EC |
1.1.1.268 |
Accepted name: |
2-(R)-hydroxypropyl-CoM dehydrogenase |
Reaction: |
2-(R)-hydroxypropyl-CoM + NAD+ = 2-oxopropyl-CoM + NADH + H+ |
|
For diagram of epoxide carboxylation, click here |
Glossary: |
coenzyme M (CoM) = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated) |
Other name(s): |
2-(2-(R)-hydroxypropylthio)ethanesulfonate dehydrogenase; 2-[2-(R)-hydroxypropylthio]ethanesulfonate:NAD+ oxidoreductase |
Systematic name: |
2-{[(2R)-2-hydroxypropyl]sulfanyl}ethane-1-sulfonate:NAD+ oxidoreductase |
Comments: |
The enzyme is highly specific for (R)-2-hydroxyalkyl thioethers of CoM, in contrast to EC 1.1.1.269, 2-(S)-hydroxypropyl-CoM dehydrogenase, which is highly specific for the (S)-enantiomer. This enzyme forms component III of a four-component enzyme system (comprising EC 4.4.1.23 [2-hydroxypropyl-CoM lyase; component I], EC 1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II], EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV]) that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 244301-33-5 |
References: |
1. |
Allen, J.R., Clark, D.D., Krum, J.G. and Ensign, S.A. A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation. Proc. Natl. Acad. Sci. USA 96 (1999) 8432–8437. [DOI] [PMID: 10411892] |
|
[EC 1.1.1.268 created 2001] |
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|
|
|
EC |
1.1.1.269 |
Accepted name: |
2-(S)-hydroxypropyl-CoM dehydrogenase |
Reaction: |
(2S)-2-hydroxypropyl-CoM + NAD+ = 2-oxopropyl-CoM + NADH + H+ |
|
For diagram of epoxide carboxylation, click here |
Glossary: |
coenzyme M (CoM) = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated) |
Other name(s): |
2-(2-(S)-hydroxypropylthio)ethanesulfonate dehydrogenase; 2-[2-(S)-hydroxypropylthio]ethanesulfonate:NAD+ oxidoreductase |
Systematic name: |
2-{[(2S)-2-hydroxypropyl]sulfanyl}ethanesulfonate:NAD+ oxidoreductase |
Comments: |
The enzyme is highly specific for (2S)-2-hydroxyalkyl thioethers of CoM, in contrast to EC 1.1.1.268, 2-(R)-hydroxypropyl-CoM dehydrogenase, which is highly specific for the (R)-enantiomer. This enzyme forms component IV of a four-component enzyme system EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC 1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II], EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV].html">click here that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 369364-40-9 |
References: |
1. |
Allen, J.R., Clark, D.D., Krum, J.G. and Ensign, S.A. A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation. Proc. Natl. Acad. Sci. USA 96 (1999) 8432–8437. [DOI] [PMID: 10411892] |
|
[EC 1.1.1.269 created 2001] |
|
|
|
|
EC |
1.1.1.272 |
Accepted name: |
D-2-hydroxyacid dehydrogenase (NADP+) |
Reaction: |
an (R)-2-hydroxycarboxylate + NADP+ = a 2-oxocarboxylate + NADPH + H+ |
|
For diagram of coenzyme M biosynthesis, click here |
Other name(s): |
ddh (gene name) |
Systematic name: |
(R)-2-hydroxycarboxylate:NADP+ oxidoreductase |
Comments: |
This enzyme, characterized from the halophilic archaeon Haloferax mediterranei and the mold Aspergillus oryzae, catalyses a stereospecific reduction of 2-oxocarboxylic acids into the corresponding D-2-hydroxycarboxylic acids. The enzyme prefers substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain, and can use NADH with much lower efficiency. cf. EC 1.1.1.345, (D)-2-hydroxyacid dehydrogenase (NAD+). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 81210-65-3 |
References: |
1. |
Domenech, J. and Ferrer, J. A new D-2-hydroxyacid dehydrogenase with dual coenzyme-specificity from Haloferax mediterranei, sequence analysis and heterologous overexpression. Biochim. Biophys. Acta 1760 (2006) 1667–1674. [DOI] [PMID: 17049749] |
2. |
Shimizu, M., Yamamoto, T., Okabe, N., Sakai, K., Koide, E., Miyachi, Y., Kurimoto, M., Mochizuki, M., Yoshino-Yasuda, S., Mitsui, S., Ito, A., Murano, H., Takaya, N. and Kato, M. Novel 4-methyl-2-oxopentanoate reductase involved in synthesis of the Japanese sake flavor, ethyl leucate. Appl. Microbiol. Biotechnol. (2015) . [DOI] [PMID: 26615399] |
|
[EC 1.1.1.272 created 2002, modified 2013] |
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|
|
|
EC |
1.1.1.338 |
Accepted name: |
(2R)-3-sulfolactate dehydrogenase (NADP+) |
Reaction: |
(2R)-3-sulfolactate + NADP+ = 3-sulfopyruvate + NADPH + H+ |
|
For diagram of coenzyme-M biosynthesis, click here |
Other name(s): |
(R)-sulfolactate:NADP+ oxidoreductase; L-sulfolactate dehydrogenase; (R)-sulfolactate dehydrogenase; ComC |
Systematic name: |
(2R)-3-sulfolactate:NADP+ oxidoreductase |
Comments: |
The enzyme from the bacterium Chromohalobacter salexigens can only utilize NADP+. It functions both biosynthetically in coenzyme M biosynthesis and degradatively, in the degradation of sulfolactate. It can not use (S)-malate and (S)-lactate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 81210-65-3 |
References: |
1. |
Denger, K. and Cook, A.M. Racemase activity effected by two dehydrogenases in sulfolactate degradation by Chromohalobacter salexigens: purification of (S)-sulfolactate dehydrogenase. Microbiology 156 (2010) 967–974. [DOI] [PMID: 20007648] |
|
[EC 1.1.1.338 created 2012] |
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|
|
|
EC |
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] |
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[EC 1.2.7.12 created 1992 as EC 1.2.99.5, transferred 2017 to EC 1.2.7.12] |
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|
|
EC
|
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] |
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|
|
|
EC |
1.3.4.1 |
Accepted name: |
fumarate reductase (CoM/CoB) |
Reaction: |
fumarate + CoM + CoB = succinate + CoM-S-S-CoB |
Glossary: |
CoB = coenzyme B = N-(7-sulfanylheptanoyl)threonine = N-(7-mercaptoheptanoyl)threonine (deprecated)
CoM = coenzyme M = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated) |
Other name(s): |
thiol:fumarate reductase; Tfr |
Systematic name: |
fumarate CoM:CoB oxidoreductase (succinate-forming) |
Comments: |
The enzyme, isolated from the archaeon Methanobacterium thermoautotrophicum, is very oxygen sensitive. It cannot use reduced flavins, reduced coenzyme F420, or NAD(P)H as an electron donor. Distinct from EC 1.3.1.6 [fumarate reductase (NADH)], EC 1.3.5.1 [succinate dehydrogenase (ubiquinone)], and EC 1.3.5.4 [fumarate reductase (quinol)]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Khandekar, S.S. and Eirich, L.D. Purification and characterization of an anabolic fumarate reductase from Methanobacterium thermoautotrophicum. Appl. Environ. Microbiol. 55 (1989) 856–861. [PMID: 2499256] |
2. |
Heim, S., Kunkel, A., Thauer, R.K. and Hedderich, R. Thiol:fumarate reductase (Tfr) from Methanobacterium thermoautotrophicum. Identification of the catalytic sites for fumarate reduction and thiol oxidation. Eur. J. Biochem. 253 (1998) 292–299. [DOI] [PMID: 9578488] |
