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Ligand 5,10-methenyl-5,6,7,8-tetrahydromethanopterin

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

methanogenesis from CO2

KEGG

Carbon metabolism, Methane metabolism, Microbial metabolism in diverse environments

MetaCyc

3PG-factor 420 biosynthesis, factor 420 biosynthesis I (archaea), factor 420 biosynthesis II (mycobacteria), formaldehyde oxidation VI (H4MPT pathway), methanogenesis from H2 and CO2, methoxylated aromatic compound degradation II, reductive acetyl coenzyme A pathway II (autotrophic methanogens) more

Show all BRENDA pathways known for 5,10-methenyl-5,6,7,8-tetrahydromethanopterin

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (6 results)

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Show Natural Substrate (6 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.12.98.2

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

657579, 658635, 658966, 658978, 696971

6hae, 3D-view

1.12.98.2

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

657579, 658635, 658966, 658978, 696971

6hav, 3D-view

1.12.98.2

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

657579, 658635, 658966, 658978, 696971

6hux, 3D-view

1.12.98.2

3 entries

1.5.98.1

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

696301

-

3.5.4.27

5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = 5-formyl-5,6,7,8-tetrahydromethanopterin

755911, 719205, 721676, 727375

-

3.5.4.27

5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = ?

246743, 246745, 246737, 209741

-

3.5.4.27

2 entries

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

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.98.1

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

0

-

3.5.4.27

formyl-tetrahydromethanopterin = methenyl-tetrahydromethanopterin + H2O

0

-

Substrate in Enzyme-catalyzed Reactions (8 results)

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Show Substrate (8 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.12.98.2

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

657579, 658635, 658966, 658978, 696971

6hae, 3D-view

1.12.98.2

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

657579, 658635, 658966, 658978, 696971

6hav, 3D-view

1.12.98.2

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

657579, 658635, 658966, 658978, 696971

6hux, 3D-view

1.12.98.2

3 entries

1.12.99.6

H2 + methenyltetrahydromethanopterin = H+ + methylenetetrahydromethanopterin

690060, 687827

-

1.5.98.1

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

696301

-

3.5.4.27

5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = 5-formyl-5,6,7,8-tetrahydromethanopterin

755911, 719205, 721676, 727375

-

3.5.4.27

5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = ?

246743, 246745, 246737, 209741

-

3.5.4.27

5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = N5-formyl-5,6,7,8-tetrahydromethanopterin

246743, 246745, 246739, 246744, 246740, 246742, 246741, 209741, 246737, 246738

-

3.5.4.27

3 entries

Product in Enzyme-catalyzed Reactions (8 results)

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Show Product (8 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.12.98.2

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

0

6hae, 3D-view

1.12.98.2

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

0

6hav, 3D-view

1.12.98.2

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

0

6hux, 3D-view

1.12.98.2

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

0, 394696

6hae, 3D-view

1.12.98.2

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

0, 394696

6hav, 3D-view

1.12.98.2

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

0, 394696

6hux, 3D-view

1.12.98.2

6 entries

1.5.98.1

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

288524, 13757, 13748, 13747, 0, 13750, 13752, 13753, 288527, 486086, 13749, 13755

-

3.5.4.27

formyl-tetrahydromethanopterin = methenyl-tetrahydromethanopterin + H2O

0

-

3D Structure of Enzyme-Ligand-Complex (PDB) (19 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (19 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.12.98.2

6hae, 3D-view

1.12.98.2

6hav, 3D-view

1.12.98.2

6hux, 3D-view

1.12.98.2

6hae, 3D-view

1.12.98.2

6hav, 3D-view

1.12.98.2

6hux, 3D-view

1.12.98.2

6hae, 3D-view

1.12.98.2

6hav, 3D-view

1.12.98.2

6hux, 3D-view

1.12.98.2

6hae, 3D-view

1.12.98.2

6hav, 3D-view

1.12.98.2

6hux, 3D-view

1.12.98.2

6hae, 3D-view

1.12.98.2

6hav, 3D-view

1.12.98.2

6hux, 3D-view

1.12.98.2

6hae, 3D-view

1.12.98.2

6hav, 3D-view

1.12.98.2

6hux, 3D-view

1.12.98.2

18 entries

1.5.99.9

3iqf, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (1 result)

