EC |
1.5.1.47 |
Accepted name: |
dihydromethanopterin reductase [NAD(P)+] |
Reaction: |
5,6,7,8-tetrahydromethanopterin + NAD(P)+ = 7,8-dihydromethanopterin + NAD(P)H + H+ |
|
For diagram of methanopterin biosynthesis (part 4), click here |
Other name(s): |
DmrA; H2MPT reductase; 5,6,7,8-tetrahydromethanopterin 5,6-oxidoreductase; dihydromethanopterin reductase |
Systematic name: |
5,6,7,8-tetrahydromethanopterin:NAD(P)+ 5,6-oxidoreductase |
Comments: |
The enzyme, characterized from the bacterium Methylobacterium extorquens, is involved in biosynthesis of dephospho-tetrahydromethanopterin. The specific activity with NADH is 15% of that with NADPH at the same concentration [1]. It does not reduce 7,8-dihydrofolate (cf. EC 1.5.1.3, dihydrofolate reductase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Caccamo, M.A., Malone, C.S. and Rasche, M.E. Biochemical characterization of a dihydromethanopterin reductase involved in tetrahydromethanopterin biosynthesis in Methylobacterium extorquens AM1. J. Bacteriol. 186 (2004) 2068–2073. [DOI] [PMID: 15028691] |
|
[EC 1.5.1.47 created 2013, modified 2014] |
|
|
|
|
EC |
1.5.98.1 |
Accepted name: |
methylenetetrahydromethanopterin dehydrogenase |
Reaction: |
5,10-methylenetetrahydromethanopterin + oxidized coenzyme F420 = 5,10-methenyltetrahydromethanopterin + reduced coenzyme F420 |
|
For diagram of methane biosynthesis, click here |
Other name(s): |
N5,N10-methylenetetrahydromethanopterin dehydrogenase; 5,10-methylenetetrahydromethanopterin dehydrogenase |
Systematic name: |
5,10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase |
Comments: |
Coenzyme F420 is a 7,8-didemethyl-8-hydroxy-5-deazariboflavin derivative; methanopterin is a pterin analogue. The enzyme is involved in the formation of methane from CO2 in the methanogen Methanothermobacter thermautotrophicus. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 100357-01-5 |
References: |
1. |
Hartzell, P.L., Zvilius, G., Escalante-Semerena, J.C. and Donnelly, M.I. Coenzyme F420 dependence of the methylenetetrahydromethanopterin dehydrogenase of Methanobacterium thermoautotrophicum. Biochem. Biophys. Res. Commun. 133 (1985) 884–890. [DOI] [PMID: 4084309] |
2. |
te Brömmelstroet, B.W., Geerts, W.J., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri. Biochim. Biophys. Acta 1079 (1991) 293–302. [DOI] [PMID: 1911853] |
|
[EC 1.5.98.1 created 1989 as EC 1.5.99.9, modified 2004, transferred to EC 1.5.98.1 2014] |
|
|
|
|
EC |
1.5.98.2 |
Accepted name: |
5,10-methylenetetrahydromethanopterin reductase |
Reaction: |
5-methyltetrahydromethanopterin + oxidized coenzyme F420 = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420 |
|
For diagram of methane biosynthesis, click here |
Other name(s): |
5,10-methylenetetrahydromethanopterin cyclohydrolase; N5,N10-methylenetetrahydromethanopterin reductase; methylene-H4MPT reductase; coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase; N5,N10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase |
Systematic name: |
5-methyltetrahydromethanopterin:coenzyme-F420 oxidoreductase |
Comments: |
Catalyses an intermediate step in methanogenesis from CO2 and H2 in methanogenic archaea. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Ma, K. and Thauer, R.K. Purification and properties of N5,N10-methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum (strain Marburg). Eur. J. Biochem. 191 (1990) 187–193. [DOI] [PMID: 2379499] |
