Information on EC 1.1.98.4 - F420H2:quinone oxidoreductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.98.4
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RECOMMENDED NAME
GeneOntology No.
F420H2:quinone oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a quinol + oxidized coenzyme F420 = a quinone + reduced coenzyme F420
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
methanogenesis from CO2
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SYSTEMATIC NAME
IUBMB Comments
quinol:coenzyme-F420 oxidoreductase
An enzyme complex that contains FAD and iron-sulfur clusters. The enzyme has been described in the archaea Methanosarcina mazei and Archaeoglobus fulgidus.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
1,4-naphthoquinone + reduced coenzyme F420
1,4-naphthoquinol + oxidized coenzyme F420
show the reaction diagram
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-
-
-
?
2,3-dimethoxy-5-methyl-1,4-benzoquinone + reduced coenzyme F420
2,3-dimethoxy-5-methyl-1,4-benzoquinol + oxidized coenzyme F420
show the reaction diagram
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-
-
-
?
2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone + reduced coenzyme F420
2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol + oxidized coenzyme F420
show the reaction diagram
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-
-
-
?
2,3-dimethyl-1,4-naphthoquinone + reduced coenzyme F420
2,3-dimethyl-1,4-naphthoquinol + oxidized coenzyme F420
show the reaction diagram
2-hydroxy-1,4-naphthoquinone + reduced coenzyme F420
2-hydroxy-1,4-naphthoquinol + oxidized coenzyme F420
show the reaction diagram
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-
-
-
?
2-methyl-1,4-naphthoquinone + reduced coenzyme F420
2-methyl-1,4-naphthoquinol + oxidized coenzyme F420
show the reaction diagram
menaquinone + reduced coenzyme F420
menaquinol + oxidized coenzyme F420
show the reaction diagram
oxidized methyl viologen + reduced coenzyme F420
reduced methyl viologen + oxidized coenzyme F420
show the reaction diagram
the purified subunit oxidizes reduced cofactor F420 using the electron-acceptor system methyl viologen plus metronidazole
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-
?
tetramethyl-4-benzoquinone + reduced coenzyme F420
tetramethyl-1,4-benzoquinol + oxidized coenzyme F420
show the reaction diagram
additional information
?
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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
menaquinone + reduced coenzyme F420
menaquinol + oxidized coenzyme F420
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron-sulfur cluster
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19
2,3-dimethyl-1,4-naphthoquinone
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pH 8.0, 65°C
0.007 - 0.05
reduced coenzyme F420
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.21
pH 7, 22°C, crude extract, electron-acceptor system consisting of metronidazole and methyl viologen
9.3
pH 7, 22°C, purified enzyme, electron-acceptor system consisting of metronidazole and methyl viologen
17
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activity with reduced coenzyme F420 as electron donor and methylviologen and metronidazole as electron acceptors at pH 8.5 at a temperature of 39°C
68
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activity with reduced coenzyme F420 as electron donor and tetramethyl-4-benzoquinone as electron acceptors at pH 8.5 at a temperature of 39°C
136
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activity with reduced coenzyme F420 as electron donor and 2,3-dimethyl-1,4-naphthoquinone as electron acceptors at pH 8.5 at a temperature of 39°C
173
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activity with reduced coenzyme F420 as electron donor and 2-methyl-1,4-naphthoquinone as electron acceptors at pH 8.5 at a temperature of 39°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 80
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20°C: about 40% of maximal activity, 80°C: about 55% of maximal activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16000
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x * 40000 + x * 37000 + x * 22000 + x * 20000 x * 16000, SDS-PAGE
20000
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x * 40000 + x * 37000 + x * 22000 + x * 20000 x * 16000, SDS-PAGE
22000
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x * 40000 + x * 37000 + x * 22000 + x * 20000 x * 16000, SDS-PAGE
32000
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x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides
33000
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x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides
40000
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x * 40000 + x * 37000 + x * 22000 + x * 20000 x * 16000, SDS-PAGE
41000
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x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides
45000
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x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides
56000
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x * 56000, x * 45000, x * 41000, x * 39000, x * 37000, x * 33000, x * 32000, SDS-PAGE reveals the presence of at least seven polypeptides
115000
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gel filtration
270000
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gel filtration, native PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
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1 h, stable in presence of 1 M (NH4)2SO4, in the presence of 1 M K2HPO (pH 8) only 60% activity is recovered
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme activity is almost stable in aerobic solutions. No activity is lost when 2 mg purified protein in 1 ml 50 mM Tricine/KOH, pH 7.5, containing 0.2% dodecyl-/I-D-maltoside is stored at 4°C for 6 h under air as the gas phase
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722162
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichia coli