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Show Turnover Number (1 entry)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.12.98.2

975

-

pH 7.5, 60°C

727402

K_M Value (23 results)

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Show KM Value (23 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.12.98.2

0.05

-

pH 7.5, 60°C

727402

1.12.98.2

0.07

-

pH and temperature not specified in the publication

727402

1.12.98.2

0.85

-

-

394696

3.5.4.27

0.025

-

pH 7.6, 65°C, mutant enzyme R183E

721676

3.5.4.27

0.026

-

pH 7.6, 65°C, mutant enzyme E186A

721676

3.5.4.27

0.03

-

-

209741

3.5.4.27

0.03

-

recombinant enzyme

246743

3.5.4.27

0.04

-

-

246743

3.5.4.27

0.043

-

pH 7.6, 65°C, mutant enzyme R183A

721676

3.5.4.27

0.043

-

pH 7.6, 65°C, mutant enzyme R183K

721676

3.5.4.27

0.043

-

pH 7.6, 65°C, mutant enzyme R183Q

721676

3.5.4.27

0.047

-

pH 7.6, 65°C, mutant enzyme K94V

721676

3.5.4.27

0.05

-

pH 7.6, 65°C, mutant enzyme E186N

721676

3.5.4.27

0.055

-

pH 7.6, 65°C, wild-type enzyme

721676

3.5.4.27

0.06

-

pH 7.6, 10°C

727375

3.5.4.27

0.062

-

pH 7.6, 65°C, mutant enzyme E186D

721676

3.5.4.27

0.077

-

pH 7.6, 65°C, mutant enzyme K94E

721676

3.5.4.27

0.1

-

1 M K2HPO4

246741

3.5.4.27

0.14

-

0.6 M K2HPO4

246741

3.5.4.27

0.2

-

0.3 M K2HPO4

246741

3.5.4.27

0.22

-

-

246740

3.5.4.27

0.57

-

-

246739

3.5.4.27

2

-

-

246741

1.12.98.2

3 entries

3.5.4.27

20 entries

References & Links

Literature References (35)

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Show Reference (35 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

13747

2307649

Protein content and enzyme activities in methanol- and acetate-grown Methanosarcina thermophila

1990

Jablonski, P.E.; DiMarco, A.A.; Bobik, T.A.; Cabell, M.C.; Ferry, J.G.

J. Bacteriol.

172

1271-1275

13748

-

Function of methanofuran, tetramethanopterin, and coenzyme F420 in Archaeoglobus fulgidus

1989

Moeller-Zinkhan, D.; Boerner, G.; Thauer, R.K.

Arch. Microbiol.

152

362-368

13749

2743220

Aerobic purification of N5,N10-methylenetetrahydromethanopterin dehydrogenase, separated from N5,N10-methenyltetrahydromethanopterin cyclohydrolase, from Methanobacterium thermoautotrophicum strain Marburg

1989

Mukhopadhyay, B.; Daniels, L.

Can. J. Microbiol.

35

499-507

13750

4084309

Coenzyme dependence of the methylenetetrahydromethanopterin dehydrogenase of Methanobacterium thermoautotrophicum

1985

Hartzell, P.L.; Zvilius, G.; Escalante-Semerena, J.C.; Donnelly, M.I.

Biochem. Biophys. Res. Commun.

133

884-890

13752

1991149

Purification and characterization of coenzyme F420-dependent 5,10-methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautothrophicum strain DELTAH

1991

te Broemmelstroet, B.W.; Hensgens, C.M.H.; Keltjens, J.T.; van der Drift, C.; Vogels, G.D.

Biochim. Biophys. Acta

1073

77-84

13753

7851382

Re-face specificity at C14a of methylenetetrahydromethanopterin and si-face specificity at C5 of coenzyme F420 for coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase from methanogenic archaea

1995

Klein, A.R.; Thauer, R.K.

