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Information on EC 1.2.7.12 - formylmethanofuran dehydrogenase
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1.2.7.12 formylmethanofuran dehydrogenaseIUBMB Comments
Contains a molybdopterin cofactor and numerous [4Fe-4S] clusters. In some organisms an additional subunit enables the incorporation of tungsten when molybdenum availability is low. The enzyme catalyses a reversible reaction in methanogenic archaea, and is involved in methanogenesis from CO2 as well as the oxidation of coenzyme M to CO2. The reaction is endergonic, and is driven by coupling with the soluble CoB-CoM heterodisulfide reductase via electron bifurcation.
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Word Map
- 1.2.7.12
-
methanogen
-
methanogenesis
-
methanobacterium
- thermoautotrophicum
- methanosarcina
- molybdopterin
- barkeri
-
heterodisulfide
-
formyltransferase
- methanothermobacter
-
tungsten-containing
- wolfei
-
molybdenum-containing
-
formylmethanofuran:tetrahydromethanopterin
-
molybdoenzyme
-
hydrogenotrophic
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
+
+
2
=
+
+
2
+
2
+
+
2
oxidized ferredoxin [iron-sulfur] cluster
=
+
+
2
reduced ferredoxin [iron-sulfur] cluster
+
2
Synonyms
formylmethanofuran dehydrogenase, formyl-methanofuran dehydrogenase, pf02663, formyl-mfr dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Dehydrogenase, formylmethanofuran
-
-
-
-
EC 1.2.99.5
-
-
formerly
-
Fmd
FmdE
formyl-methanofuran dehydrogenase
formyl-MFR dehydrogenase
Fwd
FwdA-DFGH/FwdAFmdBCE
PF02663
Fmd
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a formylmethanofuran + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster = CO2 + a methanofuran + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
a formylmethanofuran + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster = CO2 + a methanofuran + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
the enzyme catalyzes a methanofuran-dependent exchange between CO2 and the formyl group of formylmethanofuran, N-carboxymethanofuran is an intermediate in CO2 reduction to formylmethanofuran
-
a formylmethanofuran + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster = CO2 + a methanofuran + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
bioenergetics, reaction is driven by the import of two to four sodium ions
-
a formylmethanofuran + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster = CO2 + a methanofuran + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
reaction step catalyzed by enzyme is not energy-driven
-
a formylmethanofuran + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster = CO2 + a methanofuran + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
formylmethanofuran:ferredoxin oxidoreductase
Contains a molybdopterin cofactor and numerous [4Fe-4S] clusters. In some organisms an additional subunit enables the incorporation of tungsten when molybdenum availability is low. The enzyme catalyses a reversible reaction in methanogenic archaea, and is involved in methanogenesis from CO2 as well as the oxidation of coenzyme M to CO2. The reaction is endergonic, and is driven by coupling with the soluble CoB-CoM heterodisulfide reductase via electron bifurcation.
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CAS REGISTRY NUMBER
COMMENTARY
119940-12-4
-
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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
CO2 + methanofuran + reduced acceptor
formylmethanofuran + H2O + acceptor
-
-
-
-
?
formylmethanofuran + H2O + ferredoxin
CO2 + methanofuran + reduced ferredoxin
-
-
-
-
?
formylmethanofuran + H2O + oxidized carbamoylviologen
CO2 + methanofuran + reduced carbamoylviologen
-
-
-
-
r
formylmethanofuran + H2O + oxidized ferredoxin
CO2 + methanofuran + reduced ferredoxin
-
-
-
-
r
formylmethanofuran + H2O + oxidized ferredoxin [iron-sulfur] cluster
CO2 + methanofuran + reduced ferredoxin [iron-sulfur] cluster
formylmethanofuran + H2O + oxidized methyl viologen
CO2 + methanofuran + reduced methyl viologen + H+
-
-
-
-
r
formylmethanofuran + oxidized 1,1',2,2'-tetramethylviologen
CO2 + methanofuran + reduced 1,1',2,2'-tetramethylviologen
formylmethanofuran + oxidized acceptor
?