|
[EC 1.3.4.1 created 2014 as EC 1.3.98.2, transferred 2014 to EC 1.3.4.1] |
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|
|
|
EC |
1.8.1.5 |
Accepted name: |
2-oxopropyl-CoM reductase (carboxylating) |
Reaction: |
CoM + acetoacetate + NADP+ = 2-oxopropyl-CoM + CO2 + NADPH |
|
For diagram of epoxide carboxylation, click here |
Glossary: |
coenzyme M (CoM) = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated) |
Other name(s): |
NADPH:2-(2-ketopropylthio)ethanesulfonate oxidoreductase/carboxylase; NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase; 2-mercaptoethanesulfonate,acetoacetate:NADP+ oxidoreductase (decarboxylating) |
Systematic name: |
2-sulfanylethane-1-sulfonate,acetoacetate:NADP+ oxidoreductase (decarboxylating) |
Comments: |
Also acts on thioethers longer in chain length on the oxo side, e.g. 2-oxobutyl-CoM, but this portion must be attached to CoM (2-sulfanylethane-1-sulfonate); no CoM analogs will substitute. This enzyme forms component II of a four-component enzyme system EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC 1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II], EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV].html">click here that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 244301-63-1 |
References: |
1. |
Allen, J.R., Clark, D.D., Krum, J.G. and Ensign, S.A. A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation. Proc. Natl. Acad. Sci. USA 96 (1999) 8432–8437. [DOI] [PMID: 10411892] |
2. |
Clark, D.D., Allen, J.R. and Ensign, S.A. Characterization of five catalytic activities associated with the NADPH:2-ketopropyl-coenzyme M [2-(2-ketopropylthio)ethanesulfonate] oxidoreductase/carboxylase of the Xanthobacter strain Py2 epoxide carboxylase system. Biochemistry 39 (2000) 1294–1304. [DOI] [PMID: 10684609] |
|
[EC 1.8.1.5 created 2001] |
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|
EC |
1.8.7.3 |
Accepted name: |
ferredoxin:CoB-CoM heterodisulfide reductase |
Reaction: |
2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM = 2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+ |
Glossary: |
CoB = coenzyme B = N-(7-sulfanylheptanoyl)threonine = N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (deprecated)
CoM = coenzyme M = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated)
CoM-S-S-CoB = CoB-CoM heterodisulfide = N-{7-[(2-sulfoethyl)dithio]heptanoyl}-O3-phospho-L-threonine =
O3-phospho-N-{7-[2-(2-sulfoethyl)disulfan-1-yl]heptanoyl}-L-threonine |
Other name(s): |
hdrABC (gene names); hdrA1B1C1 (gene names); hdrA2B2C2 (gene names) |
Systematic name: |
CoB,CoM:ferredoxin oxidoreductase |
Comments: |
HdrABC is an enzyme complex that is found in most methanogens and catalyses the reduction of the CoB-CoM heterodisulfide back to CoB and CoM. HdrA contains a FAD cofactor that acts as the entry point for electrons, which are transferred via HdrC to the HdrB catalytic subunit. One form of the enzyme from Methanosarcina acetivorans (HdrA2B2C2) can also catalyse EC 1.8.98.4, coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase. cf. EC 1.8.98.5, H2:CoB-CoM heterodisulfide,ferredoxin reductase, EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase, and EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Buan, N.R. and Metcalf, W.W. Methanogenesis by Methanosarcina acetivorans involves two structurally and functionally distinct classes of heterodisulfide reductase. Mol. Microbiol. 75 (2010) 843–853. [DOI] [PMID: 19968794] |
2. |
Yan, Z., Wang, M. and Ferry, J.G. A ferredoxin- and F420H2-dependent, electron-bifurcating, heterodisulfide reductase with homologs in the domains Bacteria and Archaea. mBio 8 (2017) e02285-16. [DOI] [PMID: 28174314] |
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[EC 1.8.7.3 created 2017] |
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EC |
1.8.98.1 |
Accepted name: |
dihydromethanophenazine:CoB-CoM heterodisulfide reductase |
Reaction: |
CoB + CoM + methanophenazine = CoM-S-S-CoB + dihydromethanophenazine |
|
For diagram of methane biosynthesis, click here |
Glossary: |
CoB = coenzyme B = N-(7-sulfanylheptanoyl)threonine = N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (deprecated)
CoM = coenzyme M = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated)
methanophenazine = 2-{[(6E,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl]oxy}phenazine
CoM-S-S-CoB = CoB-CoM heterodisulfide = N-{7-[(2-sulfoethyl)dithio]heptanoyl}-O3-phospho-L-threonine = O3-phospho-N-{7-[2-(2-sulfoethyl)disulfan-1-yl]heptanoyl}-L-threonine |
Other name(s): |
hdrDE (gene names); CoB—CoM heterodisulfide reductase (ambiguous); heterodisulfide reductase (ambiguous); coenzyme B:coenzyme M:methanophenazine oxidoreductase |
Systematic name: |
CoB:CoM:methanophenazine oxidoreductase |
Comments: |
This enzyme, found in methanogenic archaea that belong to the Methanosarcinales order, regenerates CoM and CoB after the action of EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase. It is a membrane-bound enzyme that contains (per heterodimeric unit) two distinct b-type hemes and two [4Fe-4S] clusters. cf. EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase, EC 1.8.98.5, H2:CoB-CoM heterodisulfide,ferredoxin reductase, EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase and EC 1.8.98.4, coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Hedderich, R., Berkessel, A. and Thauer, R.K. Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg). Eur. J. Biochem. 193 (1990) 255–261. [DOI] [PMID: 2121478] |
2. |
Abken, H.J., Tietze, M., Brodersen, J., Bäumer, S., Beifuss, U. and Deppenmeier, U. Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei gol. J. Bacteriol. 180 (1998) 2027–2032. [PMID: 9555882] |
3. |
Simianu, M., Murakami, E., Brewer, J.M. and Ragsdale, S.W. Purification and properties of the heme- and iron-sulfur-containing heterodisulfide reductase from Methanosarcina thermophila. Biochemistry 37 (1998) 10027–10039. [DOI] [PMID: 9665708] |
4. |
Murakami, E., Deppenmeier, U. and Ragsdale, S.W. Characterization of the intramolecular electron transfer pathway from 2-hydroxyphenazine to the heterodisulfide reductase from Methanosarcina thermophila. J. Biol. Chem. 276 (2001) 2432–2439. [DOI] [PMID: 11034998] |
|
[EC 1.8.98.1 created 2003, modified 2017] |
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|
|
EC |
1.8.98.4 |
Accepted name: |
coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase |
Reaction: |
2 oxidized coenzyme F420 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 reduced coenzyme F420 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB |
Glossary: |
CoB = coenzyme B = N-(7-sulfanylheptanoyl)threonine = N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (deprecated)
CoM = coenzyme M = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated)
