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Ligand 5,6,7,8-tetrahydromethanopterin

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

methanogenesis from CO2

KEGG

Biosynthesis of cofactors, Carbon metabolism, Folate biosynthesis, Methane metabolism, Microbial metabolism in diverse environments

MetaCyc

formaldehyde oxidation VI (H4MPT pathway), methanogenesis from H2 and CO2, methanogenesis from methoxylated aromatic compounds, methoxylated aromatic compound degradation II, phosphopantothenate biosynthesis III (archaea), reductive acetyl coenzyme A pathway II (autotrophic methanogens), tetrahydromethanopterin biosynthesis more

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

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (8 results)

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Show Natural Substrate (8 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.99.15

5,6,7,8-tetrahydromethanopterin + oxidized acceptor = 7,8-dihydromethanopterin + reduced acceptor

742870

-

2.1.1.86

5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M = 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + H+

733227

-

2.3.1.101

formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin

727375

-

2.3.1.101

formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + N5-formyl-5,6,7,8-tetrahydromethanopterin

486094, 486093, 486095, 486096, 486092, 486089, 486085, 486084

-

2.3.1.101

2 entries

4.2.1.147

5,6,7,8-tetrahydromethanopterin + formaldehyde = 5,10-methylenetetrahydromethanopterin + H2O

725231, 727849

-

4.4.1.22

5,6,7,8-tetrahydromethanopterin + formaldehyde = 5,10-methylenetetrahydromethanopterin + H2O

749071

-

6.3.2.33

ATP + tetrahydromethanopterin + L-glutamate = ADP + phosphate + 5,6,7,8-tetrahydrosarcinapterin

700925

-

6.3.2.33

GTP + tetrahydromethanopterin + L-glutamate = GDP + phosphate + 5,6,7,8-tetrahydrosarcinapterin

700925

-

6.3.2.33

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (9 results)

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Show Natural Product (9 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.1.47

7,8-dihydromethanopterin + NAD(P)H + H+ = 5,6,7,8-tetrahydromethanopterin + NAD(P)+

0

-

1.5.1.47

7,8-dihydromethanopterin + NADPH + H+ = 5,6,7,8-tetrahydromethanopterin + NADP+

0

-

1.5.99.15

7,8-dihydromethanopterin + FMNH2 = 5,6,7,8-tetrahydromethanopterin + FMN

0

-

1.5.99.15

7,8-dihydromethanopterin + reduced acceptor = 5,6,7,8-tetrahydromethanopterin + oxidized acceptor

0

-

1.5.99.15

7,8-dihydromethanopterin + reduced ferredoxin = 5,6,7,8-tetrahydromethanopterin + ferredoxin

0

-

2.1.1.86

5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate = 5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate

639489, 0

-

2.1.1.86

5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + H+ = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M

0

-

2.1.1.86

5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M

0

-

2.1.1.86

5-methyl-5,6,7,8-tetrahydromethanopterin + CoM + 2 Na+/in = 5,6,7,8-tetrahydromethanopterin + 2-(methylsulfanyl)ethane-1-sulfonate + 2 Na+/out

0

-

1.5.1.47

2 entries

1.5.99.15

3 entries

2.1.1.86

4 entries

Substrate in Enzyme-catalyzed Reactions (13 results)

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Show Substrate (13 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.99.15

5,6,7,8-tetrahydromethanopterin + oxidized acceptor = 7,8-dihydromethanopterin + reduced acceptor

742870

-

2.1.1.384

a [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein] + tetrahydromethanopterin = N5-methyltetrahydromethanopterin + a [Co(I) methoxylated-aromatic-compound-specific corrinoid protein]

764942

-

2.1.1.86

5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M = 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + H+

733227

-

2.1.1.86

5,6,7,8-tetrahydromethanopterin + methylcob(III)alamin = 5-methyl-5,6,7,8-tetrahydromethanopterin + cob(III)alamin

734072

-

2.1.1.86

2 entries

2.1.2.1

tetrahydromethanopterin + L-Ser = glycine + ?

659269

-

2.3.1.101

formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin

726828, 727375

-

2.3.1.101

formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + N5-formyl-5,6,7,8-tetrahydromethanopterin

486089, 486086, 486094, 486093, 486097, 486095, 486096, 486088, 486091, 486092, 486084, 486087, 11925, 486085

-

2.3.1.101

N-furfurylformamide + 5,6,7,8-tetrahydromethanopterin = 2-(aminomethyl)furane + N5-formyl-5,6,7,8-tetrahydromethanopterin

11925, 486087

-

2.3.1.101

3 entries

2.3.1.169

CH3-CO-S-CoA + H+ + tetrahydromethanopterin = CH3-tetrahydromethanopterin + CO + HS-CoA

644858

-

4.2.1.147

5,6,7,8-tetrahydromethanopterin + formaldehyde = 5,10-methylenetetrahydromethanopterin + H2O

725231, 727849

-

4.4.1.22

5,6,7,8-tetrahydromethanopterin + formaldehyde = 5,10-methylenetetrahydromethanopterin + H2O

