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1.2.7.12

Accepted name:

formylmethanofuran dehydrogenase

Reaction:

a formylmethanofuran + H₂O + 2 oxidized ferredoxin [iron-sulfur] cluster = CO₂ + a methanofuran + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H⁺

For diagram of methane biosynthesis, click here

Glossary:

methanofuran a = 4-[4-(2-{[(4R*,5S*)-4,5,7-tricarboxyheptanoyl]-γ-L-glutamyl-γ-L-glutamylamino}ethyl)phenoxymethyl]furan-2-ylmethanamine

Other name(s):

formylmethanofuran:acceptor oxidoreductase

Systematic name:

formylmethanofuran:ferredoxin oxidoreductase

Comments:

Contains a molybdopterin cofactor and numerous [4Fe-4S] clusters. In some organisms an additional subunit enables the incorporation of tungsten when molybdenum availability is low. The enzyme catalyses a reversible reaction in methanogenic archaea, and is involved in methanogenesis from CO₂ as well as the oxidation of coenzyme M to CO₂. The reaction is endergonic, and is driven by coupling with the soluble CoB-CoM heterodisulfide reductase via electron bifurcation.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 119940-12-4

References:

1.	Karrasch, M., Börner, G., Enssle, M. and Thauer, R.K. The molybdoenzyme formylmethanofuran dehydrogenase from Methanosarcina barkeri contains a pterin cofactor. Eur. J. Biochem. 194 (1990) 367–372. [DOI] [PMID: 2125267]
2.	Bertram, P.A., Schmitz, R.A., Linder, D. and Thauer, R.K. Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum. Identification and characterization of a tungsten isoenzyme of formylmethanofuran dehydrogenase. Arch. Microbiol. 161 (1994) 220–228. [PMID: 8161283]
3.	Bertram, P.A., Karrasch, M., Schmitz, R.A., Bocher, R., Albracht, S.P. and Thauer, R.K. Formylmethanofuran dehydrogenases from methanogenic Archaea. Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron-sulfur proteins. Eur. J. Biochem. 220 (1994) 477–484. [DOI] [PMID: 8125106]
4.	Vorholt, J.A. and Thauer, R.K. The active species of ’CO₂’ utilized by formylmethanofuran dehydrogenase from methanogenic Archaea. Eur. J. Biochem. 248 (1997) 919–924. [DOI] [PMID: 9342247]
5.	Meuer, J., Kuettner, H.C., Zhang, J.K., Hedderich, R. and Metcalf, W.W. Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation. Proc. Natl. Acad. Sci. USA 99 (2002) 5632–5637. [DOI] [PMID: 11929975]
6.	Kaster, A.K., Moll, J., Parey, K. and Thauer, R.K. Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea. Proc. Natl. Acad. Sci. USA 108 (2011) 2981–2986. [DOI] [PMID: 21262829]
7.	Wagner, T., Ermler, U. and Shima, S. The methanogenic CO₂ reducing-and-fixing enzyme is bifunctional and contains 46 [4Fe-4S] clusters. Science 354 (2016) 114–117. [PMID: 27846502]

[EC 1.2.7.12 created 1992 as EC 1.2.99.5, transferred 2017 to EC 1.2.7.12]

1.2.99.5

Transferred entry:

formylmethanofuran dehydrogenase. Now EC 1.2.7.12, formylmethanofuran dehydrogenase

[EC 1.2.99.5 created 1992, deleted 2017]

2.3.1.101

Accepted name:

formylmethanofuran—tetrahydromethanopterin N-formyltransferase

Reaction:

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

For diagram of methane biosynthesis, click here

Glossary:

methanofuran = 4-[4-(2-{[(4R*,5S^*)-4,5,7-tricarboxyheptanoyl]-γ-L-glutamyl-γ-L-glutamylamino}ethyl)phenoxymethyl]furfurylamine
tetrahydromethanopterin = 1-(4-{(1R)-1-[(6S,7S)-2-amino-7-methyl-4-oxo-3,4,5,6,7,8-hexahydropteridin-6-yl]ethylamino}phenyl)-1-deoxy-5-O-{5-O-[(1S)-1,3-dicarboxypropylphosphonato]-α-D-ribofuranosyl}-D-ribitol