CoM-S-S-CoB = CoB-CoM heterodisulfide = N-{7-[(2-sulfoethyl)dithio]heptanoyl}-O3-phospho-L-threonine =
O3-phospho-N-{7-[2-(2-sulfoethyl)disulfan-1-yl]heptanoyl}-L-threonine |
Other name(s): |
hdrA2B2C2 (gene names) |
Systematic name: |
CoB,CoM,ferredoxin:coenzyme F420 oxidoreductase |
Comments: |
The enzyme, characterized from the archaeon Methanosarcina acetivorans, catalyses the reduction of CoB-CoM heterodisulfide back to CoB and CoM. The enzyme consists of three components, HdrA, HdrB and HdrC, all of which contain [4Fe-4S] clusters. Electrons enter at HdrA, which also contains FAD, and are transferred via HdrC to the catalytic component, HdrB. During methanogenesis from acetate the enzyme catalyses the activity of EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase. However, it can also use electron bifurcation to direct electron pairs from reduced coenzyme F420 towards the reduction of both ferredoxin and CoB-CoM heterodisulfide. This activity is proposed to take place during Fe(III)-dependent anaerobic methane oxidation. cf. EC 1.8.98.5, H2:CoB-CoM heterodisulfide,ferredoxin reductase, EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase, and EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Yan, Z., Wang, M. and Ferry, J.G. A ferredoxin- and F420H2-dependent, electron-bifurcating, heterodisulfide reductase with homologs in the domains Bacteria and Archaea. mBio 8 (2017) e02285-16. [DOI] [PMID: 28174314] |
|
[EC 1.8.98.4 created 2017] |
|
|
|
|
EC |
1.8.98.5 |
Accepted name: |
H2:CoB-CoM heterodisulfide,ferredoxin reductase |
Reaction: |
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB |
Glossary: |
CoB = coenzyme B = N-(7-sulfanylheptanoyl)threonine = N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (deprecated)
CoM = coenzyme M = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated)
CoM-S-S-CoB = CoB-CoM heterodisulfide = N-{7-[(2-sulfoethyl)dithio]heptanoyl}-O3-phospho-L-threonine =
O3-phospho-N-{7-[2-(2-sulfoethyl)disulfan-1-yl]heptanoyl}-L-threonine |
Systematic name: |
CoB,CoM,ferredoxin:H2 oxidoreductase |
Comments: |
This enzyme complex is found in H2-oxidizing CO2-reducing methanogenic archaea such as Methanothermobacter thermautotrophicus. It consists of a cytoplasmic complex of HdrABC reductase and MvhAGD hydrogenase. Electron pairs donated by the hydrogenase are transferred via its δ subunit to the HdrA subunit of the reductase, where they are bifurcated, reducing both ferredoxin and CoB-CoM heterodisulfide. The reductase can also form a similar complex with formate dehydrogenase, see EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase. cf. EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase, EC 1.8.98.4, coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase, and EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Reeve, J.N., Beckler, G.S., Cram, D.S., Hamilton, P.T., Brown, J.W., Krzycki, J.A., Kolodziej, A.F., Alex, L., Orme-Johnson, W.H. and Walsh, C.T. A hydrogenase-linked gene in Methanobacterium thermoautotrophicum strain δ H encodes a polyferredoxin. Proc. Natl. Acad. Sci. USA 86 (1989) 3031–3035. [DOI] [PMID: 2654933] |
2. |
Hedderich, R., Koch, J., Linder, D. and Thauer, R.K. The heterodisulfide reductase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic of pyridine-nucleotide-dependent thioredoxin reductases. Eur. J. Biochem. 225 (1994) 253–261. [DOI] [PMID: 7925445] |
3. |
Setzke, E., Hedderich, R., Heiden, S. and Thauer, R.K. H2: heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum. Composition and properties. Eur. J. Biochem. 220 (1994) 139–148. [DOI] [PMID: 8119281] |
4. |
Stojanowic, A., Mander, G.J., Duin, E.C. and Hedderich, R. Physiological role of the F420-non-reducing hydrogenase (Mvh) from Methanothermobacter marburgensis. Arch. Microbiol. 180 (2003) 194–203. [DOI] [PMID: 12856108] |
5. |
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] |
6. |
Costa, K.C., Lie, T.J., Xia, Q. and Leigh, J.A. VhuD facilitates electron flow from H2 or formate to heterodisulfide reductase in Methanococcus maripaludis. J. Bacteriol. 195 (2013) 5160–5165. [DOI] [PMID: 24039260] |
|
[EC 1.8.98.5 created 2017] |
|
|
|
|
EC |
1.8.98.6 |
Accepted name: |
formate:CoB-CoM heterodisulfide,ferredoxin reductase |
Reaction: |
2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB |
Glossary: |
CoB = coenzyme B = N-(7-sulfanylheptanoyl)threonine = N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (deprecated)
CoM = coenzyme M = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated)
CoM-S-S-CoB = CoB-CoM heterodisulfide = N-{7-[(2-sulfoethyl)dithio]heptanoyl}-O3-phospho-L-threonine =
O3-phospho-N-{7-[2-(2-sulfoethyl)disulfan-1-yl]heptanoyl}-L-threonine |
Systematic name: |
coenzyme B,coenzyme M,ferredoxin:formate oxidoreductase |
Comments: |
The enzyme is found in formate-oxidizing CO2-reducing methanogenic archaea such as Methanococcus maripaludis. It consists of a cytoplasmic complex of HdrABC reductase and formate dehydrogenase. Electron pairs donated by formate dehydrogenase are transferred to the HdrA subunit of the reductase, where they are bifurcated, reducing both ferredoxin and CoB-CoM heterodisulfide. cf. EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase, EC 1.8.98.4, coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase, EC 1.8.98.5, H2:CoB-CoM heterodisulfide,ferredoxin reductase, and EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Costa, K.C., Wong, P.M., Wang, T., Lie, T.J., Dodsworth, J.A., Swanson, I., Burn, J.A., Hackett, M. and Leigh, J.A. Protein complexing in a methanogen suggests electron bifurcation and electron delivery from formate to heterodisulfide reductase. Proc. Natl. Acad. Sci. USA 107 (2010) 11050–11055. [DOI] [PMID: 20534465] |
2. |
Costa, K.C., Lie, T.J., Xia, Q. and Leigh, J.A. VhuD facilitates electron flow from H2 or formate to heterodisulfide reductase in Methanococcus maripaludis. J. Bacteriol. 195 (2013) 5160–5165. [DOI] [PMID: 24039260] |
|
[EC 1.8.98.6 created 2017] |
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|
|
|
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 |
2.1.1.90 |
Accepted name: |
methanol—corrinoid protein Co-methyltransferase |
Reaction: |
methanol + a [Co(I) methanol-specific corrinoid protein] = a [methyl-Co(III) methanol-specific corrinoid protein] + H2O |
Other name(s): |
methanol cobalamin methyltransferase; methanol:5-hydroxybenzimidazolylcobamide methyltransferase; MT 1 (ambiguous); methanol—5-hydroxybenzimidazolylcobamide Co-methyltransferase; mtaB (gene name) |
Systematic name: |
methanol:5-hydroxybenzimidazolylcobamide Co-methyltransferase |
Comments: |
The enzyme, which catalyses the transfer of methyl groups from methanol to a methanol-specific corrinoid protein (MtaC), is involved in methanogenesis from methanol. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. Free cob(I)alamin can substitute for the corrinoid protein in vitro [2].