Eur. J. Biochem.

227

169-174

13755

8215796

Two N5,N10-methylenetetrahydromethanopterin dehydrogenases in the extreme thermophile Methanopyrus kandleri: characterization of the coenzyme F420-dependent enzyme

1993

Klein, A.R.; Koch, J.; Stetter, K.O.; Thauer, R.K.

Arch. Microbiol.

160

186-192

13757

7852356

Cloning, sequencing, and transcriptional analysis of the coenzyme F420-dependent methylene-5,6,7,8-tetrahydromethanopterin dehydrogenase gene from Methanobacterium thermoautotrophicum strain Marburg and functional expression in Escherichia coli

1995

Mukhopadhyay, B.; Purwantini, E.; Pihl, T.D.; Reeve, J.N.; Daniels, L.

J. Biol. Chem.

270

2827-2832

209741

10215859

A methenyl tetrahydromethanopterin cyclohydrolase and a methenyl tetrahydrofolate cyclohydrolase in Methylobacterium extorquens AM1

1999

Pomper, B.K.; Vorholt, J.A.; Chistoserdova, L.; Lidstrom, M.E.; Thauer, R.K.

Eur. J. Biochem.

261

475-480

246737

4062290

Methenyl-tetrahydromethanopterin cyclohydrolase in cell extracts of Methanobacterium

1985

Donnelly, M.I.; Escalante-Semerena, J.C.; Rinehart, K.L.; Wolfe, R.S.

Arch. Biochem. Biophys.

242

430-439

246738

3782039

Purification and properties of the 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanobacterium thermoautotrophicum

1986

Dimarco, A.A.; Donnelly, M.I.; Wolfe, R.S.

J. Bacteriol.

168

1372-1377

246739

2298699

Purification and properties of 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanosarcina barkeri

1990

te Boemmelstroet, B.W.; Hensgens, C.M.H.; Geerts, W.J.; Keltjens, J.T.; van der Drift, C.; Vogels, G.D.

J. Bacteriol.

172

564-571

246740

8481088

N5,N10-Methenyltetrahydromethanopterin cyclohydrolase from the extremely thermophilic sulfate reducing Archaeoglobus fulgidus: comparison of its properties with those of the cyclohydrolase from the extremely thermophilic Methanopyrus kandleri

1993

Klein, A.R.; Breitung, J.; Linder, D.; Stetter, K.O.; Thauer, R.K.

Arch. Microbiol.

159

213-219

246741

-

N5,N10-Methenyltetrahydromethanopterin cyclohydrolase from the extreme thermophile Methanopyrus kandleri: increase of the catalytic efficiency (kcat/KM) and thermostability in the presence of salts

1991

Breitung, J.; Schmitz, R.A.; Stetter, K.O.; Thauer, R.K.

Arch. Microbiol.

156

517-524

246742

10545331

The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri

1999

Grabarse, W.; Vaupel, M.; Vorholt, J.A.; Shima, S.; Thauer, R.K.; Wittershagen, A.; Bourenkov, G.; Bartunik, H.D.; Ermler, U.

Structure Fold. Des.

7

1257-1268

246743

9676239

Overproduction and one-step purification of the N5,N10-methenyltetrahydromethanopterin cyclohydrolase (Mch) from the hyperthermophilic Methanopyrus kandleri

1998

Vaupel, M.; Vorholt, J.A.; Thauer, R.K.

Extremophiles

2

15-22

246744

10482517

Distribution of tetrahydromethanopterin-dependent enzymes in methylotrophic bacteria and phylogeny of methenyl tetrahydromethanopterin cyclohydrolase

1999

Vorholt, J.A.; Christoserdova, L.; Stolyar, S.M.; Thauer, R.K.; Lidstrom, M.E.

J. Bacteriol.

181

5750-5757

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

288524

1911853

Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri

1991

te Brommelstroet, B.W.; Geerts, W.J.; Keltjens, J.T.; van der Drift, C.; Vogels, G.D.

