BRENDA - Enzyme Database show
show all sequences of 1.2.7.5

The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique glycolytic pathway

Mukund, S.; Adams, M.W.W.; J. Biol. Chem. 266, 14208-14216 (1991)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
no effect of CoA
Pyrococcus furiosus
General Stability
General Stability
Organism
10% glycerol and 2 mM DTT stabilize during purification
Pyrococcus furiosus
Inhibitors
Inhibitors
Commentary
Organism
Structure
arsenite
50% inhibition at 1 mM
Pyrococcus furiosus
crotonaldehyde
substrate inhibition above 0.2 mM
Pyrococcus furiosus
cyanide
50% inhibition at 8 mM
Pyrococcus furiosus
iodoacetate
50% inhibition at 0.2 mM
Pyrococcus furiosus
additional information
no effect of CoA
Pyrococcus furiosus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.04
-
crotonaldehyde
pH 8.4, 80°C, with methyl viologen as electron acceptor
Pyrococcus furiosus
1
-
glyceraldehyde
pH 8.4, 65°C, with methyl viologen as electron acceptor
Pyrococcus furiosus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
6.6 gatoms per 85000g of protein
Pyrococcus furiosus
Molybdenum
part of a tungsten-molybdopterin cofactor
Pyrococcus furiosus
Tungsten
1.0 gatoms per 85000g of protein; part of a tungsten-molybdopterin cofactor
Pyrococcus furiosus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
80000
-
1 * 80000, SDS-PAGE
Pyrococcus furiosus
90000
-
gel filtration
Pyrococcus furiosus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
an aldehyde + H2O + oxidized ferredoxin
Pyrococcus furiosus
-
an acid + H+ + reduced ferredoxin
-
Pyrococcus furiosus
?
glyceraldehyde + H2O + oxidized ferredoxin
Pyrococcus furiosus
involved in glycolysis
glycerate + H+ + reduced ferredoxin
-
Pyrococcus furiosus
ir
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pyrococcus furiosus
-
hyperthermophilic archaeon; strain DSM 3638
-
Oxidation Stability
Oxidation Stability
Organism
sensitive against O2, dithionite is added to avoid trace contamination with O2 during purification and enzyme assay
Pyrococcus furiosus
Purification (Commentary)
Commentary
Organism
to homogeneity under strict anaerobic conditions
Pyrococcus furiosus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
53.6
-
purified enzyme, substrate crotonaldehyde with methyl viologen as electron acceptor
Pyrococcus furiosus
Storage Stability
Storage Stability
Organism
-196°C, pure enzyme pellet is thawed anaerobically after storage in liquid N2, no loss of activity for several months
Pyrococcus furiosus
4°c or 23°C, pure enzyme, 50 mM Tris-HCl, pH 8.0, 2 mM sodium dithionite, 2 mM DTT, 10% v/v glycerol, loss of 25% activity after 6 h under strict anaerobic conditions
Pyrococcus furiosus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetaldehyde + H2O + oxidized ferredoxin
-
11938
Pyrococcus furiosus
acetate + H+ + reduced ferredoxin
-
11938
Pyrococcus furiosus
ir
an aldehyde + H2O + oxidized ferredoxin
-
11938
Pyrococcus furiosus
an acid + H+ + reduced ferredoxin
-
11938
Pyrococcus furiosus
?
an aldehyde + H2O + oxidized ferredoxin
-
11938
Pyrococcus furiosus
an acid + H+ + reduced ferredoxin
-
11938
Pyrococcus furiosus
ir
butyraldehyde + H2O + oxidized ferredoxin
-
11938
Pyrococcus furiosus
butyrate + H+ + reduced ferredoxin
-
11938
Pyrococcus furiosus
ir
crotonaldehyde + H2O + oxidized ferredoxin
best substrate
11938
Pyrococcus furiosus
pyruvate + H+ + reduced ferredoxin
-
-
-
ir
crotonaldehyde + H2O + oxidized methyl viologen
artifical electron acceptor
11938
Pyrococcus furiosus
pyruvate + H+ + reduced methyl viologen
-
-
-
ir
formaldehyde + H2O + oxidized ferredoxin
-
11938
Pyrococcus furiosus
formate + H+ + reduced ferredoxin
-
11938
Pyrococcus furiosus
ir
glyceraldehyde + H2O + oxidized ferredoxin
-
11938
Pyrococcus furiosus
glycerate + H+ + reduced ferredoxin
-
11938
Pyrococcus furiosus
ir
glyceraldehyde + H2O + oxidized ferredoxin
involved in glycolysis
11938
Pyrococcus furiosus
glycerate + H+ + reduced ferredoxin
-
11938
Pyrococcus furiosus
ir
glyceraldehyde + H2O + oxidized methyl viologen
-
11938
Pyrococcus furiosus
glycerate + H+ + reduced methyl viologen
-
11938
Pyrococcus furiosus
ir
additional information
enzyme shows an active and an inactive form
11938
Pyrococcus furiosus
?