-
formation of formylmethanofuran, which is an intermediate in methanogenesis from CO2
-
-
?
formylmethanofuran + oxidized benzylviologen + H2O
methanofuran + reduced benzylviologen + CO2
formylmethanofuran + oxidized carbamoylmethylviologen + H2O
methanofuran + reduced carbamoylmethylviologen + CO2
-
-
-
?
formylmethanofuran + oxidized methylviologen + H2O
methanofuran + reduced methylviologen + CO2
CO2 + methanofuran + reduced ferredoxin
formylmethanofuran + H2O + oxidized ferredoxin
-
-
-
-
?
CO2 + methanofuran + reduced ferredoxin
formylmethanofuran + H2O + oxidized ferredoxin
-
-
-
-
?
Formamide + oxidized acceptor
?
-
molybdenum enzyme, 0.1% of the activity relative to formylmethanofuran
-
-
?
Formate + oxidized acceptor
?
-
molybdenum enzyme, 1% of the activity relative to formylmethanofuran
-
-
?
Formate + oxidized acceptor
?
-
molybdenum enzyme, 3% of the activity relative to formylmethanofuran
-
-
?
formylmethanofuran + H2O + oxidized ferredoxin [iron-sulfur] cluster
CO2 + methanofuran + reduced ferredoxin [iron-sulfur] cluster
-
-
-
-
?
formylmethanofuran + H2O + oxidized ferredoxin [iron-sulfur] cluster
CO2 + methanofuran + reduced ferredoxin [iron-sulfur] cluster
-
-
-
-
?
formylmethanofuran + oxidized 1,1',2,2'-tetramethylviologen
CO2 + methanofuran + reduced 1,1',2,2'-tetramethylviologen
-
-
-
-
?
formylmethanofuran + oxidized 1,1',2,2'-tetramethylviologen
CO2 + methanofuran + reduced 1,1',2,2'-tetramethylviologen
-
-
-
-
?
formylmethanofuran + oxidized 1,1',2,2'-tetramethylviologen
CO2 + methanofuran + reduced 1,1',2,2'-tetramethylviologen
-
r
-
?
formylmethanofuran + oxidized 1,1',2,2'-tetramethylviologen
CO2 + methanofuran + reduced 1,1',2,2'-tetramethylviologen
-
tungsten enzymes are specific for N-formylmethanofuran
-
-
?
formylmethanofuran + oxidized 1,1',2,2'-tetramethylviologen
CO2 + methanofuran + reduced 1,1',2,2'-tetramethylviologen
-
molybdenum enzyme is specific for N-formylmethanofuran
-
-
?
formylmethanofuran + oxidized 1,1',2,2'-tetramethylviologen
CO2 + methanofuran + reduced 1,1',2,2'-tetramethylviologen
-
-
-
-
?
formylmethanofuran + oxidized 1,1',2,2'-tetramethylviologen
CO2 + methanofuran + reduced 1,1',2,2'-tetramethylviologen
-
tungsten enzymes are specific for N-formylmethanofuran
-
-
?
formylmethanofuran + oxidized benzylviologen + H2O
methanofuran + reduced benzylviologen + CO2
-
r
-
-
?
formylmethanofuran + oxidized benzylviologen + H2O
methanofuran + reduced benzylviologen + CO2
-
-
-
?
formylmethanofuran + oxidized benzylviologen + H2O
methanofuran + reduced benzylviologen + CO2
-
-
-
-
?
formylmethanofuran + oxidized methylviologen + H2O
methanofuran + reduced methylviologen + CO2
-
-
-
-
?
formylmethanofuran + oxidized methylviologen + H2O
methanofuran + reduced methylviologen + CO2
-
-
-
?
formylmethanofuran + oxidized methylviologen + H2O
methanofuran + reduced methylviologen + CO2
-
-
-
-
?
formylmethanofuran + oxidized methylviologen + H2O
methanofuran + reduced methylviologen + CO2
-
-
-
-
?
formylmethanofuran + oxidized methylviologen + H2O
methanofuran + reduced methylviologen + CO2
-
-
-
-
?
N-Furfurylformamide + oxidized acceptor
?
-
molybdenum enzyme, 11% of the activity relative to formylmethanofuran
-
-
?
N-Furfurylformamide + oxidized acceptor
?
-
-
-
-
?
N-Furfurylformamide + oxidized acceptor
?
-
molybdenum enzyme, 1% of the activity relative to formylmethanofuran
-
-
?
N-Methylformamide + oxidized acceptor
?
-
molybdenum enzyme, 0.2% of the activity relative to formylmethanofuran
-
-
?
additional information
?