Inactivated by oxygen and other oxidizing agents, and reactivated by catalytic amounts of ATP and hydrogen. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 86611-98-5 |
References: |
1. |
van der Meijden, P., te Brömmelstroet, B.W., Poirot, C.M., van der Drift, C. and Vogels, G.D. Purification and properties of methanol:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri. J. Bacteriol. 160 (1984) 629–635. [PMID: 6438059] |
2. |
Sauer, K. and Thauer, R.K. Methanol:coenzyme M methyltransferase from Methanosarcina barkeri – substitution of the corrinoid harbouring subunit MtaC by free cob(I)alamin. Eur. J. Biochem. 261 (1999) 674–681. [DOI] [PMID: 10215883] |
|
[EC 2.1.1.90 created 1989, modified 2012] |
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|
|
EC |
2.1.1.246 |
Accepted name: |
[methyl-Co(III) methanol-specific corrinoid protein]—coenzyme M methyltransferase |
Reaction: |
a [methyl-Co(III) methanol-specific corrinoid protein] + CoM = methyl-CoM + a [Co(I) methanol-specific corrinoid protein] |
Glossary: |
CoM = coenzyme M = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated) |
Other name(s): |
methyltransferase 2 (ambiguous); mtaA (gene name) |
Systematic name: |
methylated methanol-specific corrinoid protein:CoM methyltransferase |
Comments: |
The enzyme, which is involved in methanogenesis from methanol, catalyses the transfer of a methyl group from a corrinoid protein (see EC 2.1.1.90, methanol—corrinoid protein Co-methyltransferase), where it is bound to the cobalt cofactor, to CoM, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis. Free methylcob(I)alamin can substitute for the corrinoid protein in vitro [5]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
LeClerc, G.M. and Grahame, D.A. Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression. J. Biol. Chem. 271 (1996) 18725–18731. [DOI] [PMID: 8702528] |
2. |
Harms, U. and Thauer, R.K. Methylcobalamin: coenzyme M methyltransferase isoenzymes MtaA and MtbA from Methanosarcina barkeri. Cloning, sequencing and differential transcription of the encoding genes, and functional overexpression of the mtaA gene in Escherichia coli. Eur. J. Biochem. 235 (1996) 653–659. [DOI] [PMID: 8654414] |
3. |
Sauer, K. and Thauer, R.K. Methanol:coenzyme M methyltransferase from Methanosarcina barkeri. Zinc dependence and thermodynamics of the methanol:cob(I)alamin methyltransferase reaction. Eur. J. Biochem. 249 (1997) 280–285. [DOI] [PMID: 9363780] |
4. |
Sauer, K., Harms, U. and Thauer, R.K. Methanol:coenzyme M methyltransferase from Methanosarcina barkeri. Purification, properties and encoding genes of the corrinoid protein MT1. Eur. J. Biochem. 243 (1997) 670–677. [DOI] [PMID: 9057830] |
5. |
Sauer, K. and Thauer, R.K. Methanol:coenzyme M methyltransferase from Methanosarcina barkeri – substitution of the corrinoid harbouring subunit MtaC by free cob(I)alamin. Eur. J. Biochem. 261 (1999) 674–681. [DOI] [PMID: 10215883] |
|
[EC 2.1.1.246 created 2012] |
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|
|
EC |
2.1.1.247 |
Accepted name: |
[methyl-Co(III) methylamine-specific corrinoid protein]—coenzyme M methyltransferase |
Reaction: |
a [methyl-Co(III) methylamine-specific corrinoid protein] + CoM = methyl-CoM + a [Co(I) methylamine-specific corrinoid protein] |
Glossary: |
CoM = coenzyme M = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated) |
Other name(s): |
methyltransferase 2 (ambiguous); MT2 (ambiguous); MT2-A; mtbA (gene name); [methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M methyltransferase |
Systematic name: |
methylated monomethylamine-specific corrinoid protein:CoM methyltransferase |
Comments: |
Contains zinc [2]. The enzyme, which is involved in methanogenesis from mono-, di-, and trimethylamine, catalyses the transfer of a methyl group bound to the cobalt cofactor of several corrinoid proteins (mono-, di-, and trimethylamine-specific corrinoid proteins, cf. EC 2.1.1.248, methylamine—corrinoid protein Co-methyltransferase, EC 2.1.1.249, dimethylamine—corrinoid protein Co-methyltransferase, and EC 2.1.1.250, trimethylamine—corrinoid protein Co-methyltransferase) to CoM, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Burke, S.A. and Krzycki, J.A. Involvement of the "A" isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine. J. Bacteriol. 177 (1995) 4410–4416. [DOI] [PMID: 7635826] |
2. |
LeClerc, G.M. and Grahame, D.A. Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression. J. Biol. Chem. 271 (1996) 18725–18731. [DOI] [PMID: 8702528] |
3. |
Ferguson, D.J., Jr. and Krzycki, J.A. Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri. J. Bacteriol. 179 (1997) 846–852. [DOI] [PMID: 9006042] |
4. |
Burke, S.A., Lo, S.L. and Krzycki, J.A. Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine. J. Bacteriol. 180 (1998) 3432–3440. [PMID: 9642198] |
5. |
Ferguson, D.J., Jr., Gorlatova, N., Grahame, D.A. and Krzycki, J.A. Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri. J. Biol. Chem. 275 (2000) 29053–29060. [DOI] [PMID: 10852929] |
|
[EC 2.1.1.247 created 2012] |
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|
|
EC |
2.1.1.248 |
Accepted name: |
methylamine—corrinoid protein Co-methyltransferase |
Reaction: |
methylamine + a [Co(I) methylamine-specific corrinoid protein] = a [methyl-Co(III) methylamine-specific corrinoid protein] + NH3 |
Other name(s): |
mtmB (gene name); monomethylamine methyltransferase |
Systematic name: |
monomethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase |
Comments: |
The enzyme, which catalyses the transfer of a methyl group from methylamine to a methylamine-specific corrinoid protein (MtmC), is involved in methanogenesis from methylamine. The enzyme contains the unusual amino acid pyrrolysine [3]. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.247, methylated methylamine-specific corrinoid protein:coenzyme M methyltransferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Burke, S.A. and Krzycki, J.A. Reconstitution of Monomethylamine:Coenzyme M methyl transfer with a corrinoid protein and two methyltransferases purified from Methanosarcina barkeri. J. Biol. Chem. 272 (1997) 16570–16577. [DOI] [PMID: 9195968] |
