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Information on EC 1.5.98.2 - 5,10-methylenetetrahydromethanopterin reductase
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EC Tree
1.5.98.2 5,10-methylenetetrahydromethanopterin reductaseIUBMB Comments
Catalyses an intermediate step in methanogenesis from CO2 and H2 in methanogenic archaea.
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Word Map
- 1.5.98.2
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methanogenic
- co2
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f420-reducing
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methanobacterium
- thermoautotrophicum
- prostaglandin
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methanogenesis
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prosthetic
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methanopyrus
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abyssal
-
chemoattractant
- kandleri
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eosinophils
- colitis
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hyperthermophile
- barkeri
-
methanosarcina
- reductases
- 5-deazaflavin
- archaebacteria
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
n5,n10-methylenetetrahydromethanopterin reductase, mk0524, 5,10-methylenetetrahydromethanopterin reductase, h2-dependent methylenetetrahydromethanopterin dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5,10-methylene-H4MPT reductase
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coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase
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EC 1.5.99.11
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formerly
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H(2)-dependent methylene-H(4)MPT dehydrogenase
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H(2)-forming N(5),N(10)-methylenetetrahydromethanopterin dehydrogenase
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Hmd
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Hmd and Mtd constitute an alternate pathway for the reduction of F420 with H2 (Hmd-Mtd cycle)
MK0524
MTBMA_c03270
N5,N10-methylenetetrahydromethanopterin reductase
N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent)
N5,N10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase
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N5,N10-methylenetetrahydromethanopterin reductase
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N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent)
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N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent)
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N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent)
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N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent)
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N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent)
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5-methyltetrahydromethanopterin + oxidized coenzyme F420 = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyltetrahydromethanopterin + oxidized coenzyme F420 = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
stereochemistry
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5-methyltetrahydromethanopterin + oxidized coenzyme F420 = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
5-methyltetrahydromethanopterin:coenzyme-F420 oxidoreductase
Catalyses an intermediate step in methanogenesis from CO2 and H2 in methanogenic archaea.
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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-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyltetrahydromethanopterin + oxidized coenzyme F420
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
additional information
?
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-
recombinantly overexpressed Mer is able to use NADPH and methylglyoxal to produce lactaldehyde, reaction of EC 1.1.1.283. Mer does not catalyze the reduction of methylglyoxal to lactaldehyde in the presence of reduced Fo, the precursor of cofactor F420
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5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyltetrahydromethanopterin + oxidized coenzyme F420
the reductase is specific for reduced coenzyme F420 as electron donor. NADH, NADPH or reduced dyes can not substitute for the 5-deazaflavin
-
-
?
5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyltetrahydromethanopterin + oxidized coenzyme F420
the reductase is specific for reduced coenzyme F420 as electron donor. NADH, NADPH or reduced dyes can not substitute for the 5-deazaflavin
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-
?
5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyltetrahydromethanopterin + oxidized coenzyme F420
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-
-
-
?
5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyltetrahydromethanopterin + oxidized coenzyme F420
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the enzyme is involved in methanogenesis from CO2
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-
?
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
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-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
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-
-
-
?
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
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-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
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-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
-
-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
-
-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
-
-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
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-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
-
-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
-
-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
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-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
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-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
-
-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
-
-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
the enzyme is involved in methanogenesis from CO2
-
-
?
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
the enzyme is specific for reduced coenzyme F420. Ternary complex mechanism
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-
?
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
the enzyme is involved in methanogenesis from CO2
-
-
?
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
the enzyme is specific for reduced coenzyme F420. Ternary complex mechanism
-
-
?
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
-
-
-
?
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
the enzyme is involved in methanogenesis from CO2
-
-
?
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
-
-
-
?
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
the enzyme is involved in methanogenesis from CO2
-
-
?
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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-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyltetrahydromethanopterin + oxidized coenzyme F420
-
the enzyme is involved in methanogenesis from CO2
-
-
?
