Information on EC 1.2.99.5 - formylmethanofuran dehydrogenase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
1.2.99.5
-
RECOMMENDED NAME
GeneOntology No.
formylmethanofuran dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
formylmethanofuran + H2O + acceptor = CO2 + methanofuran + reduced acceptor
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
methanogenesis from H2 and CO2
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-
methyl-coenzyme M oxidation to CO2
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-
reductive acetyl coenzyme A pathway II (autotrophic methanogens)
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methanogenesis from CO2
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Methane metabolism
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Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
formylmethanofuran:acceptor oxidoreductase
A molybdoprotein containing a pterin cofactor. Tungstate can substitute for molybdate. The enzyme catalyses a reversible reaction in methanogenic bacteria, and is involved in methanogenesis from CO2 as well as the oxidation of methyl-coenzyme M to CO2. Methyl viologen can act as acceptor. Also oxidizes N-furfurylformamide.
CAS REGISTRY NUMBER
COMMENTARY hide
119940-12-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunit E
UniProt
Manually annotated by BRENDA team
chemolithoautotrophic
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-
Manually annotated by BRENDA team
contains two tungsten isoenzymes and probably no molybdenum enzyme
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-
Manually annotated by BRENDA team
subunit E
UniProt
Manually annotated by BRENDA team
subunit E
UniProt
Manually annotated by BRENDA team
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
CO2 + methanofuran + reduced ferredoxin
formylmethanofuran + H2O + oxidized ferredoxin
show the reaction diagram
Formamide + oxidized acceptor
?
show the reaction diagram
Formate + oxidized acceptor
?
show the reaction diagram
formylmethanofuran + H2O + oxidized ferredoxin
CO2 + methanofuran + reduced ferredoxin
show the reaction diagram
-
-
-
-
r
Formylmethanofuran + oxidized 1,1',2,2'-tetramethylviologen
CO2 + methanofuran + reduced 1,1',2,2'-tetramethylviologen
show the reaction diagram
Formylmethanofuran + oxidized acceptor
?
show the reaction diagram
-
formation of formylmethanofuran, which is an intermediate in methanogenesis from CO2
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-
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Formylmethanofuran + oxidized benzylviologen
Formylmethanofuran + reduced benzylviologen
show the reaction diagram
Formylmethanofuran + oxidized carbamoylmethylviologen
Formylmethanofuran + reduced carbamoylmethylviologen
show the reaction diagram
-
-
-
-
Formylmethanofuran + oxidized methylviologen
Formylmethanofuran + reduced methylviologen
show the reaction diagram
N-Furfurylformamide + oxidized acceptor
?
show the reaction diagram
N-Methylformamide + oxidized acceptor
?
show the reaction diagram
additional information
?
-
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
CO2 + methanofuran + reduced ferredoxin
formylmethanofuran + H2O + oxidized ferredoxin
show the reaction diagram
formylmethanofuran + H2O + oxidized ferredoxin
CO2 + methanofuran + reduced ferredoxin
show the reaction diagram
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-
-
-
r
Formylmethanofuran + oxidized acceptor
?
show the reaction diagram
-
formation of formylmethanofuran, which is an intermediate in methanogenesis from CO2
-
-
-
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pterin
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K2HPO4
-
stimulates
Molybdenum
Tungsten
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
Formamide
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molybdenum enzyme
0.035 - 1.7
formate
0.06 - 0.1
formylmethanofuran
0.1
methanofuran
5
methylformamide
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molybdenum enzyme
0.037 - 0.8
methylviologen
0.013 - 0.03
N-formylmethanofuran
0.053 - 70
N-Furfurylformamide
0.125
oxidized 1,1',2,2'-tetramethylviologen
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-
0.015
oxidized benzylviologen
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-
0.008
oxidized carbamoylviologen
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-
0.04
oxidized methylviologen
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-
0.4
reduced 1,1',2,2'-tetramethylviologen
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10.7
formylmethanofuran
Methanosarcina barkeri
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01
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pH 7.5, 65°C, cell extract
0.2
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pH 7.5, 65°C
0.43
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pH 7.5, 65°C, cell extract
0.7
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pH 7.5, 65°C, cell extract
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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tungsten-substituted molybdenum enzyme
7.9
-
non-substituted molybdenum enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
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no activity below pH 6.5, maximal activity above pH 7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 70
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25°C: less than 5% of maximal activity, 60°C: about 90% of maximal activity, 70°C: maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6
calculated from amino acid sequence
6.1
-
calculated from amino acid sequence
6.2
calculated from amino acid sequence
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17400
calculated from amino acid sequence
21500
calculated from amino acid sequence
23100
-
calculated from amino acid sequence
130000
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native PAGE
200000
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and MW 400000, native PAGE
260000
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gel filtration
400000
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and MW 200000, native PAGE
440000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
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or trimer, 1 or 2 * 64000 + 1 or 2 * 51000 + 1 or 2 * 31000, SDs-PAGE
tetramer
trimer
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or hexamer, 1 or 2 * 64000 + 1 or 2 * 51000 + 1 or 2 * 31000, SDS-PAGE
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 hide
LITERATURE
55
-
pH 7.4, thermostable up to
65
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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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme in crude enzyme extract is unstable to freezing
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
molybdenum-containing isoenzyme
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nickel-chelating resin column chromatography
Poly-Prep resin column chromatography
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tungsten-containing isoenzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression of the six genes of the fmd operon 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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