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
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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
Carbon fixation pathways in prokaryotes
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Microbial metabolism in diverse environments
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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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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
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
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-
-
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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
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-
-
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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
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r
additional information
?
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-
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
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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
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in 1 mM Tris-HCl (pH 7.6), at 25C
0.058
hydroxycobalamin
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recombinant enzyme, in 0.1 M MES, at pH 5.1 and 25C
0.665
methylcobalamin
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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]
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Km above 0.1 mM, in 1 mM Tris-HCl (pH 7.6), at 25C
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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
Clostridioides 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]
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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
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in 1 mM Tris-HCl (pH 7.6), at 25C
5976
1330
hydroxycobalamin
Clostridioides difficile
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recombinant enzyme, in 0.1 M MES, at pH 5.1 and 25C
5159
2.1
methylcobalamin
Moorella thermoacetica
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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
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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
27000
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2 * 27000, SDS-PAGE
28000
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2 * 28000
28550
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2 * 28550, recombinant enzyme, MALDI-TOF mass spectrometry
28640
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2 * 28640, native enzyme, MALDI-TOF mass spectrometry
28641
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2 * 28641, deduced from amino acid sequence
30000
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2 * 30000, SDS-PAGE
31000
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2 * 31000, calculated from amino acid sequence
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
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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
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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
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expressed in Escherichia coli strain JM109
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expression in Escherichia coli
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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
Show AA Sequence (124 entries)
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