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Literature summary extracted from

  • Doukov, T.; Hemmi, H.; Drennan, C.; Ragsdale, S.
    Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer: Role of an active site asparagine residue in activation of methyl transfer by methyltransferases (2007), J. Biol. Chem., 282, 6609-6618.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.258 mutant enzyme N199A is expressed in Escherichia coli B834(DE3)pLysS cells Moorella thermoacetica

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.258 wild type and mutant enzyme in complex with 5-methyltetrahydrofolate, hanging drop vapor diffusion method, using 8-15% (w/v) polyethylene glycol monomethyl ether 5000, 20-50 mM calcium acetate, 50 mM HEPES, pH 7.5, and 20% (v) glycerol Moorella thermoacetica

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.258 N199A the mutant exhibits about 20fold weakened affinity for 5-methyltetraydrofolate but a much more marked 20000-40000fold effect on catalysis as compared to the wild type enzyme Moorella thermoacetica

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.258 Moorella thermoacetica
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.258 phenyl-Sepharose column chromatography Moorella thermoacetica

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.258 methylcobalamin + tetrahydrofolate
-
 Moorella thermoacetica hydroxocobalamin + 5-methyltetrahydrofolate
-
 ?
2.1.1.258 [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate
-
 Moorella thermoacetica [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.258 homodimer x-ray crystallography Moorella thermoacetica

Synonyms

EC Number Synonyms Comment Organism
2.1.1.258 methyltetrahydrofolate corrinoid-iron sulfur protein methyltransferase
-
 Moorella thermoacetica
2.1.1.258 MeTr
-
 Moorella thermoacetica

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.1.258 0.00003
-
 methylcobalamin mutant enzyme N199A, at pH 8.4 and 55°C Moorella thermoacetica
2.1.1.258 0.005
-
 [Co(I) corrinoid Fe-S protein] mutant enzyme N199A, in 0.1 M potassium succinate, pH 5.0, 60 mM NaCl, at 25°C Moorella thermoacetica
2.1.1.258 0.05
-
 methylcobalamin wild type enzyme, at pH 8.4 and 55°C Moorella thermoacetica
2.1.1.258 1.1
-
 [Co(I) corrinoid Fe-S protein] wild type enzyme, in 0.1 M potassium succinate, pH 5.0, 60 mM NaCl, at 25°C Moorella thermoacetica

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.1.1.258 0.02
-
 [Co(I) corrinoid Fe-S protein] mutant enzyme N199A, in 0.1 M potassium succinate, pH 5.0, 60 mM NaCl, at 25°C Moorella thermoacetica
2.1.1.258 500
-
 [Co(I) corrinoid Fe-S protein] wild type enzyme, in 0.1 M potassium succinate, pH 5.0, 60 mM NaCl, at 25°C Moorella thermoacetica