-
-
during growth on medium supplemented with selenium only the isoenzyme with selenocysteine at the active site is transcribed. In selenium-deprived medium two tungsten-containing isoenzymes are transcribed
-
-
?
additional information
?
-
-
no activity with coenzyme F420 as electron acceptor
-
-
?
additional information
?
-
-
enzyme is involved in methanogenesis
-
-
?
additional information
?
-
-
no reduction of metronidazole, methylene blue, FAD or coenzyme F420 with formylmethanofuran
-
-
?
additional information
?
-
-
initial step of methanogenesis
-
-
?
additional information
?
-
-
the tungsten-containing isoenzyme is constitutively transcribed, the transcription of the molybdenum operon is induced by molybdate
-
-
?
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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
CO2 + methanofuran + reduced acceptor
formylmethanofuran + H2O + acceptor
-
-
-
-
?
formylmethanofuran + H2O + ferredoxin
CO2 + methanofuran + reduced ferredoxin
-
-
-
-
?
formylmethanofuran + H2O + oxidized ferredoxin
CO2 + methanofuran + reduced ferredoxin
-
-
-
-
r
formylmethanofuran + H2O + oxidized ferredoxin [iron-sulfur] cluster
CO2 + methanofuran + reduced ferredoxin [iron-sulfur] cluster
formylmethanofuran + oxidized acceptor
?
-
formation of formylmethanofuran, which is an intermediate in methanogenesis from CO2
-
-
?
CO2 + methanofuran + reduced ferredoxin
formylmethanofuran + H2O + oxidized ferredoxin
-
-
-
-
?
CO2 + methanofuran + reduced ferredoxin
formylmethanofuran + H2O + oxidized ferredoxin
-
-
-
-
?
formylmethanofuran + H2O + oxidized ferredoxin [iron-sulfur] cluster
CO2 + methanofuran + reduced ferredoxin [iron-sulfur] cluster
-
-
-
-
?
formylmethanofuran + H2O + oxidized ferredoxin [iron-sulfur] cluster
CO2 + methanofuran + reduced ferredoxin [iron-sulfur] cluster
-
-
-
-
?
additional information
?
-
-
during growth on medium supplemented with selenium only the isoenzyme with selenocysteine at the active site is transcribed. In selenium-deprived medium two tungsten-containing isoenzymes are transcribed
-
-
?
additional information
?
-
-
enzyme is involved in methanogenesis
-
-
?
additional information
?
-
-
initial step of methanogenesis
-
-
?
additional information
?
-
-
the tungsten-containing isoenzyme is constitutively transcribed, the transcription of the molybdenum operon is induced by molybdate
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pterin
-
contains 0.5-0.7 mol of a pterin cofactor of MW 800000 per mol of enzyme, contains di(carboxamidomethyl)-derivatives of molybdopterin guanine dinucleotide, of molybdopterin adenine dinucleotide and of molybdopterin hypoxanthine dinucleotide in the ratio 1.0:1.0:0.1
pterin
-
contains molybdopterin guanine dinucleotide as pterin cofactor
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Molybdenum
Tungsten
Zn2+
Iron
-
contains approximately 30 mol non-heme iron per mol and 30 mol acid-labile sulfur per mol. Subunit F contains 4 tandemly repeated bacterial-ferredoxin-like domains and is predicted to be a polyferredoxin that contains 32 iron atoms in eight [4Fe-4S] clusters
Iron
-
contains 28 mol of non-heme iron and acid labile sulfur per mol of 220000 MW enzyme
Iron
-
contains 4 mol of non-heme iron and 4 mol of acid-labile sulfur per mol of enzyme
Iron
-
contains 8 mol of non-heme iron and 8 mol of acid-labile sulfur per mol of enzyme
Iron
-
the molybdenum isoenzyme contains 6.6 mol non-heme iron per mol of the 146000 MW protein
Molybdenum
-
enzyme exists as molybdenum iron-sulfur protein or as tungsten iron-sulfur protein
Molybdenum
-
contains 0.6-0.8 mol of molybdenum per mol of 200000 MW enzyme
Molybdenum
-
contains 0.5-0.8 mol of molybdenum per mol of 220000 MW enzyme
Molybdenum
-
contains 0.3-0.6 mol of molybdenum per mol of enzyme
Molybdenum
-
a molybdenum-containing isoenzyme and a tungsten-containing isoenzyme
Molybdenum
-
enzyme exists as molybdenum iron-sulfur protein or as tungsten iron-sulfur protein