2. |
Burke, S.A., Lo, S.L. and Krzycki, J.A. Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine. J. Bacteriol. 180 (1998) 3432–3440. [PMID: 9642198] |
3. |
Krzycki, J.A. Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases. Curr. Opin. Chem. Biol. 8 (2004) 484–491. [DOI] [PMID: 15450490] |
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[EC 2.1.1.248 created 2012] |
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|
|
EC |
2.1.1.249 |
Accepted name: |
dimethylamine—corrinoid protein Co-methyltransferase |
Reaction: |
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein] = a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine |
Other name(s): |
mtbB (gene name); dimethylamine methyltransferase |
Systematic name: |
dimethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase |
Comments: |
The enzyme, which catalyses the transfer of a methyl group from dimethylamine to a dimethylamine-specific corrinoid protein (MtbC), is involved in methanogenesis from dimethylamine. The enzyme contains the unusual amino acid pyrrolysine [3]. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.247, methylated methylamine-specific corrinoid protein:coenzyme M methyltransferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Wassenaar, R.W., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and characterization of dimethylamine:5-hydroxybenzimidazolyl-cobamide methyltransferase from Methanosarcina barkeri Fusaro. Eur. J. Biochem. 253 (1998) 692–697. [DOI] [PMID: 9654067] |
2. |
Ferguson, D.J., Jr., Gorlatova, N., Grahame, D.A. and Krzycki, J.A. Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri. J. Biol. Chem. 275 (2000) 29053–29060. [DOI] [PMID: 10852929] |
3. |
Krzycki, J.A. Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases. Curr. Opin. Chem. Biol. 8 (2004) 484–491. [DOI] [PMID: 15450490] |
|
[EC 2.1.1.249 created 2012] |
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|
EC |
2.1.1.250 |
Accepted name: |
trimethylamine—corrinoid protein Co-methyltransferase |
Reaction: |
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein] = a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine |
Other name(s): |
mttB (gene name); trimethylamine methyltransferase |
Systematic name: |
trimethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase |
Comments: |
The enzyme, which catalyses the transfer of a methyl group from trimethylamine to a trimethylamine-specific corrinoid protein (MttC), is involved in methanogenesis from trimethylamine. The enzyme contains the unusual amino acid pyrrolysine [2]. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.247, methylated methylamine-specific corrinoid protein:coenzyme M methyltransferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Ferguson, D.J., Jr. and Krzycki, J.A. Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri. J. Bacteriol. 179 (1997) 846–852. [DOI] [PMID: 9006042] |
2. |
Krzycki, J.A. Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases. Curr. Opin. Chem. Biol. 8 (2004) 484–491. [DOI] [PMID: 15450490] |
|
[EC 2.1.1.250 created 2012] |
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|
EC |
2.1.1.251 |
Accepted name: |
methylated-thiol—coenzyme M methyltransferase |
Reaction: |
methanethiol + CoM = methyl-CoM + hydrogen sulfide (overall reaction)
(1a) methanethiol + a [Co(I) methylated-thiol-specific corrinoid protein] = a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide (1b) a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + CoM = methyl-CoM + a [Co(I) methylated-thiol-specific corrinoid protein] |
Glossary: |
CoM = coenzyme M = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated) |
Other name(s): |
mtsA (gene name) |
Systematic name: |
methylated-thiol:CoM methyltransferase |
Comments: |
The enzyme, which is involved in methanogenesis from methylated thiols, such as methane thiol, dimethyl sulfide, and 3-(methylsulfanyl)propanoate, catalyses two successive steps - the transfer of a methyl group from the substrate to the cobalt cofactor of a methylated-thiol-specific corrinoid protein (MtsB), and the subsequent transfer of the methyl group from the corrinoid protein to CoM. With most other methanogenesis substrates this process is carried out by two different enzymes (for example, EC 2.1.1.90, methanol—corrinoid protein Co-methyltransferase, and EC 2.1.1.246, [methyl-Co(III) methanol-specific corrinoid protein]—coenzyme M methyltransferase). The cobalt is oxidized during methylation from the Co(I) state to the Co(III) state, and is reduced back to the Co(I) form during demethylation. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Paul, L. and Krzycki, J.A. Sequence and transcript analysis of a novel Methanosarcina barkeri methyltransferase II homolog and its associated corrinoid protein homologous to methionine synthase. J. Bacteriol. 178 (1996) 6599–6607. [DOI] [PMID: 8932317] |
2. |
Tallant, T.C. and Krzycki, J.A. Methylthiol:coenzyme M methyltransferase from Methanosarcina barkeri, an enzyme of methanogenesis from dimethylsulfide and methylmercaptopropionate. J. Bacteriol. 179 (1997) 6902–6911. [DOI] [PMID: 9371433] |
3. |
Tallant, T.C., Paul, L. and Krzycki, J.A. The MtsA subunit of the methylthiol:coenzyme M methyltransferase of Methanosarcina barkeri catalyses both half-reactions of corrinoid-dependent dimethylsulfide: coenzyme M methyl transfer. J. Biol. Chem. 276 (2001) 4485–4493. [DOI] [PMID: 11073950] |
|
[EC 2.1.1.251 created 2012] |
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|
EC |
2.1.1.252 |
Accepted name: |
tetramethylammonium—corrinoid protein Co-methyltransferase |
Reaction: |
tetramethylammonium + a [Co(I) tetramethylammonium-specific corrinoid protein] = a [methyl-Co(III) tetramethylammonium-specific corrinoid protein] + trimethylamine |
Other name(s): |
mtqB (gene name); tetramethylammonium methyltransferase |
Systematic name: |
tetramethylammonium:5-hydroxybenzimidazolylcobamide Co-methyltransferase |
Comments: |
