BRENDA - Enzyme Database show
show all sequences of 2.3.1.101

Salt dependence, kinetic properties and catalytic mechanism of N-formylmethanofuran:tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleri

Breitung, J.; Brner, G.; Scholz, S.; Linder, D.; Stetter, K.O.; Thauer, R.K.; Eur. J. Biochem. 210, 971-981 (1992)

Data extracted from this reference:

General Stability
General Stability
Organism
presence of salts, 1.5 M, required for optimal stabilization, order of efficiency in protecting the enzyme from heat inactivation at 90C: K2HPO4, (NH4)2SO4, KCl, NH4Cl, NaCl, Na2SO4, Na2HPO4
Methanopyrus kandleri
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.05
-
formylmethanofuran
-
Methanopyrus kandleri
0.1
-
5,6,7,8-tetrahydromethanopterin
-
Methanopyrus kandleri
20
-
N-Furfurylformamide
-
Methanopyrus kandleri
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
K2HPO4
no activity in absence, assay mixture contains 2 M
Methanopyrus kandleri
(NH4)2SO4
-
Methanopyrus kandleri
Salts
absolutely dependent on the presence of phosphate or sulfate salts for activity, efficiency of activation in decreasing order: K2HPO4, (NH4)2SO4, K2SO4, Na2SO4, Na2HPO4, no activation: NaCl, KCl, NH4Cl
Methanopyrus kandleri
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
1 * 35000, SDS-PAGE
Methanopyrus kandleri
Organic Solvent Stability
Organic Solvent
Commentary
Organism
additional information
enzyme completely soluble in 80% ammonium sulfate
Methanopyrus kandleri
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanopyrus kandleri
-
-
-
Purification (Commentary)
Commentary
Organism
-
Methanopyrus kandleri
Reaction
Reaction
Commentary
Organism
formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin
ternary complex type mechanism
Methanopyrus kandleri
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
-
Methanopyrus kandleri
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
formylmethanofuran + 5,6,7,8-tetrahydromethanopterin
specific for tetrahydromethanopterin
486087
Methanopyrus kandleri
methanofuran + N5-formyl-5,6,7,8-tetrahydromethanopterin
-
486087
Methanopyrus kandleri
-
N-furfurylformamide + 5,6,7,8-tetrahydromethanopterin
pseudo-substrate
486087
Methanopyrus kandleri
2-(aminomethyl)furane + N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 35000, SDS-PAGE
Methanopyrus kandleri
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
90
-
-
Methanopyrus kandleri
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
90
-
stable up to, in presence of salts
Methanopyrus kandleri
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
-
Methanopyrus kandleri
General Stability (protein specific)
General Stability
Organism
presence of salts, 1.5 M, required for optimal stabilization, order of efficiency in protecting the enzyme from heat inactivation at 90C: K2HPO4, (NH4)2SO4, KCl, NH4Cl, NaCl, Na2SO4, Na2HPO4
Methanopyrus kandleri
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.05
-
formylmethanofuran
-
Methanopyrus kandleri
0.1
-
5,6,7,8-tetrahydromethanopterin
-
Methanopyrus kandleri
20
-
N-Furfurylformamide
-
Methanopyrus kandleri
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
K2HPO4
no activity in absence, assay mixture contains 2 M
Methanopyrus kandleri
(NH4)2SO4
-
Methanopyrus kandleri
Salts
absolutely dependent on the presence of phosphate or sulfate salts for activity, efficiency of activation in decreasing order: K2HPO4, (NH4)2SO4, K2SO4, Na2SO4, Na2HPO4, no activation: NaCl, KCl, NH4Cl
Methanopyrus kandleri
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
1 * 35000, SDS-PAGE
Methanopyrus kandleri
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
additional information
enzyme completely soluble in 80% ammonium sulfate
Methanopyrus kandleri
Purification (Commentary) (protein specific)
Commentary
Organism
-
Methanopyrus kandleri
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
-
Methanopyrus kandleri
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
formylmethanofuran + 5,6,7,8-tetrahydromethanopterin
specific for tetrahydromethanopterin
486087
Methanopyrus kandleri
methanofuran + N5-formyl-5,6,7,8-tetrahydromethanopterin
-
486087
Methanopyrus kandleri
-
N-furfurylformamide + 5,6,7,8-tetrahydromethanopterin
pseudo-substrate
486087
Methanopyrus kandleri
2-(aminomethyl)furane + N5-formyl-5,6,7,8-tetrahydromethanopterin
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 35000, SDS-PAGE
Methanopyrus kandleri
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
90
-
-
Methanopyrus kandleri
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
90
-
stable up to, in presence of salts
Methanopyrus kandleri
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
-
Methanopyrus kandleri
Other publictions for EC 2.3.1.101
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)
727375
Kojima
A reversed genetic approach re ...
uncultured archaeon
Environ. Microbiol.
16
3431-3442
2014
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-
1
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2
-
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1
1
-
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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2
1
1
1
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1
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-
-
-
675376
Acharya
The structure of formylmethano ...
Methanopyrus kandleri
J. Mol. Biol.
357
870-879
2006
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-
1
-
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3
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1
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661043
Shima
Hyperthermophilic and salt-dep ...
Methanopyrus kandleri
Biochem. Soc. Trans.
32
269-272
2004
1
-
-
-
-
1
-
-
-
2
1
-
-
4
-
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1
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1
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3
-
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2
-
-
-
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-
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-
-
-
486096
Pomper
Generation of formate by the f ...
Methylorubrum extorquens
FEBS Lett.
523
133-137
2002
-
-
-
-
-
-
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1
-
2
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1
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2
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726443
Mamat
Crystal structures and enzymat ...
Archaeoglobus fulgidus, Methanopyrus kandleri, Methanopyrus kandleri DSM 6324, Methanosarcina barkeri, Methanosarcina barkeri DSM 804
Protein Sci.
11
:2168-2178
2002
-
-
2
2
-
-
-
-
-
3
-
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9
-
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5
4
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3
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2
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5
4
-
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3
-
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-
-
-
486095
Pomper
Characterization of the formyl ...
Methylorubrum extorquens, Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
Eur. J. Biochem.
268
4769-4775
2001
-
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1
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2
-
4
1
2
-
21
1