2. |
te Brömmelstroet, B.W., Geerts, W.J., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri. Biochim. Biophys. Acta 1079 (1991) 293–302. [DOI] [PMID: 1911853] |
3. |
Ma, K. and Thauer, R.K. Single step purification of methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum by specific binding to blue sepharose CL-6B. FEBS Lett. 268 (1990) 59–62. [DOI] [PMID: 1696553] |
4. |
te Brömmelstroet, B.W., Hensgens, C.M., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methylenetetrahydromethanopterin reductase, a coenzyme F420-dependent enzyme, from Methanobacterium thermoautotrophicum strain ΔH*. J. Biol. Chem. 265 (1990) 1852–1857. [PMID: 2298726] |
5. |
te Brömmelstroet, B.W., Hensgens, C.M., Geerts, W.J., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanosarcina barkeri. J. Bacteriol. 172 (1990) 564–571. [DOI] [PMID: 2298699] |
|
[EC 1.5.98.2 created 2000 as EC 1.5.99.11, modified 2004, transferred to EC 1.5.98.2 2014] |
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|
|
|
EC
|
1.5.99.9
|
Transferred entry: | methylenetetrahydromethanopterin dehydrogenase. As the acceptor is known the enzyme has been transferred to EC 1.5.98.1, methylenetetrahydromethanopterin dehydrogenase
|
[EC 1.5.99.9 created 1989, modified 2004, deleted 2014] |
|
|
|
|
EC
|
1.5.99.11
|
Transferred entry: | methylenetetrahydromethanopterin dehydrogenase. As the acceptor is known the enzyme has been transferred to EC 1.5.98.2, 5,10-methylenetetrahydromethanopterin reductase
|
[EC 1.5.99.11 created 2000, modified 2004, deleted 2014] |
|
|
|
|
EC |
1.5.99.15 |
Accepted name: |
dihydromethanopterin reductase (acceptor) |
Reaction: |
5,6,7,8-tetrahydromethanopterin + oxidized acceptor = 7,8-dihydromethanopterin + reduced acceptor |
|
For diagram of methanopterin biosynthesis (part 4), click here |
Other name(s): |
DmrX |
Systematic name: |
5,6,7,8-tetrahydromethanopterin:acceptor 5,6-oxidoreductase |
Comments: |
This archaeal enzyme catalyses the last step in the biosynthesis of tetrahydromethanopterin, a folate analogue used in methanogenesis. The enzyme, characterized from the archaea Methanosarcina mazei and Methanocaldococcus jannaschii, is an iron-sulfur flavoprotein. cf. EC 1.5.1.47, dihydromethanopterin reductase [NAD(P)+]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Wang, S., Tiongson, J. and Rasche, M.E. Discovery and characterization of the first archaeal dihydromethanopterin reductase, an iron-sulfur flavoprotein from Methanosarcina mazei. J. Bacteriol. 196 (2014) 203–209. [DOI] [PMID: 23995635] |
|
[EC 1.5.99.15 created 2014] |
|
|
|
|
EC |
1.12.98.2 |
Accepted name: |
5,10-methenyltetrahydromethanopterin hydrogenase |
Reaction: |
H2 + 5,10-methenyltetrahydromethanopterin = H+ + 5,10-methylenetetrahydromethanopterin |
Other name(s): |
H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase; nonmetal hydrogenase; N5,N10-methenyltetrahydromethanopterin hydrogenase; hydrogen:N5,N10-methenyltetrahydromethanopterin oxidoreductase |
Systematic name: |
hydrogen:5,10-methenyltetrahydromethanopterin oxidoreductase |
Comments: |
Does not catalyse the reduction of artificial dyes. Does not by itself catalyse a H2/H+ exchange reaction. Does not contain nickel or iron-sulfur clusters. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 100357-01-5 |
References: |
1. |
Zirngibl, C., Hedderich, R. and Thauer, R.K. N5,N10-Methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum has hydrogenase activity. FEBS Lett. 261 (1990) 112–116. |
