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Literature summary extracted from

  • Mamat, B.; Roth, A.; Grimm, C.; Ermler, U.; Tziatzios, C.; Schubert, D.; Thauer, R.K., Shima, S.
    Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship (2002), Protein Sci., 11, :2168-2178.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.101 expression in Escherichia coli Methanosarcina barkeri
2.3.1.101 expression in Escherichia coli Archaeoglobus fulgidus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.101 vapor diffusion method at 4°C, crystal structure at 1.9 A resolution Methanosarcina barkeri
2.3.1.101 vapor diffusion method at 4°C, crystal structure at 2.0 A resolution Archaeoglobus fulgidus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.1.101 K3PO4 0.01 M salt concentration is required for 50% activity at 37°C. 0.1 M salt concentration is required for 100% activity at 37°C Methanosarcina barkeri
2.3.1.101 K3PO4 0.1 M salt concentration is required for 50% activity at 83°C. 1.0 M salt concentration is required for 100% activity at 83°C Archaeoglobus fulgidus
2.3.1.101 K3PO4 1.0 M salt concentration is required for 50% activity at 89°C. 1.5 M salt concentration is required for 100% activity at 89°C Methanopyrus kandleri

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.101 Archaeoglobus fulgidus O28076
-
-
2.3.1.101 Methanopyrus kandleri Q49610
-
-
2.3.1.101 Methanopyrus kandleri DSM 6324 Q49610
-
-
2.3.1.101 Methanosarcina barkeri P55301
-
-
2.3.1.101 Methanosarcina barkeri DSM 804 P55301
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.101 methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin
-
 Methanopyrus kandleri formylmethanofuran + 5,6,7,8-tetrahydromethanopterin
-
 r
2.3.1.101 methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin
-
 Methanosarcina barkeri formylmethanofuran + 5,6,7,8-tetrahydromethanopterin
-
 r
2.3.1.101 methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin
-
 Archaeoglobus fulgidus formylmethanofuran + 5,6,7,8-tetrahydromethanopterin
-
 r
2.3.1.101 methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin
-
 Methanopyrus kandleri DSM 6324 formylmethanofuran + 5,6,7,8-tetrahydromethanopterin
-
 r
2.3.1.101 methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin
-
 Methanosarcina barkeri DSM 804 formylmethanofuran + 5,6,7,8-tetrahydromethanopterin
-
 r

Subunits

EC Number Subunits Comment Organism
2.3.1.101 dimer dimer and tetramer are about 20% and about 80%, respectively, in 20–100 mM potassium phosphate at pH 7.2. The ratio is independent of the buffer concentration. Oligomers larger than a tetramer can not be detected Methanosarcina barkeri
2.3.1.101 monomer monomer/dimer/tetramer equilibrium. Mostly in a monomeric state at a phosphate concentration of 100 mM and which tetramerizes only potassium phosphate concentrations above 400 mM Methanopyrus kandleri
2.3.1.101 tetramer dimer and tetramer are about 20% and about 80%, respectively, in 20–100 mM potassium phosphate at pH 7.2. The ratio is independent of the buffer concentration. Oligomers larger than a tetramer can not be detected Methanosarcina barkeri
2.3.1.101 tetramer the enzyme already reveals a tetrameric state at salt concentrations below 0.1 M Archaeoglobus fulgidus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.3.1.101 80
-
 50% inactivation after 20 min at 0.005 M K3PO4. No inactivation after 20 min at 0.05 M K3PO4 Archaeoglobus fulgidus
2.3.1.101 80
-
 50% inactivation after 20 min at 0.05 M K3PO4. No inactivation after 20 min at 0.5 M K3PO4 Methanosarcina barkeri
2.3.1.101 80
-
 50% inactivation after 20 min at 1.2 M K3PO4. No inactivation after 20 min at 1.5 M K3PO4 Methanopyrus kandleri