BRENDA - Enzyme Database show
show all sequences of 1.12.98.3

The F420H2 dehydrogenase from Methanosarcina mazei is a Redox-driven proton pump closely related to NADH dehydrogenases

Baumer, S.; Ide, T.; Jacobi, C.; Johann, A.; Gottschalk, G.; Deppenmeier, U.; J. Biol. Chem. 275, 17968-17973 (2000)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Methanosarcina mazei
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
membrane-bound enzyme
Methanosarcina mazei
16020
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
H2 + 2-(2,3-dihydropentaprenyloxy)phenazine
Methanosarcina mazei
coenzyme F420-dependent reduction of 2-hydroxyphenazine as catalyzed by the membrane-bound enzyme is coupled to proton translocation across the cytoplasmic membrane, exhibiting a stoichiometry of 0.9 H+ translocated per two electrons transferred. The electrochemical proton gradient thereby generated drives ATP synthesis from ADP and diphosphate
2-dihydropentaprenyloxyphenazine
-
-
?
H2 + 2-(2,3-dihydropentaprenyloxy)phenazine
Methanosarcina mazei DSM 3647
coenzyme F420-dependent reduction of 2-hydroxyphenazine as catalyzed by the membrane-bound enzyme is coupled to proton translocation across the cytoplasmic membrane, exhibiting a stoichiometry of 0.9 H+ translocated per two electrons transferred. The electrochemical proton gradient thereby generated drives ATP synthesis from ADP and diphosphate
2-dihydropentaprenyloxyphenazine
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanosarcina mazei
Q8PU58 and F1SVL1 and Q8PZ67 and F1SVH7 and F1SVE4 and Q8PU59 and Q8PU60 and Q8PU61 and F1SVE0 and F1SVK0 and F1SVH9 and F1SVL2 and F1SVE1
Q8PU58: subunit A, F1SVL1: subunit C, Q8PZ67: subunit F, F1SVH7: subunit B, F1SVE4: subunit D, Q8PU59: subunit H, Q8PU60: subunit I, Q8PU61: subunit J, F1SVE0: subunit K, F1SVK0; subunit L, F1SVH9: subunit M, F1SVL2: subunit N, F1SVE1: subunit O
-
Methanosarcina mazei DSM 3647
Q8PU58 and F1SVL1 and Q8PZ67 and F1SVH7 and F1SVE4 and Q8PU59 and Q8PU60 and Q8PU61 and F1SVE0 and F1SVK0 and F1SVH9 and F1SVL2 and F1SVE1
Q8PU58: subunit A, F1SVL1: subunit C, Q8PZ67: subunit F, F1SVH7: subunit B, F1SVE4: subunit D, Q8PU59: subunit H, Q8PU60: subunit I, Q8PU61: subunit J, F1SVE0: subunit K, F1SVK0; subunit L, F1SVH9: subunit M, F1SVL2: subunit N, F1SVE1: subunit O
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
H2 + 2-(2,3-dihydropentaprenyloxy)phenazine
coenzyme F420-dependent reduction of 2-hydroxyphenazine as catalyzed by the membrane-bound enzyme is coupled to proton translocation across the cytoplasmic membrane, exhibiting a stoichiometry of 0.9 H+ translocated per two electrons transferred. The electrochemical proton gradient thereby generated drives ATP synthesis from ADP and diphosphate
727829
Methanosarcina mazei
2-dihydropentaprenyloxyphenazine
-
-
-
?
H2 + 2-(2,3-dihydropentaprenyloxy)phenazine
cofactor F420(H2)-dependent reduction of 2-hydroxyphenazine as catalyzed by the membrane-bound enzyme is coupled to proton translocation across the cytoplasmic membrane, exhibiting a stoichiometry of 0.9 H+ translocated per two electrons transferred
727829
Methanosarcina mazei
2-dihydropentaprenyloxyphenazine
-
-
-
?
H2 + 2-(2,3-dihydropentaprenyloxy)phenazine
coenzyme F420-dependent reduction of 2-hydroxyphenazine as catalyzed by the membrane-bound enzyme is coupled to proton translocation across the cytoplasmic membrane, exhibiting a stoichiometry of 0.9 H+ translocated per two electrons transferred. The electrochemical proton gradient thereby generated drives ATP synthesis from ADP and diphosphate
727829
Methanosarcina mazei DSM 3647
2-dihydropentaprenyloxyphenazine
-
-
-
?
H2 + 2-(2,3-dihydropentaprenyloxy)phenazine
cofactor F420(H2)-dependent reduction of 2-hydroxyphenazine as catalyzed by the membrane-bound enzyme is coupled to proton translocation across the cytoplasmic membrane, exhibiting a stoichiometry of 0.9 H+ translocated per two electrons transferred
727829
Methanosarcina mazei DSM 3647
2-dihydropentaprenyloxyphenazine
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
coenzyme F420
the reaction is dependent on the cofactor F420
Methanosarcina mazei
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Methanosarcina mazei
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
coenzyme F420
the reaction is dependent on the cofactor F420
Methanosarcina mazei
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
membrane-bound enzyme
Methanosarcina mazei
16020
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
H2 + 2-(2,3-dihydropentaprenyloxy)phenazine
Methanosarcina mazei
coenzyme F420-dependent reduction of 2-hydroxyphenazine as catalyzed by the membrane-bound enzyme is coupled to proton translocation across the cytoplasmic membrane, exhibiting a stoichiometry of 0.9 H+ translocated per two electrons transferred. The electrochemical proton gradient thereby generated drives ATP synthesis from ADP and diphosphate
2-dihydropentaprenyloxyphenazine
-
-
?
