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Literature summary for 2.1.1.258 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
Search for more literature for 2.1.1.258

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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

Organism UniProt Comment Textmining
Moorella thermoacetica
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
homodimer x-ray crystallography Moorella thermoacetica

Synonyms

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00003
-
 methylcobalamin mutant enzyme N199A, at pH 8.4 and 55°C Moorella thermoacetica
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
0.05
-
 methylcobalamin wild type enzyme, at pH 8.4 and 55°C Moorella thermoacetica
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]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
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
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