749071

-

6.3.2.33

ATP + tetrahydromethanopterin + L-glutamate = ADP + phosphate + 5,6,7,8-tetrahydrosarcinapterin

700925

-

6.3.2.33

GTP + tetrahydromethanopterin + L-glutamate = GDP + phosphate + 5,6,7,8-tetrahydrosarcinapterin

700925

-

6.3.2.33

2 entries

Product in Enzyme-catalyzed Reactions (11 results)

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Show Product (11 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.1.47

7,8-dihydromethanopterin + NAD(P)H + H+ = 5,6,7,8-tetrahydromethanopterin + NAD(P)+

0

-

1.5.1.47

7,8-dihydromethanopterin + NADPH + H+ = 5,6,7,8-tetrahydromethanopterin + NADP+

0

-

1.5.99.15

7,8-dihydromethanopterin + FMNH2 = 5,6,7,8-tetrahydromethanopterin + FMN

0

-

1.5.99.15

7,8-dihydromethanopterin + reduced acceptor = 5,6,7,8-tetrahydromethanopterin + oxidized acceptor

0

-

1.5.99.15

7,8-dihydromethanopterin + reduced dithiothreitol = 5,6,7,8-tetrahydromethanopterin + oxidized dithiothreitol

0

-

1.5.99.15

7,8-dihydromethanopterin + reduced ferredoxin = 5,6,7,8-tetrahydromethanopterin + ferredoxin

0

-

2.1.1.86

5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate = 5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate

639489, 0

-

2.1.1.86

5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + H+ = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M

0

-

2.1.1.86

5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M

0

-

2.1.1.86

5-methyl-5,6,7,8-tetrahydromethanopterin + CoM + 2 Na+/in = 5,6,7,8-tetrahydromethanopterin + 2-(methylsulfanyl)ethane-1-sulfonate + 2 Na+/out

0

-

1.5.1.47

2 entries

1.5.99.15

4 entries

2.1.1.86

4 entries

2.3.1.101

methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin = formylmethanofuran + 5,6,7,8-tetrahydromethanopterin

0

-

Enzyme Cofactor/Cosubstrate (1 result)

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Show Cofactor (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

4.2.1.147

dependent on

727849

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (3 results)

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Show Turnover Number (3 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.1.2.1

3.53

-

pH 7.4, 37°C

659269

2.3.1.101

1970

-

-

486089

2.3.1.101

2770

-

-

486089

2.3.1.101

2 entries

K_M Value (10 results)

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Show KM Value (10 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.1.1.86

0.88

-

-

639489

2.1.2.1

0.1

-

pH 7.4, 37°C

659269

2.3.1.101

0.017

-

-

486086

2.3.1.101

0.03

-

-

486095

2.3.1.101

0.04

-

-

486089

2.3.1.101

0.08

-

pH 6.0, 10°C

727375

2.3.1.101

0.1

-

-

486087, 486097

2.3.1.101

0.1

-

wild-type enzyme

486091

2.3.1.101

0.107

-

recombinant enzyme

486091

2.3.1.101

7 entries

4.2.1.147

1

-

30°C, pH 8.0

725231

References & Links

Literature References (27)

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Show Reference (27 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

11925

2384164

N-Furfurylformamide as a pseudo-substrate for formylmethanofuran converting enzymes from methanogenic bacteria

1990

Breitung, J.; Börner, G.; Karrasch, M.; Berkessel, A.; Thauer, R.K.

FEBS Lett.

268

257-260

486084

-

The role of formylmethanofuran:tetrahydromethanopterin formyltransferase in methanogenesis from carbon dioxide

1986

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

J. Biol. Chem.

261

16652-16659

486085

-

Structure of methanofuran, the carbon dioxide reduction factor of Methanobacterium thermoautotrophicum

1984

Leigh, J.A.; Rinehart, K.L.; Wolfe, R.S.

J. Am. Chem. Soc.

106

3636-3640

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

486087

1483480

Salt dependence, kinetic properties and catalytic mechanism of N-formylmethanofuran:tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleri

1992

Breitung, J.; Börner, G.; Scholz, S.; Linder, D.; Stetter, K.O.; Thauer, R.K.

Eur. J. Biochem.

210

971-981

486088

2403564

The formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanobacterium thermoautotrophicum delta H. Nucleotide sequence and functional expression of the cloned gene

1990

DiMarco, A.A.; Sment, K.A.; Konisky, J.; Wolfe, R.S.

J. Biol. Chem.

265

472-476

486089

2261993

Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanosarcina barkeri. Identification of N5-formyltetrahydromethanopterin as the product

1990

Breitung, J.; Thauer, R.K.

FEBS Lett.

275

226-230

486091

7601152

Formylmethanofuran:tetrahydromethanopterin formyltransferase (Ftr) from the hyperthermophilic Methanopyrus kandleri. Cloning, sequencing and functional expression of the ftr gene and one-step purification of the enzyme overproduced in Escherichia coli

1995

Shima, S.; Weiss, D.S.; Thauer, R.K.

Eur. J. Biochem.