Molybdenum
-
the molybdenum enzyme also contains tungsten when the archaeon is grown on molybdenum-deprived medium supplemented with tungstate. The tungsten-substituted molybdenum enzyme is catalytically active
Molybdenum
-
enzyme exists as molybdenum iron-sulfur protein or as tungsten iron-sulfur protein
Molybdenum
-
enzyme exists as a molybdenum containing isoenzyme and as a tungsten containing isoenzyme
Molybdenum
-
molybdenum isoenzyme contains approximately 0.23 mol molybdenum and 0.46 mol molybdopterin guanine dinucleotide per mol of the 146000 MW protein
Tungsten
-
contains two tungsten-containing isoenzymes: one isoenzyme with selenocysteine at the active site and the other with Cys at the active site
Tungsten
-
a molybdenum-containing isoenzyme and a tungsten-containing isoenzyme
Tungsten
-
enzyme exists as molybdenum iron-sulfur protein or as tungsten iron-sulfur protein
Tungsten
-
enzyme exists as a molybdenum-containing isoenzyme and a tungsten-containing isoenzyme
Tungsten
-
tungsten-containing isoenzyme: contains 0.4 mol of tungsten per mol of enzyme
Tungsten
-
the molybdenum enzyme also contains tungsten when the archaeon is grown on molybdenum-deprived medium supplemented with tungstate. The tungsten-substituted molybdenum enzyme is catalytically active
Tungsten
-
enzyme exists as molybdenum iron-sulfur protein or as tungsten iron-sulfur protein
Tungsten
-
enzyme exists as a molybdenum-containing isoenzyme and a tungsten-containing isoenzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CN-
-
molybdenum-containing enzymes are inactivated, tungsten-containing isoenzymes are not inactivated
CN-
-
molybdenum-containing enzymes are inactivated, tungsten-containing isoenzymes are not inactivated
CN-
-
molybdenum-containing enzymes are inactivated, tungsten-containing isoenzymes are not inactivated
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.037
methylviologen
-
methylviologen, tungsten-substituted molybdenum enzyme and non-substituted molybdenum enzyme
0.013
N-formylmethanofuran
-
formylmethanofuran, tungsten-substituted molybdenum enzyme and non-substituted molybdenum enzyme
0.02
N-formylmethanofuran
-
value below, methylviologen, molybdenum enzyme
0.03
N-formylmethanofuran
-
-
0.03
N-formylmethanofuran
-
methylviologen, tungsten-substituted molybdenum enzyme
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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
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7.5
-
no activity below pH 6.5, maximal activity above pH 7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
70
70
-
tungsten-substituted molybdenum enzyme and non-substituted molybdenum enzyme
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 70
-
25°C: less than 5% of maximal activity, 60°C: about 90% of maximal activity, 70°C: maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
contains two tungsten isoenzymes and probably no molybdenum enzyme
-
-
brenda
-
-
-
brenda
a molybdenum-containing isoenzyme and a tungsten-containing isoenzyme
-
-
brenda
a molybdenum-containing isoenzyme and a tungsten-containing isoenzyme
-
-
brenda
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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
-
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
-
isoform Fwd1 is important but not indispensable for CO-dependent growth of Methanosarcina acetivorans
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
-
Show AA Sequence and Transmembrane Helices (2393 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14000
-
6 different types of subunits, x * 65100, subunit FmdA, + x * 31600, subunit FmdC, + x * 22800, subunit FmdE, + x * 14000, subunit FmdD, + x * ? + x * ?, calculation from nucleotide sequence
15000
-
1 * 65000 + 1 * 53000 + 1 * 31000 + 1 * 15000, SDS-PAGE
17000
-
x * 65000 + x * 50000 + x * 37000 + x * 34000 + x * 29000 + x * 17000, SDS-PAGE