Other name(s):

formylmethanofuran-tetrahydromethanopterin formyltransferase; formylmethanofuran:tetrahydromethanopterin formyltransferase; N-formylmethanofuran(CHO-MFR):tetrahydromethanopterin(H₄MPT) formyltransferase; FTR; formylmethanofuran:5,6,7,8-tetrahydromethanopterin N⁵-formyltransferase

Systematic name:

formylmethanofuran:5,6,7,8-tetrahydromethanopterin 5-formyltransferase

Comments:

Methanofuran is a complex 4-substituted furfurylamine and is involved in the formation of methane from CO₂ in Methanobacterium thermoautotrophicum.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 105669-83-8

References:

1.	Donnelly, M.I. and Wolfe, R.S. The role of formylmethanofuran: tetrahydromethanopterin formyltransferase in methanogenesis from carbon dioxide. J. Biol. Chem. 261 (1986) 16653–16659. [PMID: 3097011]
2.	Leigh, J.A., Rinehart, K.L. and Wolfe, R.S. Structure of methanofuran, the carbon-dioxide reduction factor of Methanobacterium thermoautotrophicum. J. Am. Chem. Soc. 106 (1984) 3636–3640.

[EC 2.3.1.101 created 1989]

2.5.1.131

Accepted name:

(4-{4-[2-(γ-L-glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine synthase

Reaction:

[5-(aminomethyl)furan-3-yl]methyl diphosphate + γ-L-glutamyltyramine = (4-{4-[2-(γ-L-glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine + diphosphate

For diagram of methanofuran biosynthesis, click here

Other name(s):

MfnF

Systematic name:

[5-(aminomethyl)furan-3-yl]methyl-diphosphate:γ-L-glutamyltyramine [5-(aminomethyl)furan-3-yl]methyltransferase

Comments:

The enzyme, isolated from the archaeon Methanocaldococcus jannaschii, participates in the biosynthesis of the methanofuran cofactor.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Wang, Y., Xu, H., Jones, M.K. and White, R.H. Identification of the final two genes functioning in methanofuran biosynthesis in Methanocaldococcus jannaschii. J. Bacteriol. 197 (2015) 2850–2858. [DOI] [PMID: 26100040]

[EC 2.5.1.131 created 2015]

2.6.1.108

Accepted name:

(5-formylfuran-3-yl)methyl phosphate transaminase

Reaction:

L-alanine + (5-formylfuran-3-yl)methyl phosphate = pyruvate + [5-(aminomethyl)furan-3-yl]methyl phosphate

For diagram of methanofuran biosynthesis, click here

Other name(s):

mfnC (gene name); [5-(hydroxymethyl)furan-3-yl]methyl phosphate transaminase

Systematic name:

L-alanine:(5-formylfuran-3-yl)methyl phosphate aminotransferase

Comments:

A pyridoxal 5′-phosphate protein. The enzyme, characterized from the archaebacterium Methanocaldococcus jannaschii, participates in the biosynthesis of the cofactor methanofuran. Requires pyridoxal 5′-phosphate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Miller, D., Wang, Y., Xu, H., Harich, K. and White, R.H. Biosynthesis of the 5-(aminomethyl)-3-furanmethanol moiety of methanofuran. Biochemistry 53 (2014) 4635–4647. [DOI] [PMID: 24977328]

[EC 2.6.1.108 created 2015]

2.7.4.31

Accepted name:

[5-(aminomethyl)furan-3-yl]methyl phosphate kinase

Reaction:

ATP + [5-(aminomethyl)furan-3-yl]methyl phosphate = ADP + [5-(aminomethyl)furan-3-yl]methyl diphosphate

For diagram of methanofuran biosynthesis, click here

Other name(s):

MfnE

Systematic name:

ATP:[5-(aminomethyl)furan-3-yl]methyl-phosphate phosphotransferase

Comments:

Requires Mg²⁺. The enzyme, isolated from the archaeon Methanocaldococcus jannaschii, participates in the biosynthesis of the methanofuran cofactor.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Wang, Y., Xu, H., Jones, M.K. and White, R.H. Identification of the final two genes functioning in methanofuran biosynthesis in Methanocaldococcus jannaschii. J. Bacteriol. 197 (2015) 2850–2858. [DOI] [PMID: 26100040]

[EC 2.7.4.31 created 2015]

4.1.1.25

Accepted name:

tyrosine decarboxylase

Reaction:

