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
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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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General Information
General Information on EC 2.1.1.245 - 5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase
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metabolism
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the enzyme reaction initiates the unusual biological organometallic reaction sequence that constitutes the Wood-Ljungdahl or reductive acetyl-CoA pathway
additional information
genes cdhD and cdhE encode the delta and gamma subunits of the C/Fe-S enzyme from the CO dehydrogenase complex of Methanosarcina thermophila, the complex comprises a nickel/iron-sulfur, Ni/Fe-S, enzyme containing alpha and epsilon subunits and a corrinoid/iron-sulfur, C/Fe-S, enzyme containing gamma and delta subunits. The C/Fe-S enzyme contains one molecule of factor III in the base-off form which facilitates reduction of the cobalt atom to the Co1+ redox state, which is a requirement for methylation. The gamma subunit CdhE contains the single 4Fe-4S center in the C/Fe-S enzyme, overview
additional information
genes cdhD and cdhE encode the delta and gamma subunits of the C/Fe-S enzyme from the CO dehydrogenase complex of Methanosarcina thermophila, the complex comprises a nickel/iron-sulfur, Ni/Fe-S, enzyme containing alpha and epsilon subunits and a corrinoid/iron-sulfur, C/Fe-S, enzyme containing gamma and delta subunits. The C/Fe-S enzyme contains one molecule of factor III in the base-off form which facilitates reduction of the cobalt atom to the Co1+ redox state, which is a requirement for methylation. The gamma subunit CdhE contains the single 4Fe-4S center in the C/Fe-S enzyme, overview
additional information
genes cdhD and cdhE encode the delta and gamma subunits of the C/Fe-S enzyme from the CO dehydrogenase complex of Methanosarcina thermophila, the complex comprises a nickel/iron-sulfur, Ni/Fe-S, enzyme containing alpha and epsilon subunits and a corrinoid/iron-sulfur, C/Fe-S, enzyme containing gamma and delta subunits. The C/Fe-S enzyme purified contains one molecule of factor III in the base-off form which facilitates reduction of the cobalt atom to the Co1+ redox state, which is a requirement for methylation. The gamma subunit CdhE contains the single 4Fe-4S center in the C/Fe-S enzyme
additional information
genes cdhD and cdhE encode the delta and gamma subunits of the C/Fe-S enzyme from the CO dehydrogenase complex of Methanosarcina thermophila, the complex comprises a nickel/iron-sulfur, Ni/Fe-S, enzyme containing alpha and epsilon subunits and a corrinoid/iron-sulfur, C/Fe-S, enzyme containing gamma and delta subunits. The C/Fe-S enzyme purified contains one molecule of factor III in the base-off form which facilitates reduction of the cobalt atom to the Co1+ redox state, which is a requirement for methylation. The gamma subunit CdhE contains the single 4Fe-4S center in the C/Fe-S enzyme
additional information
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loss of acetyl-CoA synthesis activity of the beta-subunit of the enzyme complex does not influence the gamma and delta subunit activities