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1
1
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1
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2
1
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1
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1
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1
2
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1
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1
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1
-
2
1
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-
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-
1
-
-
-
-
-
-
-
-
-
486097
Shima
Tetrahydromethanopterin-specif ...
Methanopyrus kandleri
Methods Enzymol.
331
317-353
2001
-
-
1
-
-
-
-
2
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1
1
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1
1
1
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1
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1
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1
1
1
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1
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2
-
1
1
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1
1
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1
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1
-
1
1
1
-
1
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-
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-
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-
726828
Shima
Activation and thermostabiliza ...
Methanopyrus kandleri
Arch. Microbiol.
170
469-472
1998
1
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1
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2
1
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1
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1
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2
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1
-
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-
-
-
-
486094
Ermler
Formylmethanofuran: tetrahydro ...
Methanopyrus kandleri
Structure
5
635-646
1997
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1
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1
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3
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1
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2
1
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1
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721443
Vorholt
Pathways of autotrophic CO2 fi ...
Ferroglobus placidus, Ferroglobus placidus DSM 10642
Arch. Microbiol.
167
19-23
1997
-
-
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5
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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
1
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-
486092
Kunow
Primary structure and properti ...
Methanosarcina barkeri, Methanosarcina barkeri Fusaro / DSM 804
Arch. Microbiol.
165
97-105
1996
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-
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1
2
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8
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1
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1
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1
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1
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486093
Shima
Crystallization and preliminar ...
Methanopyrus kandleri
Proteins Struct. Funct. Genet.
26
118-120
1996
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1
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3
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486091
Shima
Formylmethanofuran:tetrahydrom ...
Methanopyrus kandleri
Eur. J. Biochem.
230
906-913
1995
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1
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4
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1
1
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7
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1
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1
1
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1
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1
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721441
Vornolt
-
Enzymes and coenzymes of the c ...
Archaeoglobus fulgidus, Archaeoglobus lithotrophicus, Archaeoglobus lithotrophicus TF-2, Archaeoglobus profundus, Archaeoglobus profundus DSM 5631
Arch. Microbiol.
163
112-118
1995
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5
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3
3
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3
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3
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3
3
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725983
Lehmacher
Cloning, sequencing and transc ...
Methanothermus fervidus, Methanothermus fervidus DSM 2088
Mol. Gen. Genet.
242
73-80
1994
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6
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486086
Schwrer
Formylmethanofuran:tetrahydrom ...
Archaeoglobus fulgidus, Archaeoglobus fulgidus VC-19 / DSM 4304
Arch. Microbiol.
159
225-232
1993
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2
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486087
Breitung
Salt dependence, kinetic prope ...
Methanopyrus kandleri
Eur. J. Biochem.
210
971-981
1992
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1
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3
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3
1
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1
5
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1
1
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2
1
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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11925
Breitung
N-Furfurylformamide as a pseud ...
Methanosarcina barkeri, Methanosarcina barkeri Fusaro / DSM 804, Methanothermobacter thermautotrophicus
FEBS Lett.
268
257-260
1990
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4
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14
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7
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7
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486088
DiMarco
The formylmethanofuran: tetrah ...
Methanothermobacter thermautotrophicus
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472-476
1990
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486089
Breitung
Formylmethanofuran: tetrahydro ...
Methanosarcina barkeri, Methanothermobacter thermautotrophicus
FEBS Lett.
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226-230
1990
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486084
Donnelly
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The role of formylmethanofuran ...
Methanothermobacter thermautotrophicus
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16652-16659
1986
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486085
Leigh
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Structure of methanofuran, the ...
Methanothermobacter thermautotrophicus
J. Am. Chem. Soc.
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3636-3640
1984
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