L-tyrosine = tyramine + CO₂

For diagram of methanofuran biosynthesis, click here

Other name(s):

L-tyrosine decarboxylase; L-(-)-tyrosine apodecarboxylase; L-tyrosine carboxy-lyase

Systematic name:

L-tyrosine carboxy-lyase (tyramine-forming)

Comments:

A pyridoxal-phosphate protein. The bacterial enzyme also acts on 3-hydroxytyrosine and, more slowly, on 3-hydroxyphenylalanine.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9002-09-9

References:

1.	McGilvery, R.W. and Cohen, P.P. The decarboxylation of L-phenylalanine by Streptococcus faecalis R. J. Biol. Chem. 174 (1948) 813–816. [PMID: 18871240]

[EC 4.1.1.25 created 1961]

4.1.99.21

Transferred entry:

(5-formylfuran-3-yl)methyl phosphate synthase. Now EC 4.2.3.153 (5-formylfuran-3-yl)methyl phosphate synthase.

[EC 4.1.99.21 created 2015, deleted 2015]

4.2.3.153

Accepted name:

(5-formylfuran-3-yl)methyl phosphate synthase

Reaction:

2 D-glyceraldehyde 3-phosphate = (5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H₂O

For diagram of methanofuran biosynthesis, click here

Glossary:

(5-formylfuran-3-yl)methyl phosphate = 4-(hydroxymethyl)furan-2-carboxaldehyde phosphate

Other name(s):

mfnB (gene name); 4-HFC-P synthase; 4-(hydroxymethyl)-2-furaldehyde phosphate synthase

Systematic name:

D-glyceraldehyde-3-phosphate phosphate-lyase [D-glyceraldehyde-3-phosphate-adding; (5-formylfuran-3-yl)methyl-phosphate-forming]

Comments:

The enzyme catalyses the reaction in the direction of producing (5-formylfuran-3-yl)methyl phosphate, an intermediate in the biosynthesis of methanofuran. The sequence of events starts with the removal of a phosphate group, followed by aldol condensation and cyclization. Methanofuran is a carbon-carrier cofactor involved in the first step of the methanogenic reduction of carbon dioxide by methanogenic archaea.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Miller, D., Wang, Y., Xu, H., Harich, K. and White, R.H. Biosynthesis of the 5-(aminomethyl)-3-furanmethanol moiety of methanofuran. Biochemistry 53 (2014) 4635–4647. [DOI] [PMID: 24977328]
2.	Bobik, T.A., Morales, E.J., Shin, A., Cascio, D., Sawaya, M.R., Arbing, M., Yeates, T.O. and Rasche, M.E. Structure of the methanofuran/methanopterin-biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii. Acta Crystallogr. F Struct. Biol. Commun. 70 (2014) 1472–1479. [DOI] [PMID: 25372812]
3.	Wang, Y., Jones, M.K., Xu, H., Ray, W.K. and White, R.H. Mechanism of the enzymatic synthesis of 4-(hydroxymethyl)-2-furancarboxaldehyde-phosphate (4-HFC-P) from glyceraldehyde-3-phosphate catalyzed by 4-HFC-P synthase. Biochemistry 54 (2015) 2997–3008. [DOI] [PMID: 25905665]

[EC 4.2.3.153 created 2015 as EC 4.1.99.21, transferred 2015 to EC 4.2.3.153]

6.3.4.24

Accepted name:

tyramine—L-glutamate ligase

Reaction:

ATP + tyramine + L-glutamate = ADP + phosphate + γ-glutamyltyramine

For diagram of methanofuran biosynthesis, click here

Other name(s):

mfnD (gene name)

Systematic name:

tyramine:L-glutamate γ-ligase (ADP-forming)

Comments:

The enzyme, which has been characterized from the archaea Methanocaldococcus fervens, participates in the biosynthesis of the cofactor methanofuran. Requires a divalent cation for activity, with Mn²⁺ giving the highest activity, followed by Mg²⁺, Co²⁺, Zn²⁺, and Fe²⁺.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Wang, Y., Xu, H., Harich, K.C. and White, R.H. Identification and characterization of a tyramine-glutamate ligase (MfnD) Involved in methanofuran biosynthesis. Biochemistry 53 (2014) 6220–6230. [DOI] [PMID: 25211225]

[EC 6.3.4.24 created 2014]