The enzyme, which catalyses the transfer of a methyl group from tetramethylammonium to a tetramethylammonium-specific corrinoid protein (MtqC), is involved in methanogenesis from tetramethylammonium. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.253, methylated tetramethylammonium-specific corrinoid protein:coenzyme M methyltransferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Asakawa, S., Sauer, K., Liesack, W. and Thauer, R.K. Tetramethylammonium:coenzyme M methyltransferase system from methanococcoides s. Arch. Microbiol. 170 (1998) 220–226. [PMID: 9732435] |
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[EC 2.1.1.252 created 2012] |
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|
EC |
2.1.1.253 |
Accepted name: |
[methyl-Co(III) tetramethylammonium-specific corrinoid protein]—coenzyme M methyltransferase |
Reaction: |
a [methyl-Co(III) tetramethylammonium-specific corrinoid protein] + CoM = methyl-CoM + a [Co(I) tetramethylammonium-specific corrinoid protein] |
Glossary: |
CoM = coenzyme M = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated) |
Other name(s): |
methyltransferase 2 (ambiguous); mtqA (gene name) |
Systematic name: |
methylated tetramethylammonium-specific corrinoid protein:CoM methyltransferase |
Comments: |
The enzyme, which is involved in methanogenesis from tetramethylammonium, catalyses the transfer of a methyl group from a corrinoid protein (see EC 2.1.1.252, tetramethylammonium—corrinoid protein Co-methyltransferase), where it is bound to the cobalt cofactor, to CoM, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Asakawa, S., Sauer, K., Liesack, W. and Thauer, R.K. Tetramethylammonium:coenzyme M methyltransferase system from methanococcoides s. Arch. Microbiol. 170 (1998) 220–226. [PMID: 9732435] |
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[EC 2.1.1.253 created 2012] |
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|
EC |
2.1.1.377 |
Accepted name: |
[methyl-Co(III) glycine betaine-specific corrinoid protein]—coenzyme M methyltransferase |
Reaction: |
a [methyl-Co(III) glycine betaine-specific corrinoid protein] + CoM = methyl-CoM + a [Co(I) glycine betaine-specific corrinoid protein] |
Other name(s): |
mtaA (gene name) |
Systematic name: |
methylated glycine betaine-specific corrinoid protein:CoM methyltransferase |
Comments: |
The enzyme, which is involved in methanogenesis from glycine betaine, catalyses the transfer of a methyl group bound to the cobalt cofactor of glycine betaine-specific corrinoid protein to coenzyme M, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, which catalyses the final step in methanogenesis. The enzyme from the methanogenic archaeon Methanolobus vulcani B1d can also catalyse the activity of EC 2.1.1.246, [methyl-Co(III) methanol-specific corrinoid protein]—coenzyme M methyltransferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Creighbaum, A.J., Ticak, T., Shinde, S., Wang, X. and Ferguson, D.J., Jr. Examination of the glycine betaine-dependent methylotrophic methanogenesis pathway: insights into anaerobic quaternary amine methylotrophy. Front. Microbiol. 10:2572 (2019). [DOI] [PMID: 31787957] |
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[EC 2.1.1.377 created 2021] |
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|
|
EC |
2.1.1.379 |
Accepted name: |
[methyl coenzyme M reductase]-L-arginine C-5-methyltransferase |
Reaction: |
2 S-adenosyl-L-methionine + a [methyl coenzyme-M reductase]-L-arginine + reduced acceptor = S-adenosyl-L-homocysteine + L-methionine + 5′-deoxyadenosine + a [methyl coenzyme-M reductase]-(5S)-C-methyl-L-arginine + acceptor |
Other name(s): |
methanogenesis marker protein 10; Mmp10 |
Systematic name: |
S-adenosyl-L-methionine:[methyl coenzyme M reductase]-L-arginine C-5-(S)-methyltransferase |
Comments: |
The enzyme, present in methanogenic archaea, catalyses a modification of an L-arginine residue at the active site of EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase (better known as methyl-coenzyme M reductase), which catalyses the last and methane-releasing step of methanogenesis. The enzyme is a radical AdoMet (radical SAM) enzyme and contains a [4Fe-4S] cluster and a Coα-[α-(5-hydroxybenzimidazolyl)]-cobamide cofactor. The methyl group, which is derived from S-adenosyl-L-methionine, is transferred to the cob(I)amide cofactor, forming methylcob(III)amide as an intermediate carrier, before being transferred to the arginine residue. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Deobald, D., Adrian, L., Schone, C., Rother, M. and Layer, G. Identification of a unique radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase. Sci. Rep. 8:7404 (2018). [DOI] [PMID: 29743535] |
2. |
Radle, M.I., Miller, D.V., Laremore, T.N. and Booker, S.J. Methanogenesis marker protein 10 (Mmp10) from Methanosarcina acetivorans is a radical S-adenosylmethionine methylase that unexpectedly requires cobalamin. J. Biol. Chem. 294 (2019) 11712–11725. [DOI] [PMID: 31113866] |
3. |
Lyu, Z., Shao, N., Chou, C.W., Shi, H., Patel, R., Duin, E.C. and Whitman, W.B. Posttranslational methylation of arginine in methyl coenzyme M reductase has a profound impact on both methanogenesis and growth of Methanococcus maripaludis. J. Bacteriol. 202 (2020) . [DOI] [PMID: 31740491] |
|
[EC 2.1.1.379 created 2021] |
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|
|
|
EC |
2.5.1.76 |
Accepted name: |
cysteate synthase |
Reaction: |
O-phospho-L-serine + sulfite = L-cysteate + phosphate |
Other name(s): |
sulfite:O-phospho-L-serine sulfotransferase (phosphate-hydrolysing, L-cysteate-forming) |
Systematic name: |
sulfite:O-phospho-L-serine sulfonotransferase (phosphate-hydrolysing, L-cysteate-forming) |
Comments: |
A pyridoxal-phosphate protein. It is highly specific for O-phospho-L-serine and sulfite. The reaction proceeds through a dehydroalanine (2-aminoacrylic acid) intermediate. The enzyme from Methanosarcina acetivorans is evolutionarily related to threonine synthase (EC 4.2.3.1), but the reaction is more similar to that of O-phosphoserine sulfhydrylase (EC 2.5.1.65). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Graham, D.E., Taylor, S.M., Wolf, R.Z. and Namboori, S.C. Convergent evolution of coenzyme M biosynthesis in the Methanosarcinales: cysteate synthase evolved from an ancestral threonine synthase. Biochem. J. 424 (2009) 467–478. [DOI] [PMID: 19761441] |