H2 + 2-(2,3-dihydropentaprenyloxy)phenazine
Methanosarcina mazei DSM 3647
coenzyme F420-dependent reduction of 2-hydroxyphenazine as catalyzed by the membrane-bound enzyme is coupled to proton translocation across the cytoplasmic membrane, exhibiting a stoichiometry of 0.9 H+ translocated per two electrons transferred. The electrochemical proton gradient thereby generated drives ATP synthesis from ADP and diphosphate
2-dihydropentaprenyloxyphenazine
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
H2 + 2-(2,3-dihydropentaprenyloxy)phenazine
coenzyme F420-dependent reduction of 2-hydroxyphenazine as catalyzed by the membrane-bound enzyme is coupled to proton translocation across the cytoplasmic membrane, exhibiting a stoichiometry of 0.9 H+ translocated per two electrons transferred. The electrochemical proton gradient thereby generated drives ATP synthesis from ADP and diphosphate
727829
Methanosarcina mazei
2-dihydropentaprenyloxyphenazine
-
-
-
?
H2 + 2-(2,3-dihydropentaprenyloxy)phenazine
cofactor F420(H2)-dependent reduction of 2-hydroxyphenazine as catalyzed by the membrane-bound enzyme is coupled to proton translocation across the cytoplasmic membrane, exhibiting a stoichiometry of 0.9 H+ translocated per two electrons transferred
727829
Methanosarcina mazei
2-dihydropentaprenyloxyphenazine
-
-
-
?
H2 + 2-(2,3-dihydropentaprenyloxy)phenazine
coenzyme F420-dependent reduction of 2-hydroxyphenazine as catalyzed by the membrane-bound enzyme is coupled to proton translocation across the cytoplasmic membrane, exhibiting a stoichiometry of 0.9 H+ translocated per two electrons transferred. The electrochemical proton gradient thereby generated drives ATP synthesis from ADP and diphosphate
727829
Methanosarcina mazei DSM 3647
2-dihydropentaprenyloxyphenazine
-
-
-
?
H2 + 2-(2,3-dihydropentaprenyloxy)phenazine
cofactor F420(H2)-dependent reduction of 2-hydroxyphenazine as catalyzed by the membrane-bound enzyme is coupled to proton translocation across the cytoplasmic membrane, exhibiting a stoichiometry of 0.9 H+ translocated per two electrons transferred
727829
Methanosarcina mazei DSM 3647
2-dihydropentaprenyloxyphenazine
-
-
-
?
General Information
General Information
Commentary
Organism
physiological function
the enzyme is part of the energy conserving electron transport system of the methanogenic archaeon Methanosarcina mazei Gö1
Methanosarcina mazei
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the enzyme is part of the energy conserving electron transport system of the methanogenic archaeon Methanosarcina mazei Gö1
Methanosarcina mazei
Other publictions for EC 1.12.98.3
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
741956
Welte
Bioenergetics and anaerobic r ...
Methanosarcina mazei
Biochim. Biophys. Acta
1837
1130-1147
2014
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4
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1
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3
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3
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1
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704289
Guss
Differences in hydrogenase gen ...
Methanosarcina acetivorans, Methanosarcina barkeri
J. Bacteriol.
191
2826-2833
2009
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2
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2
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440302
Beifuss
Methanophenazine: structure, t ...
Methanosarcina sp.
Angew. Chem.
39
2470-2472
2000
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1
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727829
Baumer
The F420H2 dehydrogenase from ...
Methanosarcina mazei, Methanosarcina mazei DSM 3647
J. Biol. Chem.
275
17968-17973
2000
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1
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1
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439643
Meuer
Purification and catalytic pro ...
Methanosarcina barkeri
Eur. J. Biochem.
265
325-335
1999
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2
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1
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1
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440300
Deppenmeier
Novel reactions involved in en ...
Methanosarcina barkeri, Methanosarcina mazei
FEBS Lett.
457
291-297
1999
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4
2
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5
2
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2
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440299
Abken
Isolation and characterization ...
Methanosarcina mazei
J. Bacteriol.
180
2027-2032
1998
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1
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440297
Arnikar
-
Effect of gamma-radiation on M ...
Methanosarcina sp.
J. Radioanal. Nucl. Chem.
142
349-358
1990
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4
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1
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1
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440298
Bhosale
-
Distribution of transition met ...
Methanosarcina sp.
FEMS Microbiol. Lett.
70
241-247
1990
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