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5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
H+ + 5,10-methylenetetrahydromethanopterin
H2 + 5,10-methenyltetrahydromethanopterin
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
additional information
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-
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
-
Substrates: -
Products: -
r
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
-
Substrates: involved in methanogenesis
Products: -
r
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
Substrates: Hmd catalyzes a step in the hydrogenotrophic methanogenesis pathway in class I methanogens
Products: -
?
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
-
Substrates: -
Products: -
r
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
-
Substrates: involved in methanogenesis
Products: -
r
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
-
Substrates: reverse reaction under argon atmosphere
Products: -
r
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
-
Substrates: -
Products: -
?
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
-
Substrates: involved in methanogenesis
Products: -
?
H+ + 5,10-methylenetetrahydromethanopterin
H2 + 5,10-methenyltetrahydromethanopterin
Substrates: the purified enzyme does not catalyze the reduction of viologen dyes, of methylene blue, of flavins, of pyridine nucleotides
Products: -
r
H+ + 5,10-methylenetetrahydromethanopterin
H2 + 5,10-methenyltetrahydromethanopterin
Substrates: the purified enzyme does not catalyze the reduction of viologen dyes, of methylene blue, of flavins, of pyridine nucleotides
Products: -
r
H+ + 5,10-methylenetetrahydromethanopterin
H2 + 5,10-methenyltetrahydromethanopterin
Substrates: -
Products: -
r
H+ + 5,10-methylenetetrahydromethanopterin
H2 + 5,10-methenyltetrahydromethanopterin
Substrates: -
Products: -
r
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
-
Substrates: r
Products: -
?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
-
Substrates: no reaction with: coenzyme F420, NAD+, NADP+
Products: -
?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
-
Substrates: reverse reaction is favoured under alkaline conditions
Products: -
?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
-
Substrates: -
Products: -
?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
-
Substrates: r
Products: -
?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
-
Substrates: no reaction with: coenzyme F420, NAD+, NADP+
Products: -
?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
-
Substrates: no reaction with viologen dyes
Products: -
?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
-
Substrates: r
Products: -
?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
-
Substrates: -
Products: -
?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
-
Substrates: r
Products: -
?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
-
Substrates: no reaction with: coenzyme F420, NAD+, NADP+
Products: -
?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
-
Substrates: no reaction with viologen dyes
Products: -
?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
-
Substrates: r
Products: -
?
additional information
?
-
-
Substrates: no reduction of methyl viologen or methyl blue
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in methanogenesis from CO2 and H2
Products: -
?
additional information
?
-
-
Substrates: no reduction of methyl viologen or methyl blue
Products: -
?
additional information
?
-
-
Substrates: no reduction of viologen dyes in the presence of H2
Products: -
?
additional information
?
-
-
Substrates: under conditions of nickel limitation, the reduction of F420 with H2 is catalyzed by the metal-free methylenetetrahydromethanopterin dehydrogenase system which is composed of H2-forming methylenetetrahydromethanopterin dehydrogenase and F420-dependent methylenetetrahydromethanopterin dehydrogenase
Products: -
?
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5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
additional information
?
-
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
-
Substrates: involved in methanogenesis
Products: -
r
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
Substrates: Hmd catalyzes a step in the hydrogenotrophic methanogenesis pathway in class I methanogens
Products: -
?
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
-
Substrates: involved in methanogenesis
Products: -
r
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
-
Substrates: involved in methanogenesis
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in methanogenesis from CO2 and H2
Products: -
?
additional information
?
-
-
Substrates: under conditions of nickel limitation, the reduction of F420 with H2 is catalyzed by the metal-free methylenetetrahydromethanopterin dehydrogenase system which is composed of H2-forming methylenetetrahydromethanopterin dehydrogenase and F420-dependent methylenetetrahydromethanopterin dehydrogenase
Products: -
?
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KCl
-
the enzyme requires the presence of salts, 50% of maximal activity is reached at 100 mM potassium phosphate, KCl or NaCl
NaCl
-
the enzyme requires the presence of salts, 50% of maximal activity is reached at 100 mM potassium phosphate, KCl or NaCl
Nickel
-
contains less than 0.1 mol Ni per mol of enzyme
potassium phosphate
-
the enzyme requires the presence of salts, 50% of maximal activity is reached at 100 mM potassium phosphate, KCl or NaCl
Zn2+
the zinc content varies from preparation to preparation between 0.5-4 mol zinc/mol enzyme
Fe
-
tightly binds an iron-containing cofactor. The iron is coordinated by two CO molecules, one sulphur and a pyridone derivative, which is linked via a phosphodiester bond to a guanosine base
Fe
Hmd holoenzyme is comprised of 2 iron atoms, each iron atom coordinates the reduction of methenyltetrahydromethanopterin and oxidation of H2 while bound to both Hmd and a cofactor molecule
Fe
-
tightly binds an iron-containing cofactor. The iron is coordinated by two CO molecules, one sulfur and a pyridone derivative, which is linked via a phosphodiester bond to a guanosine base
Iron
-
enzyme contains iron bound to a cofactor of unknown structure, one iron per monomer, iron is released from cofactor upon light inactivation
Iron
-
enzyme contains iron bound to a mercaptoethanol-extractable cofactor of unknown structure, one iron per monomer, iron is released from cofactor upon light inactivation
Iron
-
enzyme contains iron bound to an mercaptoethanol-extractable cofactor of unknown structure, contains intrinsic CO bound to iron
Iron
-
contains approximately 1 mol of iron per mol of enzyme
additional information
-
no iron-sulfur-cluster or nickel
additional information
-
lack of redoxactive transition metals
additional information
-
no iron-sulfur-cluster
additional information
-
no iron-sulfur-cluster or nickel
additional information
the enzyme does not contain iron-sulfur clusters, nickel, or flavins
additional information
-
the enzyme does not contain nickel or iron/sulfur clusters
additional information
-
the enzyme does not contain nickel or iron/sulfur clusters
additional information
-
metal-free protein
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Schwoerer, B.; Fernandez, V.M.; Zirngibl, C.; Thauer, R.K.