2. |
Klein, A., Fernandez, V.M. and Thauer, R.K. H2-Forming N5,N10-methylenetetrahydromethanopterin dehydrogenase: mechanism of H2-formation analyzed using hydrogen isotopes. FEBS Lett. 368 (1995) 203–206. [DOI] [PMID: 7628605] |
|
[EC 1.12.98.2 created 1999 as EC 1.12.99.4, transferred 2002 to EC 1.12.98.2, modified 2004] |
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|
|
|
EC
|
1.12.99.4
|
Transferred entry: | N5,N10-methenyltetrahydromethanopterin hydrogenase. Now EC 1.12.98.2, 5,10-methenyltetrahydromethanopterin hydrogenase
|
[EC 1.12.99.4 created 1999, deleted 2002] |
|
|
|
|
EC
|
2.1.1.86
|
Transferred entry: | tetrahydromethanopterin S-methyltransferase. Now EC 7.2.1.4, tetrahydromethanopterin S-methyltransferase
|
[EC 2.1.1.86 created 1989, modified 2000, modified 2017, deleted 2024] |
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|
|
|
EC |
2.1.1.384 |
Accepted name: |
[methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein]—tetrahydromethanopterin methyltransferase |
Reaction: |
a [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein] + tetrahydromethanopterin = N5-methyltetrahydromethanopterin + a [Co(I) methoxylated-aromatic-compound-specific corrinoid protein] |
Other name(s): |
mtoA (gene name) |
Systematic name: |
[methylated methoxylated-aromatic-compound-specific corrinoid protein]:tetrahydromethanopterin methyltransferase |
Comments: |
The enzyme has been characterized from several archaeal species. In the methanogenic archaeon Methermicoccus shengliensis the enzyme participates in methanogenesis from methoxylated aromatic compounds, while in the non-methanogenic Archaeoglobus fulgidus it participates in methoxydotrophic growth. The enzyme catalyses the transfer of a methyl group bound to the cobalt cofactor of a dedicated corrinoid protein (MtoC) to tetrahydromethanopterin or tetrahydrosarcinapterin. cf. EC 2.1.1.385, [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein]—tetrahydrofolate methyltransferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kurth, J.M., Nobu, M.K., Tamaki, H., de Jonge, N., Berger, S., Jetten, M.SM., Yamamoto, K., Mayumi, D., Sakata, S., Bai, L., Cheng, L., Nielsen, J.L., Kamagata, Y., Wagner, T. and Welte, C.U. Methanogenic archaea use a bacteria-like methyltransferase system to demethoxylate aromatic compounds. ISME J. 15 (2021) 3549–3565. [DOI] [PMID: 34145392] |
2. |
Welte, C.U., de Graaf, R., Dalcin Martins, P., Jansen, R.S., Jetten, M.SM. and Kurth, J.M. A novel methoxydotrophic metabolism discovered in the hyperthermophilic archaeon Archaeoglobus fulgidus. Environ. Microbiol. 23 (2021) 4017–4033. [DOI] [PMID: 33913565] |
|
[EC 2.1.1.384 created 2022] |
|
|
|
|
EC |
2.1.1.385 |
Accepted name: |
[methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein]—tetrahydrofolate methyltransferase |
Reaction: |
a [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein] + tetrahydrofolate = N5-methyltetrahydrofolate + a [Co(I) methoxylated-aromatic-compound-specific corrinoid protein] |
Other name(s): |
mtvA (gene name) |
Systematic name: |
[methylated methoxylated-aromatic-compound-specific corrinoid protein]:tetrahydrofolaten methyltransferase |
Comments: |