22800
-
6 different types of subunits, x * 65100, subunit FmdA, + x * 31600, subunit FmdC, + x * 22800, subunit FmdE, + x * 14000, subunit FmdD, + x * ? + x * ?, calculation from nucleotide sequence
29000
-
x * 65000 + x * 50000 + x * 37000 + x * 34000 + x * 29000 + x * 17000, SDS-PAGE
31000
31600
-
6 different types of subunits, x * 65100, subunit FmdA, + x * 31600, subunit FmdC, + x * 22800, subunit FmdE, + x * 14000, subunit FmdD, + x * ? + x * ?, calculation from nucleotide sequence
34000
-
x * 65000 + x * 50000 + x * 37000 + x * 34000 + x * 29000 + x * 17000, SDS-PAGE
37000
-
x * 65000 + x * 50000 + x * 37000 + x * 34000 + x * 29000 + x * 17000, SDS-PAGE
50000
-
x * 65000 + x * 50000 + x * 37000 + x * 34000 + x * 29000 + x * 17000, SDS-PAGE
51000
53000
-
1 * 65000 + 1 * 53000 + 1 * 31000 + 1 * 15000, SDS-PAGE
64000
65000
65100
-
6 different types of subunits, x * 65100, subunit FmdA, + x * 31600, subunit FmdC, + x * 22800, subunit FmdE, + x * 14000, subunit FmdD, + x * ? + x * ?, calculation from nucleotide sequence
31000
-
or hexamer, 1 or 2 * 64000 + 1 or 2 * 51000 + 1 or 2 * 31000, SDS-PAGE
31000
-
1 * 65000 + 1 * 53000 + 1 * 31000 + 1 * 15000, SDS-PAGE
31000
-
or trimer, 1 or 2 * 64000 + 1 or 2 * 51000 + 1 or 2 * 31000, SDs-PAGE
51000
-
or hexamer, 1 or 2 * 64000 + 1 or 2 * 51000 + 1 or 2 * 31000, SDS-PAGE
51000
-
or trimer, 1 or 2 * 64000 + 1 or 2 * 51000 + 1 or 2 * 31000, SDs-PAGE
64000
-
or hexamer, 1 or 2 * 64000 + 1 or 2 * 51000 + 1 or 2 * 31000, SDS-PAGE
64000
-
or trimer, 1 or 2 * 64000 + 1 or 2 * 51000 + 1 or 2 * 31000, SDs-PAGE
65000
-
1 * 65000 + 1 * 53000 + 1 * 31000 + 1 * 15000, SDS-PAGE
65000
-
x * 65000 + x * 50000 + x * 37000 + x * 34000 + x * 29000 + x * 17000, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
-
or trimer, 1 or 2 * 64000 + 1 or 2 * 51000 + 1 or 2 * 31000, SDs-PAGE
tetramer
trimer
-
or hexamer, 1 or 2 * 64000 + 1 or 2 * 51000 + 1 or 2 * 31000, SDS-PAGE
?
-
6 different polypeptides are detected by SDS-PAGE: MW 64000, MW 52000, MW 43000, MW 32000, MW 28000 and MW 14000
?
-
x * 65000 + x * 50000 + x * 37000 + x * 34000 + x * 29000 + x * 17000, SDS-PAGE
?
-
6 different types of subunits, x * 65100, subunit FmdA, + x * 31600, subunit FmdC, + x * 22800, subunit FmdE, + x * 14000, subunit FmdD, + x * ? + x * ?, calculation from nucleotide sequence
?
-
3 different polypeptides are detected by SDS-PAGE: MW 60000, MW 45000 and MW 38000
?
-
3 different polypeptides are detected by SDS-PAGE: MW 60000, MW 45000 and MW 38000
-
tetramer
-
1 * 65000 + 1 * 53000 + 1 * 31000 + 1 * 15000, SDS-PAGE
tetramer
-
1 * 65000 + 1 * 53000 + 1 * 31000 + 1 * 15000, SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nanodroplet vapor diffusion method, using 0.2 M MgCl2 and 20% (w/v) PEG 3350
nanodroplet vapor diffusion method, using 0.01 M nickel chloride, 20% (w/v) PEG MME 2000 and 0.1 M Tris pH 8.5
nanodroplet vapor diffusion method, using 0.2 M magnesium nitrate and 20% (w/v) PEG 3350 or 10% (w/v) PEG 8000, 0.2 M zinc acetate and 0.1 M MES pH 6.0
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
-
pH 7.4, in presence of 0.1 M ammonium sulfate, 0.1 M potassium sulfate, and 0.5 M potassium chloride, thermostable up to
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel-chelating resin column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the molybdenum-type formylmethanofuran dehydrogenase operon reporter genes fmdE1 and fmdA1 are expressed at 14fold higher levels during methanol growth conditions relative to acetate growth. Genes fmdF2, fmdA2, and fmdB2 are expressed about 2fold higher during these conditions, but the maximal level of expression is less than 5% of that seen for the fmdE1 and fmdA1 genes. The tungsten-type formylmethanofuran dehydrogenase genes fwdB1 and fwdA1 are also expressed 15fold higher levels during methanol growth relative to acetate
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vorholt, J.A.; Vaupel, M.; Thauer, R.K.
