

743382

-

1.97.1.9

selenate + H2 = selenite + H2O

658902

-

3.1.1.4

phosphatidylcholine + H2 = 1-acylglycerophosphocholine + fatty acid

729340

-

3.1.2.1

H2 + CO2 + CH3-H4SPt + CoASH = acetyl-CoA + H4SPt + H2O

94491

-

3.1.3.7

3'-phosphoadenosine 5'-phosphate + H2 = AMP + phosphate

730884

-

3.4.21.B12

urokinase-type plasminogen activator receptor + H2 = ?

664270

-

3.4.22.15

fibronectin + H2 = ?

727746

-

3.4.22.15

laminin + H2 = ?

727746

-

3.4.22.15

vitronectin + H2 = ?

727746

-

3.4.22.15

3 entries

Product in Enzyme-catalyzed Reactions (54 results)

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Show Product (54 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.37

(S)-malate + NAD+ = acetate + CO2 + H2 + NADH

286670

-

1.11.1.16

2 Mn2+ + 2 H+ = 2 Mn3+ + H2

-

-

1.12.1.2

H+ + reduced methyl viologen = H2 + methyl viologen

-

-

1.12.1.2

H+ + reduced methyl viologen = H2 + oxidized methyl viologen

-

-

1.12.1.2

H+ + NADH = H2 + NAD+

-

-

1.12.1.2

H+ + NADPH = H2 + NADP+

-

-

1.12.1.2

H+ + NADH + reduced ferredoxin = H2 + NAD+ + oxidized ferredoxin

-

-

1.12.1.2

H+ + reduced dithionite = H2 + oxidized dithionite

-

-

1.12.1.3

H+ + reduced benzyl viologen = H2 + oxidized benzyl viologen

-

-

1.12.1.3

H+ + NADPH = H2 + NADP+

-

-

1.12.1.3

NADPH + H+ = H2 + NADP+

-

-

1.12.1.4

NADH + H+ + reduced ferredoxin = H2 + NAD+ + oxidized ferredoxin

-

-

1.12.1.4

NADH + H+ + reduced methyl viologen = H2 + NAD+ + oxidized methyl viologen

-

-

1.12.1.4

sodium dithionite + H+ + reduced anthraquinone-2,6-disulfonic acid = H2 + oxidized anthraquinone-2,6-disulfonic acid + ?

-

-

1.12.1.4

sodium dithionite + H+ + reduced methyl viologen = H2 + oxidized methyl viologen + ?

-

-

1.12.1.4

NADH + 3 H+ + 2 reduced ferredoxin = NAD+ + 2 oxidized ferredoxin + 2 H2

-

-

1.12.1.4

NADH + 3 H+ + 2 reduced methyl viologen = NAD+ + 2 oxidized methyl viologen + 2 H2

-

-

1.12.1.5

H+ + reduced methyl viologen = H2 + oxidized methyl viologen

-

-

1.12.1.5

H+ + NADPH = H2 + NADP+

-

-

1.12.2.1

H+ + ferrocytochrome c3 = H2 + ferricytochrome c3

-

-

1.12.2.1

H+ + neutral red = H2 + oxidized neutral red

-

-

1.12.2.1

H+ + phenosafranine = H2 + oxidized phenosafranine

-

-

1.12.2.1

H+ + reduced methyl viologen = H2 + methyl viologen

-

-

1.12.2.1

reduced methyl viologen + H+ = oxidized methyl viologen + H2

-

-

1.12.7.2

H+ + reduced ferredoxin = H2 + oxidized ferredoxin

-

-

1.12.7.2

H+ + reduced methyl viologen = H2 + oxidized methyl viologen

-

-

1.12.7.2

2 H+ + reduced ferredoxin = H2 + oxidized ferredoxin

-

-

1.12.7.2

2 H+ + reduced polyferredoxin = H2 + oxidized polyferredoxin

-

-

1.12.7.2

H+ + reduced benzyl viologen = H2 + oxidized benzyl viologen

-

-

1.12.98.2

N5,N10-methylenetetrahydromethanopterin + H+ = N5,N10-methenyltetrahydromethanopterin + H2

394696

-

1.12.98.2

H+ + 5,10-methylenetetrahydromethanopterin = H2 + 5,10-methenyltetrahydromethanopterin

-

-

1.12.98.4

H2S + NADH + H+ = H2 + NAD+

-

-

1.12.98.4

H2S + NADPH + H+ = H2 + NADP+

-

-

1.12.1.2

6 entries

1.12.1.3

3 entries

1.12.1.4

6 entries

1.12.1.5

2 entries

1.12.2.1

5 entries

1.12.7.2

5 entries

1.12.98.2

2 entries

1.12.98.4

2 entries

1.12.99.6

formate = H2 + CO2

-

-

1.14.14.32

17alpha-hydroxypregnenolone + [reduced NADPH-hemoprotein reductase] + O2 = 3beta-hydroxyandrost-5-en-17-one + acetate + [oxidized NADPH-hemoprotein reductase] + H2

