Information on EC 2.1.1.258 - 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.258
-
RECOMMENDED NAME
GeneOntology No.
5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate = a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
reductive acetyl coenzyme A pathway I (homoacetogenic bacteria)
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-
reductive acetyl coenzyme A pathway II (autotrophic methanogens)
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reductive acetyl coenzyme A pathway
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Carbon fixation pathways in prokaryotes
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
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, carbon-monoxide dehydrogenase (ferredoxin) 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.
CAS REGISTRY NUMBER
COMMENTARY hide
144114-19-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Peptoclostridium difficile
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cobalamin + 5-methyltetrahydrofolate
methylcobalamin + tetrahydrofolate
show the reaction diagram
hydroxocobalamin + 5-methyltetrahydrofolate
methylcobalamin + tetrahydrofolate
show the reaction diagram
-
-
-
-
r
hydroxycobalamin + 5-methyltetrahydrofolate
methylcobalamin + tetrahydrofolate
show the reaction diagram
methylcobalamin + tetrahydrofolate
?
show the reaction diagram
-
-
-
-
?
methylcobalamin + tetrahydrofolate
cobalamin + 5-methyltetrahydrofolate
show the reaction diagram
-
-
-
-
?
methylcobalamin + tetrahydrofolate
hydroxocobalamin + 5-methyltetrahydrofolate
show the reaction diagram
-
-
-
-
r
[Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate
[methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate
show the reaction diagram
[methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate
[Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
only the protonated enzyme form is active
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-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cobalamin
-
dependent on
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the enzyme lacks any metals
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4,4'-bis(1-(phenylamino)-8-napthalenesulfonate)
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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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 0.01
5-methyltetrahydrofolate
0.0178 - 0.06
Cobalamin
2
hydroxocobalamin
-
in 1 mM Tris-HCl (pH 7.6), at 25C
0.058
hydroxycobalamin
Peptoclostridium difficile
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recombinant enzyme, in 0.1 M MES, at pH 5.1 and 25C
0.665
methylcobalamin
-
in 1 mM Tris-HCl (pH 7.6), at 25C
0.2 - 0.341
tetrahydrofolate
0.012 - 0.06
[Co(I) corrinoid Fe-S protein]
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0.1
[methyl-Co(III) corrinoid Fe-S protein]
-
Km above 0.1 mM, in 1 mM Tris-HCl (pH 7.6), at 25C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5 - 14.7
5-methyltetrahydrofolate
2.63 - 37.2
Cobalamin
1.1
hydroxocobalamin
Moorella thermoacetica
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in 1 mM Tris-HCl (pH 7.6), at 25C
77.6
hydroxycobalamin
Peptoclostridium difficile
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recombinant enzyme, in 0.1 M MES, at pH 5.1 and 25C
0.00003 - 2.2
methylcobalamin
0.005 - 18
[Co(I) corrinoid Fe-S protein]
-
0.02
[methyl-Co(III) corrinoid Fe-S protein]
Moorella thermoacetica
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kcat below 0.02 s(-1), in 1 mM Tris-HCl (pH 7.6), at 25C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
450 - 10800
5-methyltetrahydrofolate
1373
150 - 620
Cobalamin
971
14.7
hydroxocobalamin
Moorella thermoacetica
-
in 1 mM Tris-HCl (pH 7.6), at 25C
5976
1330
hydroxycobalamin
Peptoclostridium difficile
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recombinant enzyme, in 0.1 M MES, at pH 5.1 and 25C
5159
2.1
methylcobalamin
Moorella thermoacetica
-
in 1 mM Tris-HCl (pH 7.6), at 25C
4270
4.4 - 5.2
tetrahydrofolate
207
0.02 - 1600
[Co(I) corrinoid Fe-S protein]
10400
17.1
[methyl-Co(III) corrinoid Fe-S protein]
Moorella thermoacetica
-
in 1 mM Tris-HCl (pH 7.6), at 25C
19649
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026
4,4'-bis(1-(phenylamino)-8-napthalenesulfonate)
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at pH 5.8 and 25C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2 - 6.8
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the forward and reverse reaction rates decrease as the pH is lowered
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58900
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native enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16
Peptoclostridium difficile
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the recombinant enzyme is not stable at 16C or higher temperature
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amylose resin column chromatography, Ni-NTA column chromatography, Sephadex-G25 gel filtration, and Superdex 75 gel filtration
Peptoclostridium difficile
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DEAE column chromatography
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phenyl Sepharose column chromatography and Q-Sepharose column chromatography
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phenyl-Sepharose column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli B834 cells
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expressed in Escherichia coli Rosetta (DE3) pLysS cells
Peptoclostridium difficile
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expressed in Escherichia coli strain JM109
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expression in Escherichia coli
Peptoclostridium difficile
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mutant enzyme N199A is expressed in Escherichia coli B834(DE3)pLysS cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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