A polyferredoxin with eight [4Fe-4S] clusters as a subunit of molybdenum formylmethanofuran dehydrogenase from Methanosarcina barkeri
Eur. J. Biochem.
236
309-317
1996
Methanosarcina barkeri
brenda
Bertram, P.A.; Thauer, R.K.
Thermodynamics of the formylmethanofuran dehydrogenase reaction in Methanobacterium thermoautotrophicum
Eur. J. Biochem.
226
811-818
1994
Methanothermobacter thermautotrophicus
brenda
Bertram, P.A.; Karrasch, M.; Schmitz, R.A.; Böcher, R.; Albracht, S.P.J.; Thauer, R.K.
Formylmethanofuran dehydrogenase from methanogenic archaea. Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron-sulfur proteins
Eur. J. Biochem.
220
477-484
1994
Methanosarcina barkeri, Methanothermobacter thermautotrophicus, Methanothermobacter wolfeii
brenda
Schmitz, R.A.; Albracht, S.P.J.; Thauer, R.K.
A molybdenum and a tungsten isoenzyme of formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei
Eur. J. Biochem.
209
1013-1018
1992
Methanothermobacter wolfeii
brenda
Karrasch, M.; Börner, G.; Enssle, M.; Thauer, R.K.
The molybdoenzyme formylmethanofuran dehydrogenase from Methanosarcina barkeri contains a pterin cofactor
Eur. J. Biochem.
194
367-372
1990
Methanosarcina barkeri
brenda
Karrasch, M.; Börner, G.; Enssle, M.; Thauer, R.K.
Formylmethanofuran dehydrogenase from methanogenic bacteria, a molybdoenzyme
FEBS Lett.
253
226-230
1989
Methanosarcina barkeri, Methanothermobacter thermautotrophicus
brenda
Breitung, J.; Börner, G.; Karrasch, M.; Berkessel, A.; Thauer, R.K.
N-Furfurylformamide as a pseudo-substrate for formylmethanofuran converting enzymes from methanogenic bacteria
FEBS Lett.
268
257-260
1990
Methanosarcina barkeri, Methanothermobacter thermautotrophicus
brenda
Schmitz, R.A.; Albracht, S.P.J.; Thauer, R.K.
Properties of the tungsten-substituted molybdenum formylmethanofuran dehydrogenase from Methanobacterium wolfei
FEBS Lett.
309
78-81
1992
Methanothermobacter wolfeii
brenda
Börner, G.; Karrasch, M.; Thauer, R.K.
Molybdopterin adenine dinucleotide and molybdopterin hypoxanthine dinucleotide in formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum (Marburg)
FEBS Lett.
290
31-34
1991
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
brenda
Hochheimer, A.; Heddrich, R.; Thauer, R.K.
The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum: induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme
Arch. Microbiol.
170
389-393
1998
Methanothermobacter thermautotrophicus, Methanothermobacter wolfeii
brenda
Bertram, P.A.; Schmitz, R.A.; Linder, D.; Thauer, R.K.
Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum. Identification and characterization of a tungsten isoenzyme of formylmethanofuran dehydrogenase
Arch. Microbiol.
161
220-228
1994
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus Marburg / DSM 2133
brenda
Schmitz, R.A.; Linder, D.; Stetter, K.O.; Thauer, R.K.
N5,N10-Methylenetetrahydromethanopterin reductase (coenzyme F420-dependent) and formylmethanofuran dehydrogenase from the hyperthermophile Archaeoglobus fulgidus
Arch. Microbiol.
156
427-434
1991
Archaeoglobus fulgidus
-
brenda
Vorholt, J.A.
A selenium-dependent and a selenium-independent formylmethanofuran dehydrogenase and their transcriptional regulation in the hyperthermophilic Methanopyrus kandleri
Mol. Microbiol.