-

-

1.18.6.1

8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate

440145, 440134, 440143, 440144, 440151, 440142, 440171, 440176, 440177, 440140, 440146, 440147, 440149, 440152, 440157, 440166, 440174, 440153, 440159, 440164, 440180, 440150, 440155, 440156, 440158, 440163, 440178, 440179, 440181, 440183, 440184, 440187, 440188, 440189, 440169, 440162, 440148, 440165, 440170, 440161, 440167, 440168, 440160, 440138, 440154, 440186, 440175, 440182

-

1.18.6.1

reduced ferredoxin + H+ + ATP = oxidized ferredoxin + H2 + ADP + phosphate

440184, 440187, 440189, 440176

-

1.18.6.1

reduced ferredoxin + H+ + N2 + ATP + H2O = oxidized ferredoxin + H2 + NH3 + ADP + phosphate

-

-

1.18.6.1

C2H2 + ? = H2 + ?

-

-

1.18.6.1

N2 + 8 e- + 16 ATP + 8 H+ = 2 NH3 + H2 + 16 ADP + 16 phosphate

-

-

1.18.6.1

reduced ferredoxin + H+ + N2 + ATP = oxidized ferredoxin + H2 + NH3 + ADP + phosphate

-

-

1.18.6.1

N2 + 8 e- + 8 H+ + 16 ATP = 2 NH3 + H2 + 16 ADP + 16 phosphate

-

-

1.18.6.1

N2 + 10 H+ + 8 e- + 16 ATP = 2 NH4+ + H2 + 16 ADP + 16 phosphate

-

-

1.18.6.2

12 reduced ferredoxin + 12 H+ + N2 + 40 ATP + 40 H2O = 12 oxidized ferredoxin + 3 H2 + 2 NH3 + 40 ADP + 40 phosphate

-

-

1.18.6.2

CO + H+ + ATP = C2H4 + C2H6 + C3H8 + H2O + H2 + phosphate

-

-

1.19.6.1

reduced ferredoxin + H+ + N2 + ATP = oxidized ferredoxin + H2 + NH3 + ADP + phosphate

-

-

1.19.6.1

reduced flavodoxin + N2 + ATP + H2O = oxidized flavodoxin + H2 + NH3 + ADP + phosphate

-

-

1.19.6.1

reduced flavodoxin II + N2 + ATP + H2O = oxidized flavodoxin II + H2 + NH3 + ADP + phosphate

-

-

1.18.6.1

8 entries

1.18.6.2

2 entries

1.19.6.1

3 entries

1.2.1.B29

NADPH + 3 H+ + 2 reduced ferredoxin [iron-sulfur] cluster = H2 + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster

-

-

1.2.7.4

CO + H2O = CO2 + H2

390485

-

1.2.7.4

CO + H2O + methylene blue = CO2 + reduced methylene blue + H2

-

-

1.2.7.4

2 entries

1.8.98.1

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

-

-

1.8.98.5

reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+ = H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB

-

-

1.8.98.5

reduced metronidazole + CoB + CoM + H+ = H2 + oxidized metronidazole + CoM-S-S-CoB

-

-

1.8.98.5

2 entries

Activator in Enzyme-catalyzed Reactions (2 results)

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Show Activating Compound (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.8.4.1

suggested to be involved in the activation of the methylreductase, preincubation

393257

-

7.2.2.11

stimulates

210289

-

Inhibitor in Enzyme-catalyzed Reactions (9 results)

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Show Inhibitors (9 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.12.98.2

inhibits formation of N5,N10-methenyltetrahydromethanopterin

394694

-

1.12.99.6

inhibits hydrogen production

674190

-

1.18.6.1

competitive inhibitor of N2, no inhibition of N3-, C2H2, CN- or H+ reduction

440146

-

1.18.6.1

-

440144, 440146, 440154, 440158

-

1.18.6.1

competitive

440183

-

1.18.6.1

competitive inhibition of N2 binding

658040

-

1.18.6.1

H2 competes with N2 binding and inhibits N2 reduction by the FeMo protein, but H2 does not inhibit NO2- reduction for the wild-type or either of the two MoFe protein variants

742740

-

1.18.6.1

5 entries

1.18.6.2

CO-reduction by V-nitrogenase is inhibited by the addition of increasing amounts of H2

746492

-

1.19.6.1

inhibits both N2 and diazene reduction

685165

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (11 results)