The enzyme, found in acetogenic bacteria, participates in a pathway for the degradation of methoxylated aromatic compounds (methoxydotrophic growth). The enzyme catalyses the transfer of a methyl group bound to the cobalt cofactor of a dedicated corrinoid protein (MtvC) to tetrahydrofolate. cf. EC 2.1.1.384, [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein]—tetrahydromethanopterin methyltransferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kaufmann, F., Wohlfarth, G. and Diekert, G. O-demethylase from Acetobacterium dehalogenans—substrate specificity and function of the participating proteins. Eur. J. Biochem. 253 (1998) 706–711. [DOI] [PMID: 9654069] |
2. |
Naidu, D. and Ragsdale, S.W. Characterization of a three-component vanillate O-demethylase from Moorella thermoacetica. J. Bacteriol. 183 (2001) 3276–3281. [DOI] [PMID: 11344134] |
3. |
Pierce, E., Xie, G., Barabote, R.D., Saunders, E., Han, C.S., Detter, J.C., Richardson, P., Brettin, T.S., Das, A., Ljungdahl, L.G. and Ragsdale, S.W. The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum). Environ. Microbiol. 10 (2008) 2550–2573. [DOI] [PMID: 18631365] |
|
[EC 2.1.1.385 created 2022] |
|
|
|
|
EC |
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] |
|
|
|
|
EC |
2.4.2.54 |
Accepted name: |
β-ribofuranosylphenol 5′-phosphate synthase |
Reaction: |
5-phospho-α-D-ribose 1-diphosphate + 4-hydroxybenzoate = 4-(β-D-ribofuranosyl)phenol 5′-phosphate + CO2 + diphosphate |
|
For diagram of methanopterin biosynthesis (part 2), click here |
Other name(s): |
β-RFAP synthase (incorrect); β-RFA-P synthase (incorrect); AF2089 (gene name); MJ1427 (gene name); β-ribofuranosylhydroxybenzene 5′-phosphate synthase; 4-(β-D-ribofuranosyl)aminobenzene 5′-phosphate synthase (incorrect); β-ribofuranosylaminobenzene 5′-phosphate synthase (incorrect); 5-phospho-α-D-ribose 1-diphosphate:4-aminobenzoate 5-phospho-β-D-ribofuranosyltransferase (decarboxylating) (incorrect) |
Systematic name: |
5-phospho-α-D-ribose-1-diphosphate:4-hydroxybenzoate 5-phospho-β-D-ribofuranosyltransferase (decarboxylating) |
Comments: |
The enzyme is involved in biosynthesis of tetrahydromethanopterin in archaea. It can utilize both 4-hydroxybenzoate and 4-aminobenzoate as substrates, but only the former is known to be produced by methanogenic archaea [4]. The activity is dependent on Mg2+ or Mn2+ [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Rasche, M.E. and White, R.H. Mechanism for the enzymatic formation of 4-(β-D-ribofuranosyl)aminobenzene 5′-phosphate during the biosynthesis of methanopterin. Biochemistry 37 (1998) 11343–11351. [DOI] [PMID: 9698382] |
2. |
Scott, J.W. and Rasche, M.E. Purification, overproduction, and partial characterization of β-RFAP synthase, a key enzyme in the methanopterin biosynthesis pathway. J. Bacteriol. 184 (2002) 4442–4448. [DOI] [PMID: 12142414] |
3. |
Dumitru, R.V. and Ragsdale, S.W. Mechanism of 4-(β-D-ribofuranosyl)aminobenzene 5′-phosphate synthase, a key enzyme in the methanopterin biosynthetic pathway. J. Biol. Chem. 279 (2004) 39389–39395. [DOI] [PMID: 15262968] |
4. |
White, R.H. The conversion of a phenol to an aniline occurs in the biochemical formation of the 1-(4-aminophenyl)-1-deoxy-D-ribitol moiety in methanopterin. Biochemistry 50 (2011) 6041–6052. [DOI] [PMID: 21634403] |
5. |
Bechard, M.E., Farahani, P., Greene, D., Pham, A., Orry, A. and Rasche, M.E. Purification, kinetic characterization, and site-directed mutagenesis of Methanothermobacter thermautotrophicus RFAP synthase produced in Escherichia coli. AIMS Microbiol 5 (2019) 186–204. [DOI] [PMID: 31663056] |
