Information on EC 1.5.98.2 - 5,10-methylenetetrahydromethanopterin reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.5.98.2
-
RECOMMENDED NAME
GeneOntology No.
5,10-methylenetetrahydromethanopterin reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-methyltetrahydromethanopterin + oxidized coenzyme F420 = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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-
Methane metabolism
-
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methanogenesis from H2 and CO2
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Microbial metabolism in diverse environments
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reductive acetyl coenzyme A pathway II (autotrophic methanogens)
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methanogenesis from CO2
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
100357-01-5
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyltetrahydromethanopterin + oxidized coenzyme F420
show the reaction diagram
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420
show the reaction diagram
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyltetrahydromethanopterin + oxidized coenzyme F420
show the reaction diagram
-
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
show the reaction diagram
N5,N10-methylenetetrahydromethanopterin + reduced coenzyme F420
5-methyl-5,6,7,8-tetrahydromethanopterin + oxidized coenzyme F420
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coenzyme F420
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-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphate
sulfate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
5,10-methylenetetrahydromethanopterin
pH 6.8, 65°C
0.006 - 0.3
N5,N10-methylenetetrahydromethanopterin
0.003 - 0.004
reduced coenzyme F420
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
275
N5,N10-methylenetetrahydromethanopterin
Methanopyrus kandleri
Q8TXY4
65°C, pH 6.8
275
reduced coenzyme F420
Methanopyrus kandleri
Q8TXY4
65°C, pH 6.8
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01
-
pH 7.5, 65°C, cell extract
0.06
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pH 7.5, 65°C, cell extract
0.4
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pH 7.5, 65°C
1
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pH 7.5, 65°C, cell extract
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Methanosarcina barkeri (strain Fusaro / DSM 804)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
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non denaturing PAGE
36000
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4 * 36000, SDS-PAGE
300000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
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6 * 38000, SDS-PAGE
monomer
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1 * 35000, SDS-PAGE
octamer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
is of less importance
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
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
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