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
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-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
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-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
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-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
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-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
-
-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
-
-
-
r
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
the enzyme is involved in methanogenesis from CO2
-
-
?
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
the enzyme is involved in methanogenesis from CO2
-
-
?
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
the enzyme is involved in methanogenesis from CO2
-
-
?
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
the enzyme is involved in methanogenesis from CO2
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphate
maximal stimulation (100fold) at 2.5 M. Sodium-, potassium-, and ammonium salts of phosphate are equally effective
phosphate
maximal stimulation at 2.5 M. Sodium-, potassium-, and ammonium salts are equally effective
phosphate
maximal stimulation (5-6fold) at 1 M. Sodium-, potassium-, and ammonium salts of phosphate are equally effective
sulfate
maximal stimulation (100fold) at 2.2 M. Sodium-, potassium-, and ammonium salts of sulfate are equally effective
sulfate
maximal stimulation at 2.2 M. Sodium-, potassium-, and ammonium salts are equally effective
sulfate
maximal stimulation (5-6fold) at 1 M. Sodium-, potassium-, and ammonium salts of sulfate are equally effective
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
290
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
physiological function
-
the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
physiological function
-
the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
physiological function
-
the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
physiological function
-
the enzyme is involved in methanogenesis from CO2
physiological function
the enzyme is involved in methanogenesis from CO2
physiological function
the enzyme is involved in methanogenesis from CO2
physiological function
-
the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
-
physiological function
-
the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
-
physiological function
-
the enzyme is involved in methanogenesis from CO2
-
physiological function
-
the enzyme is involved in methanogenesis from CO2
-
physiological function
-
the enzyme is involved in autotrophic CO2 fixation, carbon monoxide dehydrogenase pathway
-
Show AA Sequence and Transmembrane Helices (1292 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
300000
38000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
octamer
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90
90
the enzyme is completely inactivated within a few min when incubated in 100 mM Tris/HCl pH 6.8. The rate of inactivation decreases with increasing potassium phosphate concentrations. At 100 mM potassium phosphate complete thermostability for 60 min is reached
90
-
inactivation after a few min, increased thermostability when salts are added
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
efficiency of salts in protecting the reductase from inactivation decreased in the following order: K2HPO4, KCl, (NH4)2SO4, NH4Cl, Na2HPO4, NaCl
salt concentrations between 0.1 M and 1.5 M are required for maximal stability. Potassium salts are more effective than ammonium salts, and the latter more effective than sodium salts in stabilizing the enzyme activity. The anion
thermostability of the reductase is very low in the absence of salts. In their presence, however, the reductase is highly thermostable. Salt concentrations between 0.1 M and 1.5 M are required for maximal stability. Potassium salts prove more effective than ammonium salts
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
under aerobic conditions at 4°C approximately 20% activity is lost within 24 h. Under anaerobic conditions only 10% activity is lost
726826
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ma, K.; Thauer, R.K.
Purification and properties of N5,N10-methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum (strain Marburg)
Eur. J. Biochem.
191
187-193
1990
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
brenda
te Brommelstroet, B.W.; Geerts, W.J.; Keltjens, J.T.; van der Drift, C.; Vogels, G.D.
Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri
Biochim. Biophys. Acta
1079
293-302
1991
Methanosarcina barkeri
brenda
te Brommelstroet, B.W.; Hensgens, C.M.; Keltjens, J.T.; van der Drift, C.; Vogels, G.D.
Purification and properties of 5,10-methylenetetrahydromethanopterin reductase, a coenzyme F420-dependent enzyme, from Methanobacterium thermoautotrophicum strain delta H
J. Biol. Chem.
265
1852-1857
1990
Methanothermobacter thermautotrophicus
brenda
Rospert, S.; Breitung, J.; Ma, K.; Schwoerer, B.; Zirngibl, C.; Thauer, R.K.; Linder, D.; Huber, R.; Stetter, K.O.
Methyl-coenzyme M reductase and other enzymes involved in methanogenesis from carbon dioxide and hydrogen in the extreme thermophile Methanopyrus kandleri
Arch. Microbiol.