|
[EC 2.4.2.54 created 2013, modified 2014, modified 2015] |
|
|
|
|
EC |
2.5.1.105 |
Accepted name: |
7,8-dihydropterin-6-yl-methyl-4-(β-D-ribofuranosyl)aminobenzene 5′-phosphate synthase |
Reaction: |
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-(β-D-ribofuranosyl)aniline 5′-phosphate = N-[(7,8-dihydropterin-6-yl)methyl]-4-(β-D-ribofuranosyl)aniline 5′-phosphate + diphosphate |
|
For diagram of methanopterin biosynthesis (part 2), click here |
Other name(s): |
MJ0301 (gene name); dihydropteroate synthase (ambiguous) |
Systematic name: |
(7,8-dihydropterin-6-yl)methyl-diphosphate:4-(β-D-ribofuranosyl)aniline 5′-phosphate 6-hydroxymethyl-7,8-dihydropterintransferase |
Comments: |
The enzyme, which has been studied in the archaeon Methanocaldococcus jannaschii, is involved in the biosynthesis of tetrahydromethanopterin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Xu, H., Aurora, R., Rose, G.D. and White, R.H. Identifying two ancient enzymes in Archaea using predicted secondary structure alignment. Nat. Struct. Biol. 6 (1999) 750–754. [DOI] [PMID: 10426953] |
|
[EC 2.5.1.105 created 2013] |
|
|
|
|
EC |
3.1.4.56 |
Accepted name: |
7,8-dihydroneopterin 2′,3′-cyclic phosphate phosphodiesterase |
Reaction: |
(1) 7,8-dihydroneopterin 2′,3′-cyclic phosphate + H2O = 7,8-dihydroneopterin 3′-phosphate (2) 7,8-dihydroneopterin 2′,3′-cyclic phosphate + H2O = 7,8-dihydroneopterin 2′-phosphate |
|
For diagram of methanopterin biosynthesis (part 1), click here |
Glossary: |
7,8-dihydroneopterin 2′,3′-cyclic phosphate = 2-amino-6-{(S)-hydroxy[(4R)-2-hydroxy-2-oxido-1,3,2-dioxaphospholan-4-yl]methyl}-7,8-dihydropteridin-4(1H)-one = 2-amino-6-[(1S,2R)-1,2,3-trihydroxypropyl]-7,8-dihydro-4(1H)-pteridinone 1,2-cyclic phosphate
7,8-dihydroeopterin 3′-phosphate = (2R,3S)-3-(2-amino-4-oxo-1,4,7,8-tetrahydropteridin-6-yl)-2,3-dihydroxypropyl phosphate
7,8-dihydroneopterin 2′-phosphate = (1S,2R)-1-(2-amino-4-oxo-1,4,7,8-tetrahydropteridin-6-yl)-1,3-dihydroxypropan-2-yl phosphate |
Other name(s): |
MptB |
Systematic name: |
7,8-dihydroneopterin 2′,3′-cyclic phosphate 2′/3′-phosphodiesterase |
Comments: |
Contains one zinc atom and one iron atom per subunit of the dodecameric enzyme. It hydrolyses 7,8-dihydroneopterin 2′,3′-cyclic phosphate, a step in tetrahydromethanopterin biosynthesis. In vitro the enzyme forms 7,8-dihydroneopterin 2′-phosphate and 7,8-dihydroneopterin 3′-phosphate at a ratio of 4:1. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Mashhadi, Z., Xu, H. and White, R.H. An Fe2+-dependent cyclic phosphodiesterase catalyzes the hydrolysis of 7,8-dihydro-D-neopterin 2′,3′-cyclic phosphate in methanopterin biosynthesis. Biochemistry 48 (2009) 9384–9392. [DOI] [PMID: 19746965] |
|
[EC 3.1.4.56 created 2013] |
|
|
|
|
EC |
3.5.4.27 |
Accepted name: |
methenyltetrahydromethanopterin cyclohydrolase |
Reaction: |
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = 5-formyl-5,6,7,8-tetrahydromethanopterin |
|
For diagram of methane biosynthesis, click here |
Glossary: |
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): |
5,10-methenyltetrahydromethanopterin cyclohydrolase; N5,N10-methenyltetrahydromethanopterin cyclohydrolase; methenyl-H4MPT cyclohydrolase; 5,10-methenyltetrahydromethanopterin 10-hydrolase (decyclizing) |
Systematic name: |
5,10-methenyltetrahydromethanopterin 10-hydrolase (ring-opening) |
Comments: |