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[EC 2.5.1.76 created 2009] |
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EC |
2.8.4.1 |
Accepted name: |
coenzyme-B sulfoethylthiotransferase |
Reaction: |
methyl-CoM + CoB = CoM-S-S-CoB + methane |
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For diagram of methane biosynthesis, click here |
Glossary: |
CoB = coenzyme B = N-(7-sulfanylheptanoyl)threonine = N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (deprecated)
CoM = coenzyme M = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated) |
Other name(s): |
methyl-CoM reductase; methyl coenzyme M reductase |
Systematic name: |
methyl-CoM:CoB S-(2-sulfoethyl)thiotransferase |
Comments: |
This enzyme catalyses the final step in methanogenesis, the biological production of methane. This important anaerobic process is carried out only by methanogenic archaea. The enzyme can also function in reverse, for anaerobic oxidation of methane.The enzyme requires the hydroporphinoid nickel complex coenzyme F430. Highly specific for coenzyme B with a heptanoyl chain; ethyl CoM and difluoromethyl CoM are poor substrates. The sulfide sulfur can be replaced by selenium but not by oxygen. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Bobik, T.A., Olson, K.D., Noll, K.M. and Wolfe, R.S. Evidence that the heterodisulfide of coenzyme-M and 7-mercaptanoylthreonine phosphate is a product of the methylreductase reaction in Methanobacterium. Biochem. Biophys. Res. Commun. 149 (1987) 455–460. [DOI] [PMID: 3122735] |
2. |
Ellermann, J., Hedderich, R., Boecher, R. and Thauer, R.K. The final step in methane formation: investigations with highly purified methyl coenzyme M reductase component C from Methanobacterium thermoautotrophicum (strain Marburg). Eur. J. Biochem. 184 (1988) 63–68. |
3. |
Ermler, U., Grabarse, W., Shima, S., Goubeaud, M. and Thauer, R.K. Crystal structure of methyl coenzyme M reductase: The key enzyme of biological methane formation. Science 278 (1997) 1457–1462. [DOI] [PMID: 9367957] |
4. |
Signor, L., Knuppe, C., Hug, R., Schweizer, B., Pfaltz, A. and Jaun, B. Methane formation by reaction of a methyl thioether with a photo-excited nickel thiolate — a process mimicking methanogenesis in Archaea. Chemistry 6 (2000) 3508–3516. [PMID: 11072815] |
5. |
Scheller, S., Goenrich, M., Boecher, R., Thauer, R.K. and Jaun, B. The key nickel enzyme of methanogenesis catalyses the anaerobic oxidation of methane. Nature 465 (2010) 606–608. [DOI] [PMID: 20520712] |
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[EC 2.8.4.1 created 2001, modified 2011] |
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EC |
3.1.3.71 |
Accepted name: |
2-phosphosulfolactate phosphatase |
Reaction: |
(2R)-2-phospho-3-sulfolactate + H2O = (2R)-3-sulfolactate + phosphate |
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For diagram of coenzyme-M biosynthesis, click here |
Other name(s): |
(2R)-phosphosulfolactate phosphohydrolase; ComB phosphatase |
Systematic name: |
(R)-2-phospho-3-sulfolactate phosphohydrolase |
Comments: |
Requires Mg2+. The enzyme from Methanococcus jannaschii acts on both stereoisoimers of the substrate and also hydrolyses a number of phosphate monoesters of (S)-2-hydroxycarboxylic acids, including 2-phosphomalate, 2-phospholactate and 2-phosphoglycolate. This enzyme can also hydrolyse phosphate monoesters of (R)-2-hydroxycarboxylic acids such as (S)-2-phospho-3-sulfolactate and (R)-2-phosphomalate, which, presumably, bind to the enzyme in opposite orientations. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 409095-18-7 |
References: |
1. |
Graham, D.E., Graupner, M., Xu, H. and White, R.H. Identification of coenzyme M biosynthetic 2-phosphosulfolactate phosphatase. Eur. J. Biochem. 268 (2001) 5176–5188. [DOI] [PMID: 11589710] |
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[EC 3.1.3.71 created 2002] |
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EC |
4.1.1.79 |
Accepted name: |
sulfopyruvate decarboxylase |
Reaction: |
3-sulfopyruvate = 2-sulfoacetaldehyde + CO2 |
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For diagram of coenzyme-M biosynthesis, click here |
Glossary: |
thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium
2-sulfoacetaldehyde = 2-oxoethanesulfonate |
Other name(s): |
sulfopyruvate carboxy-lyase |
Systematic name: |
3-sulfopyruvate carboxy-lyase (2-sulfoacetaldehyde-forming) |
Comments: |
Requires thiamine diphosphate. Does not decarboxylate pyruvate or phosphonopyruvate. The enzyme appears to be oxygen-sensitive. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 303155-97-7 |
References: |
1. |
Graupner, M., Xu, H. and White, R.H. Identification of the gene encoding sulfopyruvate decarboxylase, an enzyme involved in biosynthesis of coenzyme M. J. Bacteriol. 182 (2000) 4862–4867. [DOI] [PMID: 10940029] |
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[EC 4.1.1.79 created 2002] |
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EC |
4.4.1.19 |
Accepted name: |
phosphosulfolactate synthase |
Reaction: |
(2R)-2-O-phospho-3-sulfolactate = phosphoenolpyruvate + sulfite |
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For diagram of coenzyme M biosynthesis, click here |
Other name(s): |
(2R)-phospho-3-sulfolactate synthase; (2R)-O-phospho-3-sulfolactate sulfo-lyase |
Systematic name: |
(2R)-2-O-phospho-3-sulfolactate hydrogen-sulfite-lyase (phosphoenolpyruvate-forming) |
Comments: |
Requires Mg2+. The enzyme from the archaeon Methanococcus jannaschii catalyses the Michael addition of sulfite to phosphoenolpyruvate. It specifically requires phosphoenolpyruvate and its broad alkaline pH optimum suggests that it uses sulfite rather than hydrogensulfite. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 473575-53-0 |
References: |
1. |
Graham, D.E., Xu, H. and White, R.H. Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of sulfonate-biosynthesizing enzymes. J. Biol. Chem. 277 (2002) 13421–13429. [DOI] [PMID: 11830598] |
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[EC 4.4.1.19 created 2003] |
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EC |