-
-
-
-
additional information
no oxidizing activity with glyceraldehyde-3-phosphate, glyoxylate, glucose, glucose 6-phosphate, CO, H2, formate, pyruvate, 2-oxoglutarate
11938
Pyrococcus furiosus
?
-
-
-
-
additional information
NAD(P) is no electron acceptor
11938
Pyrococcus furiosus
?
-
-
-
-
additional information
no H2 evolution from reduced methyl viologen
11938
Pyrococcus furiosus
?
-
-
-
-
additional information
no activity with CoA
11938
Pyrococcus furiosus
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
monomer
1 * 80000, SDS-PAGE
Pyrococcus furiosus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
90
-
above
Pyrococcus furiosus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
additional information
-
the enzyme is thermostable
Pyrococcus furiosus
23
-
pure enzyme, 5.2 mg/ml, 50 mM Tris-HCl, pH 8.0, 2 mM sodium dithionite, 2 mM DTT, 10% v/v glycerol, exposure to air, less than 20% remaining activity after 5 min, after 10 additional min 10% residual activity is reached, which stays constant for more than 30 min
Pyrococcus furiosus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.4
-
sharp maximum
Pyrococcus furiosus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7
8.4
activity increases with increasing pH at increasing temperature, nearly no activity below pH 7.0
Pyrococcus furiosus
Cofactor
Cofactor
Commentary
Organism
Structure
Ferredoxin
-
Pyrococcus furiosus
tungsten-molybdopterin
tungstopterin center
Pyrococcus furiosus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
no effect of CoA
Pyrococcus furiosus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
Ferredoxin
-
Pyrococcus furiosus
tungsten-molybdopterin
tungstopterin center
Pyrococcus furiosus
General Stability (protein specific)
General Stability
Organism
10% glycerol and 2 mM DTT stabilize during purification
Pyrococcus furiosus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
arsenite
50% inhibition at 1 mM
Pyrococcus furiosus
crotonaldehyde
substrate inhibition above 0.2 mM
Pyrococcus furiosus
cyanide
50% inhibition at 8 mM
Pyrococcus furiosus
iodoacetate
50% inhibition at 0.2 mM
Pyrococcus furiosus
additional information
no effect of CoA
Pyrococcus furiosus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.04
-
crotonaldehyde
pH 8.4, 80°C, with methyl viologen as electron acceptor
Pyrococcus furiosus
1
-
glyceraldehyde
pH 8.4, 65°C, with methyl viologen as electron acceptor
Pyrococcus furiosus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
6.6 gatoms per 85000g of protein
Pyrococcus furiosus
Molybdenum
part of a tungsten-molybdopterin cofactor
Pyrococcus furiosus
Tungsten
1.0 gatoms per 85000g of protein; part of a tungsten-molybdopterin cofactor
Pyrococcus furiosus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
80000
-
1 * 80000, SDS-PAGE
Pyrococcus furiosus
90000
-
gel filtration
Pyrococcus furiosus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
an aldehyde + H2O + oxidized ferredoxin
Pyrococcus furiosus
-
an acid + H+ + reduced ferredoxin
-
Pyrococcus furiosus
?
glyceraldehyde + H2O + oxidized ferredoxin
Pyrococcus furiosus
involved in glycolysis
glycerate + H+ + reduced ferredoxin
-
Pyrococcus furiosus
ir
Oxidation Stability (protein specific)
Oxidation Stability
Organism
sensitive against O2, dithionite is added to avoid trace contamination with O2 during purification and enzyme assay
Pyrococcus furiosus
Purification (Commentary) (protein specific)
Commentary
Organism
to homogeneity under strict anaerobic conditions
Pyrococcus furiosus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
53.6
-
purified enzyme, substrate crotonaldehyde with methyl viologen as electron acceptor
Pyrococcus furiosus
Storage Stability (protein specific)
Storage Stability
Organism
-196°C, pure enzyme pellet is thawed anaerobically after storage in liquid N2, no loss of activity for several months
Pyrococcus furiosus
4°c or 23°C, pure enzyme, 50 mM Tris-HCl, pH 8.0, 2 mM sodium dithionite, 2 mM DTT, 10% v/v glycerol, loss of 25% activity after 6 h under strict anaerobic conditions
Pyrococcus furiosus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetaldehyde + H2O + oxidized ferredoxin
-
11938
Pyrococcus furiosus
acetate + H+ + reduced ferredoxin
-
11938
Pyrococcus furiosus
ir
an aldehyde + H2O + oxidized ferredoxin
-
11938
Pyrococcus furiosus
an acid + H+ + reduced ferredoxin
-
11938
Pyrococcus furiosus
?