156
49-55
1991
Methanopyrus kandleri
brenda
Kunow, J.; Schwoerer, B.; Setzke, E.; Thauer, R.K.
Si-face stereospecificity at C5 of coenzyme F420 for F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase, F420-dependent N5,N10-methylenetetrahydromethanopterin reductase and F420H2:dimethylnaphthoquinone oxidoreductase
Eur. J. Biochem.
214
641-646
1993
Archaeoglobus fulgidus
brenda
Vaupel, M.; Thauer, R.K.
Coenzyme F420-dependent N5,N10-methylenetetrahydromethanopterin reductase (Mer) from Methanobacterium thermoautotrophicum strain Marburg. Cloning, sequencing, transcriptional analysis, and functional expression in Escherichia coli of the mer gene
Eur. J. Biochem.
231
773-778
1995
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
brenda
Ma, K.; Thauer, R.K.
Single step purification of methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum by specific binding to blue sepharose CL-6B
FEBS Lett.
268
59-62
1990
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
brenda
Nolling, J.; Pihl, T.D.; Reeve, J.N.
Cloning, sequencing, and growth phase-dependent transcription of the coenzyme F420-dependent N5,N10-methylenetetrahydromethanopterin reductase-encoding genes from Methanobacterium thermoautotrophicum delta H and Methanopyrus kandleri
J. Bacteriol.
177
7238-7244
1995
Methanopyrus kandleri
brenda
Shima, S.; Warkentin, E.; Grabarse, W.; Sordel, M.; Wicke, M.; Thauer, R.K.; Ermler, U.
Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin reductase from two methanogenic archaea
J. Mol. Biol.
300
935-950
2000
Methanothermobacter thermautotrophicus, Methanopyrus kandleri
brenda
Hendrickson, E.L.; Leigh, J.A.
Roles of coenzyme F420-reducing hydrogenases and hydrogen- and F420-dependent methylenetetrahydromethanopterin dehydrogenases in reduction of F420 and production of hydrogen during methanogenesis
J. Bacteriol.
190
4818-4821
2008
Methanococcus maripaludis
brenda
Vornolt, J.; Kunow, J.; Stetter, K.; Thauer, R.
Enzymes and coenzymes of the carbon monoxide dehydrogenase pathway for autotrophic CO2 fixation in Archaeoglobus lithotrophicus and the lack of carbon monoxide dehydrogenase in the heterotrophic A. profundus
Arch. Microbiol.
163
112-118
1995
Archaeoglobus fulgidus, Archaeoglobus profundus, Archaeoglobus lithotrophicus, Archaeoglobus lithotrophicus TF-2, Archaeoglobus profundus DSM 5631
-
brenda
Vorholt, J.A.; Hafenbradl, D.; Stetter, K.O.; Thauer, R.K.
Pathways of autotrophic CO2 fixation and of dissimilatory nitrate reduction to N2O in Ferroglobus placidus
Arch. Microbiol.
167
19-23
1997
Ferroglobus placidus, Ferroglobus placidus DSM 10642
brenda
Ma, K.; Linder, D.; Stetter, K.O.; Thauer, R.K.
Purification and properties of N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent) from the extreme thermophile Methanopyrus kandleri
Arch. Microbiol.
155
593-600
1991
Methanosarcina barkeri, Methanothermobacter marburgensis (Q50744), Methanopyrus kandleri (Q8TXY4), Methanopyrus kandleri, Methanopyrus kandleri DSM 6324 (Q8TXY4), Methanothermobacter marburgensis DSM 2133 (Q50744)
brenda
Miller, D.; Ruhlin, M.; Ray, W.; Xu, H.; White, R.
N5,N10-methylenetetrahydromethanopterin reductase from Methanocaldococcus jannaschii also serves as a methylglyoxal reductase
FEBS Lett.
591
2269-2278
2017
Methanocaldococcus jannaschii
brenda
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Release 2023.1 (January 2023)
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