230

906-913

486092

8593103

Primary structure and properties of the formyltransferase from the mesophilic Methanosarcina barkeri. Comparison with the enzymes from thermophilic and hyperthermophilic methanogens

1996

Kunow, J.; Shima, S.; Vorholt, J.A.; Thauer, R.K.

Arch. Microbiol.

165

97-105

486093

8880936

Crystallization and preliminary x-ray diffraction studies of formylmethanofuran:tetrahydromethanopterin formyltransferase from Methanopyrus kandleri

1996

Shima, S.; Thauer, R.K.; Michel, H.; Ermler, U.

Proteins Struct. Funct. Genet.

26

118-120

486094

9195883

Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri - new insights into salt-dependence and thermostability

1997

Ermler, U.; Merckel, M.C.; Thauer, R.K.; Shima, S.

Structure

5

635-646

486095

11532013

Characterization of the formyltransferase from Methylobacterium extorquens AM1

2001

Pomper, B.K.; Vorholt, J.A.

Eur. J. Biochem.

268

4769-4775

486096

12123819

Generation of formate by the formyltransferase/hydrolase complex (Fhc) from Methylobacterium extorquens AM1

2002

Pomper, B.K.; Saurel, O.; Milon, A.; Vorholt, J.A.

FEBS Lett.

523

133-137

486097

11265475

Tetrahydromethanopterin-specific enzymes from Methanopyrus kandleri

2001

Shima, S.; Thauer, R.K.

Methods Enzymol.

331

317-353

639489

3085670

Tetrahydromethanopterin methyltransferase, a component of the methane synthesizing complex of Methanobacterium thermoautotrophicum

1986

Sauer, F.D.

Biochem. Biophys. Res. Commun.

136

542-547

644858

10671500

Evidence for intersubunit communication during acetyl-CoA cleavage by the multienzyme CO dehydrogenase/acetyl-CoA synthase complex from Methanosarcina thermophila. Evidence that the beta subunit catalyzes C-C and C-S bond cleavage

2000

Murakami, E.; Ragsdale, S.W.

J. Biol. Chem.

275

4699-4707

659269

12902326

Catalytic and thermodynamic properties of tetrahydromethanopterin-dependent serine hydroxymethyltransferase from Methanococcus jannaschii

2003

Angelaccio, S.; Chiaraluce, R.; Consalvi, V.; Buchenau, B.; Giangiacomo, L.; Bossa, F.; Contestabile, R.

J. Biol. Chem.

278

41789-41797

700925

12909715

Glutathione synthetase homologs encode alpha-L-glutamate ligases for methanogenic coenzyme F420 and tetrahydrosarcinapterin biosyntheses

2003

Li, H.; Xu, H.; Graham, D.E.; White, R.H.

Proc. Natl. Acad. Sci. USA

100

9785-9790

725231

11073907

Novel formaldehyde-activating enzyme in Methylobacterium extorquens AM1 required for growth on methanol

2000

Vorholt, J.A.; Marx, C.J.; Lidstrom, M.E.; Thauer, R.K.

J. Bacteriol.

182

6645-6650

726828

9799292

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

1998

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

Arch. Microbiol.

170

469-472

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

727849

15632161

How an enzyme binds the C1 carrier tetrahydromethanopterin. Structure of the tetrahydromethanopterin-dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1

2005

Acharya, P.; Goenrich, M.; Hagemeier, C.H.; Demmer, U.; Vorholt, J.A.; Thauer, R.K.; Ermler, U.

J. Biol. Chem.

280

13712-13719

733227

24729742

Towards a computational model of a methane producing archaeum

2014

Peterson, J.R.; Labhsetwar, P.; Ellermeier, J.R.; Kohler, P.R.; Jain, A.; Ha, T.; Metcalf, W.W.; Luthey-Schulten, Z.

Archaea

2014

898453

734072

22636775

Role of the fused corrinoid/methyl transfer protein CmtA during CO-dependent growth of Methanosarcina acetivorans

2012

Vepachedu, V.R.; Ferry, J.G.

J. Bacteriol.

194

4161-4168

742870

24523405

Structure of dihydromethanopterin reductase, a cubic protein cage for redox transfer

2014

McNamara, D.E.; Cascio, D.; Jorda, J.; Bustos, C.; Wang, T.C.; Rasche, M.E.; Yeates, T.O.; Bobik, T.A.

J. Biol. Chem.

289

8852-8864

749071

26675168

Studies on the glutathione-dependent formaldehyde-activating enzyme from Paracoccus denitrificans

2015

Hopkinson, R.J.; Leung, I.K.; Smart, T.J.; Rose, N.R.; Henry, L.; Claridge, T.D.; Schofield, C.J.

PLoS ONE

10

e0145085

764942

34145392

Methanogenic archaea use a bacteria-like methyltransferase system to demethoxylate aromatic compounds

2021

Kurth, J.; Nobu, M.; Tamaki, H.; de Jonge, N.; Berger, S.; Jetten, M.; Yamamoto, K.; Mayumi, D.; Sakata, S.; Bai, L.; Cheng, L.; Nielsen, J.; Kamagata, Y.; Wagner, T.; Welte, C.

ISME J.

15

3549-3565

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

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ChEBI

PubChem