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Information on EC 1.12.98.2 - 5,10-methenyltetrahydromethanopterin hydrogenase
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1.12.98.2 5,10-methenyltetrahydromethanopterin hydrogenaseIUBMB 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.
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Word Map
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
Reaction Schemes
Synonyms
h2-forming methylenetetrahydromethanopterin dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5,10-methylene-H4MPT dehydrogenase
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Dehydrogenase, methylenetetrahydromethanopterin
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EC 1.12.99.4
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formerly
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H2-forming methylenetetrahydromethanopterin dehydrogenase
H2-forming N5,N10-Methenyltetrahydromethanopterin dehydrogenase
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Hmd
methylenetetrahydromethanopterin dehydrogenase
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N5,N10-methenyltetrahydromethanopterin hydrogenase
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N5,N10-Methylenetetrahydromethanopterin dehydrogenase
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N5,N10-methylenetetrahydromethanopterin dehydrogenase (H2-forming)
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H2-forming methylenetetrahydromethanopterin dehydrogenase
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H2-forming methylenetetrahydromethanopterin dehydrogenase
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H2-forming methylenetetrahydromethanopterin dehydrogenase
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Hmd
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
H2 + 5,10-methenyltetrahydromethanopterin = H+ + 5,10-methylenetetrahydromethanopterin
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H2 + 5,10-methenyltetrahydromethanopterin = H+ + 5,10-methylenetetrahydromethanopterin
mechanism
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H2 + 5,10-methenyltetrahydromethanopterin = H+ + 5,10-methylenetetrahydromethanopterin
stereoselective hydride transfer
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H2 + 5,10-methenyltetrahydromethanopterin = H+ + 5,10-methylenetetrahydromethanopterin
mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
hydrogen:5,10-methenyltetrahydromethanopterin oxidoreductase
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.
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CAS REGISTRY NUMBER
COMMENTARY
100357-01-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
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r
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
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involved in methanogenesis
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r
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
Hmd catalyzes a step in the hydrogenotrophic methanogenesis pathway in class I methanogens
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?
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
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r
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
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involved in methanogenesis
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r
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
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reverse reaction under argon atmosphere
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r
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
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?
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
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involved in methanogenesis
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?
H+ + 5,10-methylenetetrahydromethanopterin
H2 + 5,10-methenyltetrahydromethanopterin
the purified enzyme does not catalyze the reduction of viologen dyes, of methylene blue, of flavins, of pyridine nucleotides
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r
H+ + 5,10-methylenetetrahydromethanopterin
H2 + 5,10-methenyltetrahydromethanopterin
the purified enzyme does not catalyze the reduction of viologen dyes, of methylene blue, of flavins, of pyridine nucleotides
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r
H+ + 5,10-methylenetetrahydromethanopterin
H2 + 5,10-methenyltetrahydromethanopterin
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r
H+ + 5,10-methylenetetrahydromethanopterin
H2 + 5,10-methenyltetrahydromethanopterin
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r
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
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r
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?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
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no reaction with: coenzyme F420, NAD+, NADP+
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?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
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reverse reaction is favoured under alkaline conditions
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?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
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?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
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r
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?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
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no reaction with: coenzyme F420, NAD+, NADP+
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?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
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no reaction with viologen dyes
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?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
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r
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?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
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?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
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r
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?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
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no reaction with: coenzyme F420, NAD+, NADP+
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?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
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no reaction with viologen dyes
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?
N5,N10-methylenetetrahydromethanopterin + H+
N5,N10-methenyltetrahydromethanopterin + H2
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r
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?
additional information
?
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no reduction of methyl viologen or methyl blue
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?
additional information
?
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the enzyme is involved in methanogenesis from CO2 and H2
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?
additional information
?
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no reduction of methyl viologen or methyl blue
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?
additional information
?
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no reduction of viologen dyes in the presence of H2
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?
additional information
?
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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
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
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involved in methanogenesis
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r
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
Hmd catalyzes a step in the hydrogenotrophic methanogenesis pathway in class I methanogens
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?
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
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involved in methanogenesis
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r
5,10-methenyltetrahydromethanopterin + H2
5,10-methylenetetrahydromethanopterin + H+
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involved in methanogenesis
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?
additional information
?
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the enzyme is involved in methanogenesis from CO2 and H2
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?
additional information
?
