Information on EC 2.3.1.101 - formylmethanofuran-tetrahydromethanopterin N-formyltransferase and Organism(s) Methanopyrus kandleri and UniProt Accession Q49610
for references in articles please use BRENDA:EC2.3.1.101
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potassium cyclic 2,3-diphosphoglycerate required for activity at 1 M, can be substituted by other salts with strongly hydrated anions, especially by K+, the enzyme is inactive and thermolabile, and changes the oligomerization state at low salt concentrations
required for activity at 1 M, can be substituted by other salts with strongly hydrated anions, especially by potassium cyclic 2,3-diphosphoglycerate, the enzyme is inactive and thermolabile, and changes the oligomerization state at low salt concentrations
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
required for activity at 1 M, can be substituted by other salts with strongly hydrated anions, especially by K+, the enzyme is inactive and thermolabile, and changes the oligomerization state at low salt concentrations
composed of two dimers, each subunit is subdivided into two tightly associated lobes both consisting of a predominantly antiparallel beta sheet flanked by alpha helices forming an alpha/beta sandwich structure, amino acid composition
structure analysis, at low salt conditions the enzyme is in an equilibrium of dimer, trimer and tetramer, the latter being the active and most thermostable enzyme form, the dimer is also active, but the monomer is inactive
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
hanging-drop vapor-diffusion method. Crystal structure at 2.0 A resolution of formyltransferase from in ternary complex with its substrates formylmethanofuran and tetrahydromethanopterin and products methanofuran and formyl-tetrahydromethanopterin. Methanofuran is embedded in an elongated cleft at the homodimer interface and fixed by multiple hydrophobic interactions. Tetrahydromethanopterin is weakly bound in a shallow and wide cleft that provides two binding sites
at cyclic 2,3-diphosphoglycerate concentrations prevailing in the cells of Methanopyrus kandleri the enzyme is completely thermostable. At molar concentrations also the potassium salts of phosphate and of 2,3-bisphosphoglycerate, the biosynthetic precursor of cyclic 2,3-diphosphoglycerate confer thermostability to the enzymes
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
at cyclic 2,3-diphosphoglycerate concentrations prevailing in the cells of Methanopyrus kandleri the enzyme is completely thermostable. At molar concentrations also the potassium salts of phosphate and of 2,3-bisphosphoglycerate, the biosynthetic precursor of cyclic 2,3-diphosphoglycerate confer thermostability to the enzymes
presence of salts, 1.5 M, required for optimal stabilization, order of efficiency in protecting the enzyme from heat inactivation at 90°C: K2HPO4, (NH4)2SO4, KCl, NH4Cl, NaCl, Na2SO4, Na2HPO4
Salt dependence, kinetic properties and catalytic mechanism of N-formylmethanofuran:tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleri
Formylmethanofuran:tetrahydromethanopterin formyltransferase (Ftr) from the hyperthermophilic Methanopyrus kandleri. Cloning, sequencing and functional expression of the ftr gene and one-step purification of the enzyme overproduced in Escherichia coli