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EC Tree
IUBMB Comments Catalyses the transfer of a methyl group from the N5 group of methyltetrahydrofolate to the 5-methoxybenzimidazolylcobamide cofactor of a corrinoid/Fe-S protein. Involved, together with EC 1.2.7.4, anaerobic carbon-monoxide dehydrogenase and EC 2.3.1.169, CO-methylating acetyl-CoA synthase, in the reductive acetyl coenzyme A (Wood-Ljungdahl) pathway of autotrophic carbon fixation in various bacteria and archaea.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
a [methyl-Co(III) corrinoid Fe-S protein]
+
=
a [Co(I) corrinoid Fe-S protein]
+
Synonyms
methyltetrahydrofolate- and corrinoid-dependent methyltransferase,
more
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methyltetrahydrofo1ate:corrinoid/iron-sulfur protein methyltransferase
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methyltetrahydrofolate corrinoid-iron sulfur protein methyltransferase
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methyltetrahydrofolate, corrinoid ironsulfur protein methyltransferase
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methyltetrahydrofolate- and corrinoid-dependent methyltransferase
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase MeTr
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acsE
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methyltetrahydrofolate- and corrinoid-dependent methyltransferase
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methyltetrahydrofolate- and corrinoid-dependent methyltransferase
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-
-
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase
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-
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase
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MeTr
-
-
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a [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate = a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate
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-
-
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5-methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase
Catalyses the transfer of a methyl group from the N5 group of methyltetrahydrofolate to the 5-methoxybenzimidazolylcobamide cofactor of a corrinoid/Fe-S protein. Involved, together with EC 1.2.7.4, anaerobic carbon-monoxide dehydrogenase and EC 2.3.1.169, CO-methylating acetyl-CoA synthase, in the reductive acetyl coenzyme A (Wood-Ljungdahl) pathway of autotrophic carbon fixation in various bacteria and archaea.
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cobalamin + 5-methyltetrahydrofolate
methylcobalamin + tetrahydrofolate
hydroxocobalamin + 5-methyltetrahydrofolate
methylcobalamin + tetrahydrofolate
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-
-
-
r
hydroxycobalamin + 5-methyltetrahydrofolate
methylcobalamin + tetrahydrofolate
methylcobalamin + tetrahydrofolate
?
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-
-
?
methylcobalamin + tetrahydrofolate
hydroxocobalamin + 5-methyltetrahydrofolate
[Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate
[methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate
[methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate
[Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate
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-
-
-
r
additional information
?
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-
only the protonated enzyme form is active
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-
?
cobalamin + 5-methyltetrahydrofolate
methylcobalamin + tetrahydrofolate
-
reaction is pH dependent with the best pH of around 5.0
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-
?
cobalamin + 5-methyltetrahydrofolate
methylcobalamin + tetrahydrofolate
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reaction is pH dependent with the best pH of around 5.0
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-
?
hydroxycobalamin + 5-methyltetrahydrofolate
methylcobalamin + tetrahydrofolate
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-
-
-
?
hydroxycobalamin + 5-methyltetrahydrofolate
methylcobalamin + tetrahydrofolate
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-
-
-
?
methylcobalamin + tetrahydrofolate
hydroxocobalamin + 5-methyltetrahydrofolate
-
-
-
-
?
methylcobalamin + tetrahydrofolate
hydroxocobalamin + 5-methyltetrahydrofolate
-
-
-
-
r
[Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate
[methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate
-
-
-
-
?
[Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate
[methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate
-
-
-
-
?
[Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate
[methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate
-
-
-
-
?
[Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate
[methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate
-
-
-
-
r
[Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate
[methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate
-
-
-
?
[Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate
[methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate
-
-
-
-
?
[Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate
[methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate
the enzyme binds the protonated form of 5-methyltetrahydrofolate 10fold stronger than the unprotonated form
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r
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additional information
the enzyme lacks any metals
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4,4'-bis(1-(phenylamino)-8-naphthalenesulfonate)
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tetrahydrofolate
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competitive inhibitor
[methyl-Co(III) corrinoid Fe-S protein]
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competitive inhibitor
-
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0.002 - 0.01
5-methyltetrahydrofolate
2
hydroxocobalamin
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in 1 mM Tris-HCl (pH 7.6), at 25°C
0.058
hydroxycobalamin
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recombinant enzyme, in 0.1 M MES, at pH 5.1 and 25°C
0.665
methylcobalamin
-
in 1 mM Tris-HCl (pH 7.6), at 25°C
0.2 - 0.341
tetrahydrofolate
0.012 - 0.06
[Co(I) corrinoid Fe-S protein]
-
0.1
[methyl-Co(III) corrinoid Fe-S protein]
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Km above 0.1 mM, in 1 mM Tris-HCl (pH 7.6), at 25°C
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0.002
5-methyltetrahydrofolate
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in 50 mM MES, pH 5.1, at 25°C
0.01
5-methyltetrahydrofolate
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using hydroxocobalamin as cosubstrate, in 1 mM Tris-HCl (pH 7.6), at 25°C
0.01
5-methyltetrahydrofolate
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using [Co(I) corrinoid Fe-S protein] as cosubstrate, in 1 mM Tris-HCl (pH 7.6), at 25°C
0.0178
Cobalamin
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25°C, pH 5.1
0.06
Cobalamin
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25°C, pH 7.2
0.2
tetrahydrofolate
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Km above 0.2 mM, using [Co(I) corrinoid Fe-S protein] as cosubstrate, in 1 mM Tris-HCl (pH 7.6), at 25°C
0.341
tetrahydrofolate
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using hydroxocobalamin as cosubstrate, in 1 mM Tris-HCl (pH 7.6), at 25°C
0.012
[Co(I) corrinoid Fe-S protein]
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in 50 mM MES, pH 5.1, at 25°C
-
0.06
[Co(I) corrinoid Fe-S protein]
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in 1 mM Tris-HCl (pH 7.6), at 25°C
-
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1.5 - 14.7
5-methyltetrahydrofolate
1.1
hydroxocobalamin
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in 1 mM Tris-HCl (pH 7.6), at 25°C
77.6
hydroxycobalamin
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recombinant enzyme, in 0.1 M MES, at pH 5.1 and 25°C
0.00003 - 2.2
methylcobalamin
0.005 - 18
[Co(I) corrinoid Fe-S protein]
-
0.02
[methyl-Co(III) corrinoid Fe-S protein]
-
kcat below 0.02 s(-1), in 1 mM Tris-HCl (pH 7.6), at 25°C
-
1.5
5-methyltetrahydrofolate
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using hydroxocobalamin as cosubstrate, in 1 mM Tris-HCl (pH 7.6), at 25°C
14.7
5-methyltetrahydrofolate
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in 50 mM MES, pH 5.1, at 25°C
2.63
Cobalamin
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25°C, pH 5.1
37.2
Cobalamin
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25°C, pH 7.2
0.00003
methylcobalamin
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mutant enzyme N199A, at pH 8.4 and 55°C
0.05
methylcobalamin
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wild type enzyme, at pH 8.4 and 55°C
2.2
methylcobalamin
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in 1 mM Tris-HCl (pH 7.6), at 25°C
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
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1.1
[Co(I) corrinoid Fe-S protein]
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wild type enzyme, in 0.1 M potassium succinate, pH 5.0, 60 mM NaCl, at 25°C
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14.7
[Co(I) corrinoid Fe-S protein]
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in 50 mM MES, pH 5.1, at 25°C
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18
[Co(I) corrinoid Fe-S protein]
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in 1 mM Tris-HCl (pH 7.6), at 25°C
-
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450 - 10800
5-methyltetrahydrofolate
14.7
hydroxocobalamin
-
in 1 mM Tris-HCl (pH 7.6), at 25°C
1330
hydroxycobalamin
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recombinant enzyme, in 0.1 M MES, at pH 5.1 and 25°C
2.1
methylcobalamin
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in 1 mM Tris-HCl (pH 7.6), at 25°C
4.4 - 5.2
tetrahydrofolate
0.02 - 1600
[Co(I) corrinoid Fe-S protein]
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17.1
[methyl-Co(III) corrinoid Fe-S protein]
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in 1 mM Tris-HCl (pH 7.6), at 25°C
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450
5-methyltetrahydrofolate
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using hydroxocobalamin as cosubstrate, in 1 mM Tris-HCl (pH 7.6), at 25°C
10800
5-methyltetrahydrofolate
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using [Co(I) corrinoid Fe-S protein] as cosubstrate, in 1 mM Tris-HCl (pH 7.6), at 25°C
150
Cobalamin
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25°C, pH 5.1
620
Cobalamin
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25°C, pH 7.2
4.4
tetrahydrofolate
-
using hydroxocobalamin as cosubstrate, in 1 mM Tris-HCl (pH 7.6), at 25°C
5.2
tetrahydrofolate
-
using [Co(I) corrinoid Fe-S protein] as cosubstrate, in 1 mM Tris-HCl (pH 7.6), at 25°C
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
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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
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1600