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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
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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enzyme contains iron bound to a cofactor of unknown structure
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additional information
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enzyme contains iron bound to a mercaptoethanol-extractable cofactor of unknown structure
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additional information
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enzyme contains iron bound to a mercaptoethanol-extractable cofactor of unknown structure, contains intrinsic CO bound to iron
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additional information
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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
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additional information
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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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
Iron
KCl
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the enzyme requires the presence of salts, 50% of maximal activity is reached at 100 mM potassium phosphate, KCl or NaCl
NaCl
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the enzyme requires the presence of salts, 50% of maximal activity is reached at 100 mM potassium phosphate, KCl or NaCl
Nickel
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contains less than 0.1 mol Ni per mol of enzyme
potassium phosphate
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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
additional information
Fe
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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
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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
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enzyme contains iron bound to a cofactor of unknown structure, one iron per monomer, iron is released from cofactor upon light inactivation
Iron
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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
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enzyme contains iron bound to an mercaptoethanol-extractable cofactor of unknown structure, contains intrinsic CO bound to iron
Iron
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contains approximately 1 mol of iron per mol of enzyme
additional information
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lack of redoxactive transition metals
additional information
the enzyme does not contain iron-sulfur clusters, nickel, or flavins
additional information
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the enzyme does not contain nickel or iron/sulfur clusters
additional information
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the enzyme does not contain nickel or iron/sulfur clusters
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
H2
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inhibits formation of N5,N10-methenyltetrahydromethanopterin
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
5,10-methenyltetrahydromethanopterin
pH 7.5, 60°C
0.07
5,10-methenyltetrahydromethanopterin
pH and temperature not specified in the publication
0.02
5,10-methylenetetrahydromethanopterin
pH and temperature not specified in the publication
0.04
5,10-methylenetetrahydromethanopterin
pH 6.5, 60°C
0.02
N5,N10-methylenetetrahydromethanopterin
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additional information
H2
the apparent Km for H2 is estimated to be approximately 60% H2 in the gas phase
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
975
5,10-methenyltetrahydromethanopterin
pH 7.5, 60°C
1462
5,10-methylenetetrahydromethanopterin
pH 6.5, 60°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
CN-
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pH 6.0, 40°C, under N2, substrate concentration of 0.003 mM
0.2
CN-
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pH 6.0, 40°C, under N2, substrate concentration of 0.01 mM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 7
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reaction rate increases hyperbolically with the proton concentration between pH 7 and pH 4.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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brenda
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brenda
formerly Methanobacterium thermoautotrophicum, strains deltaH and TM, two different isoforms of enzyme, first isoform in early and middle stages of cultivation and is F420 dependent (mtd-isoform), second isoform in late stages of cultivation is H2-dependent (mth-isoform)
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brenda
Show AA Sequence and Transmembrane Helices (148 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37992
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4 * 37992, calculation from nucleotide sequence
38000
38038
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4 * 38038, MALDI-TOF-MS analysis of peptides obtained by BrCN cleavage
43000
38000
the Hmd holoenzyme is comprised of a homodimer of 38 kDa subunits, 2 pyridone derivative cofactor molecules and 2 iron atoms
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
tetramer
homodimer
2 * 38000, structural modeling of Hmd enzyme reveals a common structural arrangement comprised of one large N-terminal domain containing alpha-helices and beta-sheets and one smaller C-terminal domain containing only alpha-helices
tetramer
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4 * 37992, calculation from nucleotide sequence
tetramer
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4 * 38038, MALDI-TOF-MS analysis of peptides obtained by BrCN cleavage
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop or sitting-drop, vapour diffusion method. Crystal structure of the Hmd apoenzyme from Methanocaldococcus jannaschii at 1.75 A resolution
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hanging-drop or sitting-drop, vapour diffusion method. Crystal structure of the Hmd apoenzyme from Methanocaldococcus jannaschii at 2.4 A resolution
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to UV-A/blue light, CO protects from inactivation
the rate of inactivation increases upon dilution and in the presence of O2 and decreases upon the addition of 5 mg/ml albumin
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sensitive to UV-A/blue light, CO protects from inactivation
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme is very labile even under strictly anoxic conditions
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394696
rapidly inactivated in the presence of molecular oxygen. The rate of inactivation increases in the presence of dithiothreitol (2 mM) or of mercaptoethanol (5 mM)
727402
the enzyme is much more sensitive towards inactivation by O2 than the enzyme from Methanothermobacter marburgensis
727402
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, pH 7.6, 50 mM Tris-HCl, 20% glycerol, under N2 gas phase, 50% loss of activity after 1 week
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