Methanopterin is a pterin analogue. The enzyme 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: 99533-50-3 |
References: |
1. |
Donnelly, M.I., Escalante-Semerena, J.C., Rinehart, K.L., Jr. and Wolfe, R.S. Methenyl-tetrahydromethanopterin cyclohydrolase in cell extracts of Methanobacterium. Arch. Biochem. Biophys. 242 (1985) 430–439. [DOI] [PMID: 4062290] |
|
[EC 3.5.4.27 created 1989] |
|
|
|
|
EC |
4.1.2.59 |
Accepted name: |
dihydroneopterin phosphate aldolase |
Reaction: |
7,8-dihydroneopterin 3′-phosphate = 6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde phosphate |
Other name(s): |
H2NMP aldolase |
Systematic name: |
7,8-dihydroneopterin 3′-phosphate glycolaldehyde phosphate-lyase [6-(hydroxymethyl)-7,8-dihydropterin-forming] |
Comments: |
The enzyme participates in methanopterin biosynthesis the archaeon Pyrococcus furiosus. The enzyme is specific for 7,8-dihydroneopterin 3′-phosphate. cf. EC 4.1.2.25, dihydroneopterin aldolase and EC 4.1.2.60, dihydroneopterin triphosphate aldolase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
de Crecy-Lagard, V., Phillips, G., Grochowski, L.L., El Yacoubi, B., Jenney, F., Adams, M.W., Murzin, A.G. and White, R.H. Comparative genomics guided discovery of two missing archaeal enzyme families involved in the biosynthesis of the pterin moiety of tetrahydromethanopterin and tetrahydrofolate. ACS Chem. Biol. 7 (2012) 1807–1816. [DOI] [PMID: 22931285] |
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[EC 4.1.2.59 created 2017] |
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EC |
4.2.1.147 |
Accepted name: |
5,6,7,8-tetrahydromethanopterin hydro-lyase |
Reaction: |
5,6,7,8-tetrahydromethanopterin + formaldehyde = 5,10-methylenetetrahydromethanopterin + H2O |
Other name(s): |
formaldehyde-activating enzyme |
Systematic name: |
5,6,7,8-tetrahydromethanopterin hydro-lyase (formaldehyde-adding, tetrahydromethanopterin-forming) |
Comments: |
Found in methylotrophic bacteria and methanogenic archaea. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Vorholt, J.A., Marx, C.J., Lidstrom, M.E. and Thauer, R.K. Novel formaldehyde-activating enzyme in Methylobacterium extorquens AM1 required for growth on methanol. J. Bacteriol. 182 (2000) 6645–6650. [DOI] [PMID: 11073907] |
2. |
Acharya, P., Goenrich, M., Hagemeier, C.H., Demmer, U., Vorholt, J.A., Thauer, R.K. and Ermler, U. How an enzyme binds the C1 carrier tetrahydromethanopterin. Structure of the tetrahydromethanopterin-dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1. J. Biol. Chem. 280 (2005) 13712–13719. [DOI] [PMID: 15632161] |
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[EC 4.2.1.147 created 2014] |
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EC |
6.3.2.33 |
Accepted name: |
tetrahydrosarcinapterin synthase |
Reaction: |
ATP + tetrahydromethanopterin + L-glutamate = ADP + phosphate + 5,6,7,8-tetrahydrosarcinapterin |
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For diagram of methanopterin biosynthesis (part 4), click here |
Other name(s): |
H4MPT:α-L-glutamate ligase; MJ0620; MptN protein |
Systematic name: |
tetrahydromethanopterin:α-L-glutamate ligase (ADP-forming) |
Comments: |