Biochim. Biophys. Acta

1079

293-302

288527

8319675

Si-face stereospecificity at C5 of coenzyme F420 for F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase, F420-dependent N5,N10-methylenetetrahydromethanopterin reductase and F420H2:dimethylnaphthoquinone oxidoreductase

1993

Kunow, J.; Schwoerer, B.; Setzke, E.; Thauer, R.K.

Eur. J. Biochem.

214

641-646

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

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.

Arch. Microbiol.

159

225-232

657579

11872465

Differential expression of methanogenesis genes of Methanothermobacter thermoautotrophicus (formerly Methanobacterium thermoautotrophicum) in pure culture and in cocultures with fatty acid-oxidizing syntrophs

2002

Luo, H.W.; Zhang, H.; Suzuki, T.; Hattori, S.; Kamagata, Y.

Appl. Environ. Microbiol.

68

1173-1179

658635

14686932

UV-A/blue-light inactivation of the ‘metal-free’ hydrogenase (Hmd) from methanogenic archaea. The enzyme contains functional iron after all

2004

Lyon, E.J.; Shima, S.; Buurman, G.; Chowdhuri, S.; Batschauer, A.; Steinbach, K.; Thauer, R.K.

Eur. J. Biochem.

271

195-204

658966

14582997

Measurement and ab initio calculation of CSA/dipole-dipole cross-correlated relaxation provide insight into the mechanism of a H2-forming dehydrogenase

2003

Bartoschek, S.; Buurman, G.; Geierstanger, B.H.; Lapham, J.; Griesinger, C.

J. Am. Chem. Soc.

125

13308-13309

658978

15506791

Carbon monoxide as an intrinsic ligand to iron in the active site of the iron-sulfur-cluster-free hydrogenase H2-forming methylenetetrahydromethanopterin dehydrogenase as revealed by infrared spectroscopy

2004

Lyon, E.J.; Shima, S.; Boecher, R.; Thauer, R.K.; Grevels, F.W.; Bill, E.; Roseboom, W.; Albracht, S.P.J.

J. Am. Chem. Soc.

126

14239-14248

687827

17924153

The exchange activities of [Fe] hydrogenase (iron-sulfur-cluster-free hydrogenase) from methanogenic archaea in comparison with the exchange activities of [FeFe] and [NiFe] hydrogenases

2008

Vogt, S.; Lyon, E.J.; Shima, S.; Thauer, R.K.

J. Biol. Inorg. Chem.

13

97-106

690060

18653896

The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site

2008

Shima, S.; Pilak, O.; Vogt, S.; Schick, M.; Stagni, M.S.; Meyer-Klaucke, W.; Warkentin, E.; Thauer, R.K.; Ermler, U.

Science

321

572-575

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

719205

20453896

Differentially expressed genes after hyper- and hypo-salt stress in the halophilic archaeon Methanohalophilus portucalensis

2010

Shih, C.J.; Lai, M.C.

Can. J. Microbiol.

56

295-307

721676

23013430

Structure and catalytic mechanism of N5,N10-methenyl-tetrahydromethanopterin cyclohydrolase

2012

Upadhyay, V.; Demmer, U.; Warkentin, E.; Moll, J.; Shima, S.; Ermler, U.

Biochemistry

51

8435-8443

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

727402

1521540

H2-forming methylenetetrahydromethanopterin dehydrogenase, a novel type of hydrogenase without iron-sulfur clusters in methanogenic archaea

1992

Zirngibl, C.; Van Dongen, W.; Schwörer, B.; Von Bünau, R.; Richter, M.; Klein, A.; Thauer, R.K.

Eur. J. Biochem.

208

511-520

755911

9799292

Activation and thermostabilization effects of cyclic 2,3-diphosphoglycerate on enzymes from the hyperthermophilic Methanopyrus kandleri

1998

Shima, S.; Herault, D.; Berkessel, A.; Thauer, R.

Arch. Microbiol.

170

469-472

Links to other databases for 5,10-methenyl-5,6,7,8-tetrahydromethanopterin

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Show Links (1 entry)

ChEBI

PubChem