H2-Forming N5,N10-methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum
Eur. J. Biochem.
212
255-261
1993
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
brenda
von Bunau, R.; Zirngibl, C.; Thauer, R.K.; Klein, A.
Hydrogen-forming and coenzyme-F420-reducing methylene tetrahydromethanopterin dehydrogenase are genetically distinct enzymes in Methanobacterium thermoautotrophicum
Eur. J. Biochem.
202
1205-1208
1991
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
brenda
Klein, A.R.; Fernandez, V.M.; Thauer, R.K.
H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase: mechanism of H2 formation analyzed using hydrogen isotopes
FEBS Lett.
368
203-206
1995
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
brenda
Schleucher, J.; Griesinger, C.; Schwrer, B.; Thauer, R.K.
H2-Forming N5,N10-methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum catalyzes a stereoselective hydride transfer as determined by two-dimensional NMR spectroscopy
Biochemistry
33
3986-3993
1994
Methanothermobacter thermautotrophicus
brenda
Zirngibl, C.; Hedderich, R.; Thauer, R.K.
N5,N10-Methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum has hydrogenase activity
FEBS Lett.
261
112-116
1990
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
-
brenda
Afting, C.; Hochheimer, A.; Thauer, R.K.
Function of H2-forming methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum in coenzyme F420 reduction with H2
Arch. Microbiol.
169
206-210
1998
Methanothermobacter thermautotrophicus
brenda
Hartmann, G.C.; Klein, A.R.; Linder, M.; Thauer, R.K.
Purification, properties and primary structure of H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase from Methanococcus thermolithotrophicus
Arch. Microbiol.
165
187-193
1996
Methanothermobacter thermautotrophicus, Methanothermococcus thermolithotrophicus
brenda
Ma, M.; Zirngibl, C.; Linder, D.; Stetter, K.O.; Thauer, R.K.
N5,N10-Methylenetetrahydromethanopterin dehydrogenase (H2-forming) from the extreme thermophile Methanopyrus kandleri
Arch. Microbiol.
156
43-48
1991
Methanopyrus kandleri
brenda
Luo, H.W.; Zhang, H.; Suzuki, T.; Hattori, S.; Kamagata, Y.
Differential expression of methanogenesis genes of Methanothermobacter thermoautotrophicus (formerly Methanobacterium thermoautotrophicum) in pure culture and in cocultures with fatty acid-oxidizing syntrophs
Appl. Environ. Microbiol.
68
1173-1179
2002
Methanothermobacter thermautotrophicus
brenda
Lyon, E.J.; Shima, S.; Buurman, G.; Chowdhuri, S.; Batschauer, A.; Steinbach, K.; Thauer, R.K.
UV-A/blue-light inactivation of the metal-free hydrogenase (Hmd) from methanogenic archaea. The enzyme contains functional iron after all
Eur. J. Biochem.
271
195-204
2004
Methanocaldococcus jannaschii, Methanothermobacter marburgensis
brenda
Bartoschek, S.; Buurman, G.; Geierstanger, B.H.; Lapham, J.; Griesinger, C.
Measurement and ab initio calculation of CSA/dipole-dipole cross-correlated relaxation provide insight into the mechanism of a H2-forming dehydrogenase
J. Am. Chem. Soc.
125
13308-13309
2003
Methanothermobacter marburgensis
brenda
Lyon, E.J.; Shima, S.; Boecher, R.; Thauer, R.K.; Grevels, F.W.; Bill, E.; Roseboom, W.; Albracht, S.P.J.
Carbon monoxide as an intrinsic ligand to iron in the active site of the iron-sulfur-cluster-free hydrogenase H2-forming methylenetetrahydromethanopterin dehydrogenase as revealed by infrared spectroscopy
J. Am. Chem. Soc.
126
14239-14248
2004
Methanothermobacter marburgensis
brenda
Pilak, O.; Mamat, B.; Vogt, S.; Hagemeier, C.H.; Thauer, R.K.; Shima, S.; Vonrhein, C.; Warkentin, E.; Ermler, U.
The Crystal structure of the apoenzyme of the iron-sulphur cluster-free hydrogenase
J. Mol. Biol.
358
798-809
2006
Methanocaldococcus jannaschii, Methanopyrus kandleri
brenda
Goldman, A.; Leigh, J.; Samudrala, R.
Comprehensive computational analysis of Hmd enzymes and paralogs in methanogenic Archaea
BMC Evol. Biol.
9
199-210
2009
Methanocaldococcus jannaschii (Q58194)
brenda
Zirngibl, C.; Van Dongen, W.; Schwrer, B.; Von Bnau, R.; Richter, M.; Klein, A.; Thauer, R.K.
H2-forming methylenetetrahydromethanopterin dehydrogenase, a novel type of hydrogenase without iron-sulfur clusters in methanogenic archaea
Eur. J. Biochem.
208
511-520
1992
Methanopyrus kandleri (Q02394), Methanopyrus kandleri, Methanopyrus kandleri DSM 6324 (Q02394), Methanothermobacter marburgensis (P32440), Methanothermobacter marburgensis DSM 2133 (P32440), Methanothermobacter wolfeii (P32441), Methanothermobacter wolfeii, Methanothermobacter wolfeii DSM 2970 (P32441)
brenda