[Co(I) corrinoid Fe-S protein]
-
in 1 mM Tris-HCl (pH 7.6), at 25°C
-
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0.026
4,4'-bis(1-(phenylamino)-8-naphthalenesulfonate)
-
at pH 5.8 and 25°C
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5.2 - 6.8
the forward and reverse reaction rates decrease as the pH is lowered
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4.8
-
calculated
4.8
-
isoelectric focusing
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brenda
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brenda
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brenda
formerly Clostridium thermoaceticum
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brenda
formerly Clostridium thermoaceticum
UniProt
brenda
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metabolism
the enzyme catalyzes a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation
metabolism
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the enzyme performs a key step in the Wood-Ljungdahl pathway of acetyl-CoA synthesis
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27000
2 * 27000, SDS-PAGE
28550
2 * 28550, recombinant enzyme, MALDI-TOF mass spectrometry
28640
2 * 28640, native enzyme, MALDI-TOF mass spectrometry
28641
2 * 28641, deduced from amino acid sequence
30000
-
2 * 30000, SDS-PAGE
31000
-
2 * 31000, calculated from amino acid sequence
58900
native enzyme, gel filtration
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homodimer
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2 * 30000, SDS-PAGE
homodimer
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2 * 31000, calculated from amino acid sequence
homodimer
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2 * 30000, SDS-PAGE
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homodimer
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2 * 31000, calculated from amino acid sequence
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homodimer
2 * 27000, SDS-PAGE
homodimer
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x-ray crystallography
homodimer
2 * 28550, recombinant enzyme, MALDI-TOF mass spectrometry
homodimer
2 * 28640, native enzyme, MALDI-TOF mass spectrometry
homodimer
2 * 28641, deduced from amino acid sequence
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hanging drop vapor diffusion method, using 9-15% (w/v) polyethylene glycol monomethyl ester 5000, 20-50 mM CaCl2, 20% (v/v) glycerol, and 50 mM HEPES, pH 7.5
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
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N199A
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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
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16
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the recombinant enzyme is not stable at 16°C or higher temperature
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amylose resin column chromatography, Ni-NTA column chromatography, Sephadex-G25 gel filtration, and Superdex 75 gel filtration
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DEAE column chromatography
phenyl Sepharose column chromatography and Q-Sepharose column chromatography
phenyl-Sepharose column chromatography
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expressed in Escherichia coli B834 cells
expressed in Escherichia coli Rosetta (DE3) pLysS cells
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expressed in Escherichia coli strain JM109
expression in Escherichia coli
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mutant enzyme N199A is expressed in Escherichia coli B834(DE3)pLysS cells
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Seravalli, J.; Zhao, S.; Ragsdale, S.W.
Mechanism of transfer of the methyl group from (6S)-methyltetrahydrofolate to the corrinoid/iron-sulfur protein catalyzed by the methyltransferase from Clostridium thermoaceticum: a key step in the Wood-Ljungdahl pathway of acetyl-CoA synthesis
Biochemistry
38
5728-5735
1999
Moorella thermoacetica
brenda
Zhao, S.; Roberts, D.; Ragsdale, S.
Mechanistic studies of the methyltransferase from Clostridium thermoaceticum: Origin of the pH dependence of the methyl group transfer from methyltetrahydrofolate to the corrinoid/iron-sulfur protein
Biochemistry
34
15075-15083
1995
Moorella thermoacetica
brenda
Zhao, S.; Ragsdale, S.
A conformational change in the methyltransferase from Clostridium thermoaceticum facilitates the methyl transfer from (6S)-methyltetrahydrofolate to the corrinoid/iron-sulfur protein in the acetyl-CoA pathway
Biochemistry
35
2476-2481
1996
Moorella thermoacetica
brenda
Roberts, D.; Zhao, S.; Doukov, T.; Ragsdale, S.
The reductive acetyl coenzyme A pathway: Sequence and heterologous expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum
J. Bacteriol.
176
6127-6130
1994
Moorella thermoacetica (Q46389)
brenda
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
J. Biol. Chem.
282
6609-6618
2007
Moorella thermoacetica
brenda
Alonso, H.; Cummins, P.; Gready, J.
Methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase (MeTr): Protonation state of the ligand and active-site residues
J. Phys. Chem. B
113
14787-14796
2009
Moorella thermoacetica (Q46389)
brenda
Zhu, X.; Gu, X.; Zhang, S.; Liu, Y.; Huang, Z.; Tan, X.
Efficient expression and purification of methyltransferase in acetyl-coenzyme a synthesis pathway of the human pathogen Clostridium difficile
Protein Expr. Purif.
78
86-93
2011
Clostridioides difficile, Clostridioides difficile 630
brenda
Doukov, T.; Seravalli, J.; Stezowski, J.; Ragsdale, S.
Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase
Structure
8
817-830
2000
Moorella thermoacetica (Q46389), Moorella thermoacetica
brenda
Zhu, X.; Li, T.; Gu, X.; Zhang, S.; Liu, Y.; Wang, Y.; Tan, X.
Structural and functional investigation into acetyl-coenzyme A synthase and methyltransferase from human pathogen Clostridium difficile
Metallomics
5
551-558
2013
Clostridioides difficile, Clostridioides difficile 630
brenda
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