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Show Turnover Number (11 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.12.1.2

70

-

pH 8.0, HoxI deletion mutant enzyme, with oxidized benzyl viologen

655890

1.12.1.2

109

-

pH 8.0, HoxI deletion mutant enzyme, with NAD+

655890

1.12.1.2

120

-

pH 8.0, wild-type enzyme complex including HoxI, with oxidized benzyl viologen

655890

1.12.1.2

143

-

pH 8.0, wild-type enzyme complex including HoxI, with NAD+

655890

1.12.1.2

212

-

-

439706

1.12.1.2

284

-

pH 8.0, HoxI deletion mutant enzyme, with ferrocyanide

655890

1.12.1.2

372

-

pH 8.0, wild-type enzyme complex including HoxI, with ferrocyanide

655890

1.12.7.2

0.683

-

-

439659

1.12.7.2

133

-

using ferredoxin CAC0587 as electron carrier, at 35°C

686793

1.12.7.2

454

-

using methyl viologen as electron carrier, at 35°C

686793

1.12.7.2

483

-

using flavodoxin CAC0587 as electron carrier, at 35°C

686793

1.12.1.2

7 entries

1.12.7.2

4 entries

K_M Value (39 results)

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Show KM Value (39 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.12.1.2

0.037

-

-

439699

1.12.1.2

0.063

-

-

439701

1.12.1.2

0.19

-

-

439693

1.12.1.3

0.012

-

-

439691

1.12.1.3

0.018

-

cosubstrate: benzyl viologen

687409

1.12.1.3

0.02

-

cosubstrate: methyl viologen

687409

1.12.1.2

3 entries

1.12.1.3

3 entries

1.12.1.4

-999

-

apparent Km value for H2 is about 6% in the gas phase, pH 7.5, 45°C

740618

1.12.7.2

0.000033

-

using ferredoxin CAC0587 as electron carrier, at 35°C

686793

1.12.7.2

0.000088

-

using flavodoxin CAC0587 as electron carrier, at 35°C

686793

1.12.7.2

0.005

-

-

439643

1.12.7.2

0.005

-

-

659110

1.12.7.2

0.016

-

using methyl viologen as electron carrier, at 35°C

686793

1.12.7.2

0.341

-

-

439659

1.12.7.2

5.6

-

-

439663

1.12.98.1

0.002

-

+ methyl viologen, pH 9

395080

1.12.98.1

0.003

-

37°C, pH 7.2, cosubstrate: oxidized coenzyme F420

395099

1.12.98.1

0.004

-

37°C, pH 7.2, cosubstrate: oxidized methyl viologen

395099

1.12.98.1

0.01

-

+ coenzyme F0, pH 7.2

395080

1.12.98.1

0.012

-

-

395089

1.12.98.2

-999

-

the apparent Km for H2 is estimated to be approximately 60% H2 in the gas phase

727402

1.12.98.2

-999

-

apparent Km for H2 is 60%

727402

1.12.98.2

0.15

-

-

394696

1.12.99.6

0.000047

-

apparent value, pH and temperature not specified in the publication

711862

1.12.99.6

0.0004

-

at pH 5.5, 10°C

713401

1.12.99.6

0.001

-

-

439646

1.12.99.6

0.001

-

at pH 5.5, 20°C

713401

1.12.99.6

0.002

-

-

439648

1.12.99.6

0.005

-

-

439643

1.12.99.6

0.006

-

at pH 4.5, 30°C; at pH 5.5, 30°C

713401

1.12.99.6

0.008

-

at pH 5.0, 30°C

713401

1.12.99.6

0.01

-

at pH 6.5, 30°C

713401

1.12.99.6

0.0113

-

-

439647

1.12.99.6

0.015

-

at pH 6.0, 30°C

713401

1.12.99.6

0.024

-

at pH 5.5, 40°C

713401

1.12.99.6

0.08

-

with methylene blue as electron acceptor

439632

1.12.99.6

0.41

-

with methyl viologen as electron acceptor

439634

1.12.99.6

1.9

-

with methyl viologen as electron acceptor

439632

1.12.99.6

25

-

-

439631

1.12.7.2

7 entries

1.12.98.1

5 entries

1.12.98.2

3 entries

1.12.99.6

16 entries

1.8.98.1

0.03

-

pH 7, 65°C, H2: heterodisulfide oxidoreductase complex

655398

References & Links

Literature References (344)

top print hide

Show Reference (344 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

94491

7718564

Substrate and accessory protein requirements and thermodynamics of acetyl-CoA synthesis and cleavage in Methanosarcina barkeri

1995

Grahame, D.A.; de Moll, E.