an aldehyde + H2O + oxidized ferredoxin
-
11938
Pyrococcus furiosus
an acid + H+ + reduced ferredoxin
-
11938
Pyrococcus furiosus
ir
butyraldehyde + H2O + oxidized ferredoxin
-
11938
Pyrococcus furiosus
butyrate + H+ + reduced ferredoxin
-
11938
Pyrococcus furiosus
ir
crotonaldehyde + H2O + oxidized ferredoxin
best substrate
11938
Pyrococcus furiosus
pyruvate + H+ + reduced ferredoxin
-
-
-
ir
crotonaldehyde + H2O + oxidized methyl viologen
artifical electron acceptor
11938
Pyrococcus furiosus
pyruvate + H+ + reduced methyl viologen
-
-
-
ir
formaldehyde + H2O + oxidized ferredoxin
-
11938
Pyrococcus furiosus
formate + H+ + reduced ferredoxin
-
11938
Pyrococcus furiosus
ir
glyceraldehyde + H2O + oxidized ferredoxin
-
11938
Pyrococcus furiosus
glycerate + H+ + reduced ferredoxin
-
11938
Pyrococcus furiosus
ir
glyceraldehyde + H2O + oxidized ferredoxin
involved in glycolysis
11938
Pyrococcus furiosus
glycerate + H+ + reduced ferredoxin
-
11938
Pyrococcus furiosus
ir
glyceraldehyde + H2O + oxidized methyl viologen
-
11938
Pyrococcus furiosus
glycerate + H+ + reduced methyl viologen
-
11938
Pyrococcus furiosus
ir
additional information
enzyme shows an active and an inactive form
11938
Pyrococcus furiosus
?
-
-
-
-
additional information
no oxidizing activity with glyceraldehyde-3-phosphate, glyoxylate, glucose, glucose 6-phosphate, CO, H2, formate, pyruvate, 2-oxoglutarate
11938
Pyrococcus furiosus
?
-
-
-
-
additional information
NAD(P) is no electron acceptor
11938
Pyrococcus furiosus
?
-
-
-
-
additional information
no H2 evolution from reduced methyl viologen
11938
Pyrococcus furiosus
?
-
-
-
-
additional information
no activity with CoA
11938
Pyrococcus furiosus
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 80000, SDS-PAGE
Pyrococcus furiosus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
90
-
above
Pyrococcus furiosus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
additional information
-
the enzyme is thermostable
Pyrococcus furiosus
23
-
pure enzyme, 5.2 mg/ml, 50 mM Tris-HCl, pH 8.0, 2 mM sodium dithionite, 2 mM DTT, 10% v/v glycerol, exposure to air, less than 20% remaining activity after 5 min, after 10 additional min 10% residual activity is reached, which stays constant for more than 30 min
Pyrococcus furiosus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.4
-
sharp maximum
Pyrococcus furiosus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7
8.4
activity increases with increasing pH at increasing temperature, nearly no activity below pH 7.0
Pyrococcus furiosus
Other publictions for EC 1.2.7.5
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)
740953
Liew
Metabolic engineering of Clost ...
Clostridium autoethanogenum
Metab. Eng.
40
104-114
2017
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1
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3
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1
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1
1
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740209
Ammam
Effect of tungstate on acetate ...
Sporomusa ovata, Sporomusa ovata DSM-2662
Biotechnol. Biofuels
9
163
2016
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737164
Basen
Single gene insertion drives b ...
Pyrococcus furiosus
Proc. Natl. Acad. Sci. USA
111
17618-17623
2014
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740626
Debnar-Daumler
Simultaneous involvement of a ...
Aromatoleum aromaticum
J. Bacteriol.
196
483-492
2014
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722823
Liao
Why is the molybdenum-substitu ...
Pyrococcus furiosus
J. Biol. Inorg. Chem.
18
175-181
2013
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722893
Liao
Tungsten-dependent formaldehyd ...
Pyrococcus furiosus
J. Inorg. Biochem.
105
927-936
2011
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745210
Sevcenco
Molybdenum incorporation in t ...
