The Enzyme Database

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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, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, 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, EXPASY, KEGG, MetaCyc, PDB, UM-BBD
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]
 
 
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 coenzyme 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]
 
 
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     
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]
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 prosthetic group, 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, EXPASY, KEGG, MetaCyc, UM-BBD, 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]
[EC 2.1.1.86 created 1989, modified 2000, modified 2017]
 
 
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, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, 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, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, 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]
[EC 4.1.2.59 created 2017]
 
 
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
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]
[EC 4.2.1.147 created 2014]
 
 
EC 6.3.2.33     
Accepted name: tetrahydrosarcinapterin synthase
Reaction: ATP + tetrahydromethanopterin + L-glutamate = ADP + phosphate + 5,6,7,8-tetrahydrosarcinapterin
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]
[EC 6.3.2.33 created 2010]
 
 


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