Biochemistry

34

4617-4624

210289

2757374

Nickel transport by the thermophilic acetogen Acetogenium kivui

1989

Yang, H.; Daniel, S.L.; Hsu, T.; Drake, H.L.

Appl. Environ. Microbiol.

55

1078-1081

246745

-

Effect of methanogenic substrates on coenzyme f420-dependent N5,N10-methylene-H4MPT dehydrogenase, N5,N10-methenyl-H4MPT cyclohydrolase and F420-reducing hydrogenase activities in Methanosarcina barkeri

1993

Mukhopadhyay, B.; Purwantini, E.; Daniels, L.

Arch. Microbiol.

159

141-146

286670

9269720

Isolation and characterization of cytosolic malate dehydrogenase from Trichomonas vaginalis

1997

Drmota, T.; Tachezy, J.; Kulda, J.

Folia Parasitol.

44

103-108

390485

11509720

Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster

2001

Dobbek, H.; Svetlitchnyi, V.; Gremer, L.; Huber, R.; Meyer, O.

Science

293

1281-1285

393257

3137210

Reductive activation of the methyl coenzyme M methylreductase system of Methanobacterium thermoautotrophicum.DELTA.H

1988

Rouviere, P.E.; Bobik, T.A.; Wolfe, R.S.

J. Bacteriol.

170

3946-3952

394192

1587288

The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes

1992

Dross, F.; Geisler, V.; Lenger, R.; Theis, F.; Krafft, T.; Fahrenholz, F.; Kojro, E.; Duchene, A.; Tripier, D.; Juvenal, K.; Krueger, A.

Eur. J. Biochem.

206

93-102

394193

8319698

Erratum

1993

Dross, F.; Geisler, V.; Lenger, R.; Theis, F.; Krafft, T.; Fahrenholz, F.; Kojro, E.; Duchene, A.; Tripier, D.; Juvenal, K.; Krueger, A.

Eur. J. Biochem.

214

949-950

394694

-

N5,N10-Methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum has hydrogenase activity

1990

Zirngibl, C.; Hedderich, R.; Thauer, R.K.

FEBS Lett.

261

112-116

394696

8599536

Purification, properties and primary structure of H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase from Methanococcus thermolithotrophicus

1996

Hartmann, G.C.; Klein, A.R.; Linder, M.; Thauer, R.K.

Arch. Microbiol.

165

187-193

395079

6211447

A selenium-containing hydrogenase from Methanococcus vannielii. Identification of the selenium moiety as a selenocysteine residue

1982

Yamazaki, S.

J. Biol. Chem.

257

7926-7929

395080

7061485

Purification and properties of an 8-hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum

1982

Jacobson, F.S.; Daniels, L.; Fox, J.A.; Walsh, C.T.; Orme-Johnson, W.H.

J. Biol. Chem.

257

3385-3388

395081

6300837

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

1983

Kojima, N.; Fox, J.A.; Hausinger, R.P.; Daniels, L.; Orme-Johnson, W.H.; Walsh, C.

Proc. Natl. Acad. Sci. USA

80

378-382

395082

-

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

1983

Jin, S.L.C.; Blanchard, D.K.; Chen, J.S.

Biochim. Biophys. Acta

748

8-20

395083

6375661

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

1984

Nelson, M.J.K.; Brown, D.P.; Ferry, J.G.

Biochem. Biophys. Res. Commun.

120

775-781

395084

3804976

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

1987

Wackett, L.P.; Hartwieg, E.A.; King, J.A.; Orme-Johnson, W.H.; Walsh, C.T.

J. Bacteriol.

169

718-727

395085

3301819

Locations of the hydrogenases of Methanobacterium formicicum after subcellular fractionation of cell extract

1987

Baron, S.F.; Brown, D.P.; Ferry, J.G.

J. Bacteriol.

169

3823-3825

395086

3663585

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

4219-4227

395087

-

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

1987

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

Can. J. Microbiol.

33

896-904

395088

3121317

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

1987

Muth, E.; Mörschel, E.; Klein, A.

Eur. J. Biochem.

169

571-577

395089

3663586

8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 2. Kinetic and hydrogen-transfer studies

1987

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

Biochemistry

26

4228-4237

395090

-

Localization of the F420-reducing hydrogenase in Methanococcus voltae cells by immuno-gold technique

1988

Muth, E.

Arch. Microbiol.

150

205-207

395092

-

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

1989

Baron, S.F.; Williams, D.S.; May, H.D.; Patel, P.S.; Aldrich, H.C.; Ferry, J.G.

Arch. Microbiol.

151

307-313

395093

2738024

Purification and properties of the membrane-associated coenzyme F420-reducing hydrogenase from Methanobacterium formicicum

1989

Baron, S.F.; Ferry, J.G.

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