Pyrococcus furiosus
J. Bacteriol.
192
4143-4152
2010
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1
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1
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692610
Sugimoto
In situ generation of oxo-sulf ...
synthetic construct
Inorg. Chem.
46
8460-8462
2007
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1
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675237
Thapper
Biochemical and spectroscopic ...
Desulfovibrio aminophilus, Desulfovibrio aminophilus DSM 12254
J. Inorg. Biochem.
100
44-50
2006
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656293
Hagedoorn
Purification and characterizat ...
Pyrobaculum aerophilum
J. Biol. Inorg. Chem.
10
259-269
2005
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1
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3
2
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6
1
1
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1
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2
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1
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1
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6
1
1
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674251
Bevers
WOR5, a novel tungsten-contain ...
Pyrococcus furiosus
J. Bacteriol.
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7056-7061
2005
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4
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1
1
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654430
Wahyudi
Characterization of aldehyde f ...
Magnetospirillum magneticum, Magnetospirillum magneticum AMB-1
Biochem. Biophys. Res. Commun.
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223-229
2003
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8
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644691
Roy
Aldehyde oxidoreductases from ...
Pyrococcus endeavori, Pyrococcus furiosus, Thermococcus litoralis, Thermococcus sp., Thermococcus sp. ES1
Methods Enzymol.
331
132-144
2001
3
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1
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15
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11
5
5
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7
2
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2
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40
2
4
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1
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4
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12
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3
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15
1
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15
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13
5
5
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2
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2
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40
3
4
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1
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4
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745202
Adams
Key role for sulfur in peptid ...
Pyrococcus furiosus
J. Bacteriol.
183
716-724
2001
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1
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1
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1
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644689
Roy
Purification and molecular cha ...
Pyrococcus furiosus
J. Bacteriol.
181
1171-1180
1999
1
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1
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2
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4
2
1
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4
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1
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2
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12
1
1
1
2
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1
1
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2
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1
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2
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1
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2
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4
2
1
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1
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-
2
-
12
1
1
1
2
-
1
1
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644690
Hu
Formaldehyde ferredoxin oxidor ...
Pyrococcus furiosus
J. Mol. Biol.
286
899-914
1999
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1
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5
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1
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1
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3
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3
1
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3
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1
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721578
Zhou
Site-directed mutations of the ...
Pyrococcus furiosus
Biochemistry
36
10892-10900
1997
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1
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4
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1
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1
1
644687
Koehler
-
Spectroscopic characterization ...
Pyrococcus endeavori, Pyrococcus furiosus
J. Am. Chem. Soc.
118
12391-12405
1996
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6
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2
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2
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2
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4
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4
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6
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2
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644688
Das
-
Modeling the tungsten sites of ...
Pyrococcus furiosus
J. Am. Chem. Soc.
118
1387-1397
1996
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1
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2
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1
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2
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2
1
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2
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2
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722057
Arendsen
-
Redox chemistry of biological ...
Pyrococcus furiosus
Chemistry
1
292-296
1996
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2
2
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1
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1
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1
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1
1
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2
2
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1
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1
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1
1
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-
722490
Mukund
Molybdenum and vanadium do not ...
Pyrococcus furiosus
J. Bacteriol.
178
163-167
1996
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1
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3
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1
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1
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1
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1
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1
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1
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1
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1
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11935
Heider
Purification, characterization ...
Thermococcus sp., Thermococcus sp. ES1
J. Bacteriol.
177
4757-4764
1995
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15
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2
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8
1
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1
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1
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16
1
1
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2
15
1
1
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4
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4
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11
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15
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6
2
1
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1
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1
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1
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16
1
1
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2
15
1
1
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644684
Kletzin
Molecular characterization of ...
Pyrococcus furiosus
J. Bacteriol.
177
4817-4819
1995
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1
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1
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1
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644686
Chan
Structure of a hyperthermophil ...
Pyrococcus furiosus
Science
267
1463-1469
1995
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1
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1
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3
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1
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1
1
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2
1
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2
1
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2
1
1
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1
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722438
George
-
Aldehyde ferredoxin oxidoreduc ...
Pyrococcus furiosus
J. Am. Chem. Soc.
114
3521-3523
1992
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1
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11938
Mukund
The novel tungsten-iron-sulfur ...
Pyrococcus furiosus
J. Biol. Chem.
266
14208-14216
1991
1
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2
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1
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1
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1
2
15
1
1
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2
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1
1
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2
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1
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2
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1
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5
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2
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3
2
2
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1
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1
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1
2
15
1
1
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2
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1
1
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