2.1.1.245: 5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase
This is an abbreviated version!
For detailed information about 5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.245
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2.1.1.245
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methanogen
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metr
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methanosarcina
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clostridium
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thermoaceticum
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ch3-h4folate
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n5-methyl
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pka
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cobalt
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ragsdale
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acetyl-enzyme
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h4folate
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barkeri
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thermophila
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ni
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cfesp
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exafs
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unprotonated
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pre-steady-state
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methane
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xanes
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cobiamide
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stopped-flow
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multienzyme
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shoemaker
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tetrahedral
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electrophilic
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companion
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cobalamin-dependent
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a-cluster
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organometallic
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h2o
- 2.1.1.245
-
methanogen
- metr
-
methanosarcina
- clostridium
- thermoaceticum
-
ch3-h4folate
-
n5-methyl
- pka
- cobalt
-
ragsdale
-
acetyl-enzyme
-
h4folate
- barkeri
- thermophila
- ni
-
cfesp
-
exafs
-
unprotonated
-
pre-steady-state
- methane
-
xanes
-
cobiamide
-
stopped-flow
-
multienzyme
-
shoemaker
-
tetrahedral
-
electrophilic
-
companion
-
cobalamin-dependent
-
a-cluster
-
organometallic
- h2o
Reaction
Synonyms
AcdS, acetyl-CoA decarbonylase/synthase complex, C/Fe-S enzyme, cdhD, CdhD1, cdhE, CH3-H4pteridine:cob(I)amide-protein methyltransferase, methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase, MeTr
ECTree
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Reaction
Reaction on EC 2.1.1.245 - 5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase
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a [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrosarcinapterin = a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrosarcinapterin
a [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrosarcinapterin = a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrosarcinapterin
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a [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrosarcinapterin = a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrosarcinapterin
random Bi-Bi mechanism of transfer of the methyl group from (6S)-methyltetrahydrofolate to the corrinoid/iron-sulfur protein: CH3-H4folate binds to MeTr in the unprotonated form and then undergoes rapid protonation. This protonation enhances the electrophilicity of the methyl group, in agreement with a 10fold increase in the pKa at N5 of CH3-H4folate. Next, the Co(I)-CFeSP attacks the methyl group in a rate-limiting SN2 reaction to form methylcob(III)amide. Finally, the products randomly dissociate. A pH-dependent conformational change is required for methyl transfer in the forward and reverse directions, a rate-limiting ionization of MeTr, not of CH3-H4folate, is responsible for the pH dependence of the methyl transfer reaction
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