23
1033-1042
1997
Methanopyrus kandleri
brenda
Karrasch, M.; Börner, G.; Thauer, R.K.
The molybdenum cofactor of formylmethanofuran dehydrogenase from Methanosarcina barkeri is a molybdopterin guanine dinucleotide
FEBS Lett.
274
48-52
1990
Methanosarcina barkeri
brenda
Vorholt, J.A.; Thauer, R.K.
The active species of 'CO2' utilized by formylmethanofuran dehydrogenase from Methanogenic archaea
Eur. J. Biochem.
248
919-924
1997
Methanosarcina barkeri, Methanothermobacter thermautotrophicus
brenda
Hochheimer, A.; Linder, D.; Thauer, R.K.; Hedderich, R.
The molybdenum formylmethanofuran dehydrogenase operon and the tungsten formylmethanofuran dehydrogenase operon from Methanobacterium thermoautotrophicum. Structures and transcriptional regulation
Eur. J. Biochem.
242
156-162
1996
Methanothermobacter thermautotrophicus
brenda
de Poorter, L.M.; Geerts, W.G.; Theuvenet, A.P.; Keltjens, J.T.
Bioenergetics of the formyl-methanofuran dehydrogenase and heterodisulfide reductase reactions in Methanothermobacter thermautotrophicus
Eur. J. Biochem.
270
66-75
2003
Methanothermobacter thermautotrophicus
brenda
Stojanowic, A.; Hedderich, R.
CO2 reduction to the level of formylmethanofuran in Methanosarcina barkeri is non-energy driven when CO is the electron donor
FEMS Microbiol. Lett.
235
163-167
2004
Methanosarcina barkeri
brenda
Andreesen, J.R.; Makdessi, K.
Tungsten, the surprisingly positively acting heavy metal element for prokaryotes
Ann. N. Y. Acad. Sci.
1125
215-229
2008
Methanothermobacter wolfeii
brenda
Axelrod, H.L.; Das, D.; Abdubek, P.; Astakhova, T.; Bakolitsa, C.; Carlton, D.; Chen, C.; Chiu, H.J.; Clayton, T.; Deller, M.C.; et al
Structures of three members of Pfam PF02663 (FmdE) implicated in microbial methanogenesis reveal a conserved alpha+beta core domain and an auxiliary C-terminal treble-clef zinc finger
Acta Crystallogr. Sect. F
66
1335-1346
2010
Thermoplasma acidophilum, Desulfitobacterium hafniense (B8FYU2), Syntrophus aciditrophicus (Q2LQ23), Desulfitobacterium hafniense DCB-2 (B8FYU2), Desulfitobacterium hafniense DCB-2, Syntrophus aciditrophicus SB (Q2LQ23), Syntrophus aciditrophicus SB
brenda
Rohlin, L.; Gunsalus, R.P.
Carbon-dependent control of electron transfer and central carbon pathway genes for methane biosynthesis in the Archaean, Methanosarcina acetivorans strain C2A
BMC Microbiol.
10
62
2010
Methanosarcina acetivorans
brenda
Costa, K.C.; Wong, P.M.; Wang, T.; Lie, T.J.; Dodsworth, J.A.; Swanson, I.; Burn, J.A.; Hackett, M.; Leigh, J.A.
Protein complexing in a methanogen suggests electron bifurcation and electron delivery from formate to heterodisulfide reductase
Proc. Natl. Acad. Sci. USA
107
11050-11055
2010
Methanothermobacter marburgensis, Methanothermobacter marburgensis S2
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
brenda
Kaster, A.; Moll, J.; Parey, K.; Thauer, R.
Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea
Proc. Natl. Acad. Sci. USA
108
2981-2986
2011
Methanothermobacter marburgensis, Methanothermobacter marburgensis DSM 2133
brenda
Matschiavelli, N.; Rother, M.
Role of a putative tungsten-dependent formylmethanofuran dehydrogenase in Methanosarcina acetivorans
Arch. Microbiol.
197
379-388
2015
Methanosarcina acetivorans
brenda
Meuer, J.; Kuettner, H.C.; Zhang, J.K.; Hedderich, R.; Metcalf, W.W.
Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation
Proc. Natl. Acad. Sci. USA
99
5632-5637
2002
Methanosarcina barkeri
brenda
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