This enzyme catalyses the biosynthesis of 5,6,7,8-tetrahydrosarcinapterin, a modified form of tetrahydromethanopterin found in the Methanosarcinales. It does not require K+, and does not discriminate between ATP and GTP [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Li, H., Xu, H., Graham, D.E. and White, R.H. Glutathione synthetase homologs encode α-L-glutamate ligases for methanogenic coenzyme F420 and tetrahydrosarcinapterin biosyntheses. Proc. Natl. Acad. Sci. USA 100 (2003) 9785–9790. [DOI] [PMID: 12909715] |
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[EC 6.3.2.33 created 2010] |
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EC |
7.2.1.4 |
Accepted name: |
tetrahydromethanopterin S-methyltransferase |
Reaction: |
5-methyl-5,6,7,8-tetrahydromethanopterin + CoM + 2 Na+[side 1] = 5,6,7,8-tetrahydromethanopterin + 2-(methylsulfanyl)ethane-1-sulfonate + 2 Na+[side 2] |
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For diagram of methane biosynthesis, click here |
Glossary: |
CoM = coenzyme M = 2-sulfanylethane-1-sulfonate
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): |
tetrahydromethanopterin methyltransferase; mtrA-H (gene names); cmtA (gene name); N5-methyltetrahydromethanopterin—coenzyme M methyltransferase; 5-methyl-5,6,7,8-tetrahydromethanopterin:2-mercaptoethanesulfonate 2-methyltransferase |
Systematic name: |
5-methyl-5,6,7,8-tetrahydromethanopterin:CoM 2-methyltransferase (Na+-transporting) |
Comments: |
Involved in the formation of methane from CO2 in methanogenic archaea. The reaction involves the export of one or two sodium ions. The enzyme from the archaeon Methanobacterium thermoautotrophicum is a membrane-associated multienzyme complex composed of eight different subunits, and contains a 5′-hydroxybenzimidazolyl-cobamide cofactor, to which the methyl group is attached during the transfer. A soluble enzyme that is induced by the presence of CO has been reported as well [6]. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 103406-60-6 |
References: |
1. |
Sauer, F.D. Tetrahydromethanopterin methyltransferase, a component of the methane synthesizing complex of Methanobacterium thermoautotrophicum. Biochem. Biophys. Res. Commun. 136 (1986) 542–547. [DOI] [PMID: 3085670] |
2. |
Gartner, P., Ecker, A., Fischer, R., Linder, D., Fuchs, G. and Thauer, R.K. Purification and properties of N5-methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanobacterium thermoautotrophicum. Eur. J. Biochem. 213 (1993) 537–545. [DOI] [PMID: 8477726] |
3. |
Weiss, D.S., Gartner, P. and Thauer, R.K. The energetics and sodium-ion dependence of N5-methyltetrahydromethanopterin:coenzyme M methyltransferase studied with cob(I)alamin as methyl acceptor and methylcob(III)alamin as methyl donor. Eur. J. Biochem. 226 (1994) 799–809. [DOI] [PMID: 7813469] |
4. |
Harms, U., Weiss, D.S., Gartner, P., Linder, D. and Thauer, R.K. The energy conserving N5-methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum is composed of eight different subunits. Eur. J. Biochem. 228 (1995) 640–648. [DOI] [PMID: 7737157] |
5. |
Gottschalk, G. and Thauer, R.K. The Na+-translocating methyltransferase complex from methanogenic archaea. Biochim. Biophys. Acta 1505 (2001) 28–36. [DOI] [PMID: 11248186] |
6. |
Vepachedu, V.R. and Ferry, J.G. Role of the fused corrinoid/methyl transfer protein CmtA during CO-dependent growth of Methanosarcina acetivorans. J. Bacteriol. 194 (2012) 4161–4168. [DOI] [PMID: 22636775] |
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[EC 7.2.1.4 created 1989 as EC 2.1.1.86, modified 2000, modified 2017, transferred 2024 to EC 7.2.1.4] |
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