4.4.1.23 |
Accepted name: |
2-hydroxypropyl-CoM lyase |
Reaction: |
(1) (R)-2-hydroxypropyl-CoM = (R)-1,2-epoxypropane + HS-CoM (2) (S)-2-hydroxypropyl-CoM = (S)-1,2-epoxypropane + HS-CoM |
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For diagram of epoxide carboxylation, click here |
Glossary: |
coenzyme M (CoM) = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated) |
Other name(s): |
epoxyalkane:coenzyme M transferase; epoxyalkane:CoM transferase; epoxyalkane:2-mercaptoethanesulfonate transferase; coenzyme M-epoxyalkane ligase; epoxyalkyl:CoM transferase; epoxypropane:coenzyme M transferase; epoxypropyl:CoM transferase; EaCoMT; 2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming); (R)-2-hydroxypropyl-CoM 2-mercaptoethanesulfonate lyase (cyclizing; (R)-1,2-epoxypropane-forming) |
Systematic name: |
(R)[or (S)]-2-hydroxypropyl-CoM:2-sulfanylethane-1-sulfonate lyase (epoxyalkane-ring-forming) |
Comments: |
Requires zinc. Acts on both enantiomers of chiral epoxyalkanes to form the corresponding (R)- and (S)-2-hydroxyalkyl-CoM adducts. The enzyme will function with some other thiols (e.g., 2-sulfanylethanol) as the nucleophile. Uses short-chain epoxyalkanes from C2 (epoxyethane) to C6 (1,2-epoxyhexane). This enzyme forms component I of a four-component enzyme system (comprising EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC 1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II], EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV]) that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 244301-07-3 |
References: |
1. |
Allen, J.R., Clark, D.D., Krum, J.G. and Ensign, S.A. A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation. Proc. Natl. Acad. Sci. USA 96 (1999) 8432–8437. [DOI] [PMID: 10411892] |
2. |
Krum, J.G., Ellsworth, H., Sargeant, R.R., Rich, G. and Ensign, S.A. Kinetic and microcalorimetric analysis of substrate and cofactor interactions in epoxyalkane:CoM transferase, a zinc-dependent epoxidase. Biochemistry 41 (2002) 5005–5014. [DOI] [PMID: 11939797] |
3. |
Coleman, N.V. and Spain, J.C. Epoxyalkane: coenzyme M transferase in the ethene and vinyl chloride biodegradation pathways of Mycobacterium strain JS60. J. Bacteriol. 185 (2003) 5536–5545. [DOI] [PMID: 12949106] |
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[EC 4.4.1.23 created 2001 as EC 4.2.99.19, transferred 2005 to EC 4.4.1.23] |
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EC |
6.2.2.1 |
Accepted name: |
thioglycine synthase |
Reaction: |
ATP + sulfide + a [methyl-coenzyme M reductase]-glycine = ADP + phosphate + a [methyl-coenzyme M reductase]-thioglycine |
Glossary: |
thioglycine = 2-aminoethanethioic O-acid |
Other name(s): |
ycaO (gene name) (ambiguous) |
Systematic name: |
[methyl-coenzyme M reductase]-glycine—sulfur ligase (thioglycine-forming) |
Comments: |
Requires Mg2+. The enzyme is found in anaerobic methanogenic and methanotrophic archaea, where it modifies a glycine residue in EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase (methyl-CoM reductase). Upon binding to its substrate, an external source of sulfide attacks the target amide bond generating a tetrahedral intermediate. The amide oxyanion attacks the γ-phosphate of ATP, releasing ADP and forming a phosphorylated thiolate intermediate that collapses to form thioglycine and phosphate. In most organisms activity requires a second protein (TfuA) , which may allosterically activate this enzyme or assist in the delivery of sulfide to the substrate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Nayak, D.D., Mahanta, N., Mitchell, D.A. and Metcalf, W.W. Post-translational thioamidation of methyl-coenzyme M reductase, a key enzyme in methanogenic and methanotrophic Archaea. Elife 6:e29218 (2017). [PMID: 28880150] |
2. |
Mahanta, N., Liu, A., Dong, S., Nair, S.K. and Mitchell, D.A. Enzymatic reconstitution of ribosomal peptide backbone thioamidation. Proc. Natl. Acad. Sci. USA 115 (2018) 3030–3035. [PMID: 29507203] |
3. |
Dong, S.H., Liu, A., Mahanta, N., Mitchell, D.A. and Nair, S.K. Mechanistic basis for ribosomal peptide backbone modifications. ACS Cent. Sci. 5 (2019) 842–851. [PMID: 31139720] |
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[EC 6.2.2.1 created 2020] |
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EC |
6.3.2.59 |
Accepted name: |
3-methyl-D-ornithine—L-lysine ligase |
Reaction: |
ATP + (3R)-3-methyl-D-ornithine + L-lysine = ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine |
Glossary: |
L-pyrrolysine = N6-{[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-yl]carbonyl}-L-lysine |
Other name(s): |
N6-[(2R,3R)-3-methylornithyl]-L-lysine synthase; 3-methylornithine—L-lysine ligase; pylC (gene name) |
Systematic name: |
(3R)-3-methyl-D-ornithine:L-lysine γ-ligase (ADP-forming) |
Comments: |
The enzyme participates in the biosynthesis of L-pyrrolysine, a naturally occurring, genetically coded amino acid found in some methanogenic archaea and a few bacterial species. L-pyrrolysine is present in several methyltransferases that are involved in methyl transfer from methylated amine compounds to coenzyme M. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Gaston, M.A., Zhang, L., Green-Church, K.B. and Krzycki, J.A. The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine. Nature 471 (2011) 647–650. [DOI] [PMID: 21455182] |
2. |
Cellitti, S.E., Ou, W., Chiu, H.P., Grunewald, J., Jones, D.H., Hao, X., Fan, Q., Quinn, L.L., Ng, K., Anfora, A.T., Lesley, S.A., Uno, T., Brock, A. and Geierstanger, B.H. D-Ornithine coopts pyrrolysine biosynthesis to make and insert pyrroline-carboxy-lysine. Nat. Chem. Biol. 7 (2011) 528–530. [DOI] [PMID: 21525873] |
3. |
Quitterer, F., List, A., Beck, P., Bacher, A. and Groll, M. Biosynthesis of the 22nd genetically encoded amino acid pyrrolysine: structure and reaction mechanism of PylC at 1.5A resolution. J. Mol. Biol. 424 (2012) 270–282. [DOI] [PMID: 22985965] |
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[EC 6.3.2.59 created 2021] |
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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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