1.1.98.6: ribonucleoside-triphosphate reductase (formate)
This is an abbreviated version!
For detailed information about ribonucleoside-triphosphate reductase (formate), go to the full flat file.
Word Map on EC 1.1.98.6
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1.1.98.6
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glycyl
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s-adenosylmethionine
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formate-lyase
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deoxyribonucleotides
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oxygen-sensitive
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flavodoxins
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adomet
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2,3-aminomutase
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coproporphyrinogen
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radical-based
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thiyl
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homolytic
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benzylsuccinate
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datp-sepharose
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medicine
- 1.1.98.6
-
glycyl
- s-adenosylmethionine
- formate-lyase
- deoxyribonucleotides
-
oxygen-sensitive
- flavodoxins
- adomet
-
2,3-aminomutase
- coproporphyrinogen
-
radical-based
-
thiyl
-
homolytic
- benzylsuccinate
-
datp-sepharose
- medicine
Reaction
Synonyms
anaerobic ribonucleoside-triphosphate reductase, anaerobic ribonucleotide reductase, class III ribonucleoside-triphosphate reductase, nrdD
ECTree
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Cofactor
Cofactor on EC 1.1.98.6 - ribonucleoside-triphosphate reductase (formate)
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iron-sulfur centre
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activation of enzyme involves generation of a specific amino acid free radical that is dependent on a reduced Fe-S cluster and S-adenosylmethionine
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activation of enzyme involves generation of a specific amino acid free radical that is dependent on a reduced Fe-S cluster and S-adenosylmethionine
S-adenosyl-L-methionine
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S-adenosyl-L-methionine is directly reduced by the Fe-S center of the small subunits during the activation of the enzyme, resulting in methionine and glycyl radical formation. S-adenosyl-L-methionine binds to the small subunits with a Kd of 10 microM and a 1:1 stoichiometry. Dithiothreitol triggers the cleavage of S-adenosyl-L-methionine, leading glycyl radical formation. 3 methionines are formed per mol of protein
S-adenosyl-L-methionine
S-adenosylmethionine together with a metal participates in the generation of the radical required for the reduction of carbon 2' of the ribosyl moiety of CTP
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S-adenosyl-L-methionine is directly reduced by the Fe-S center of the small subunits during the activation of the enzyme
[4Fe-4S]-center
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the 17.5-kDa subunit contains a 4Fe-4S cluster that joins two peptides in a 35-kDa small homodimer (beta2)
[4Fe-4S]-center
the [4Fe-4S]+ form is extremely sensitive to oxygen and converted to [4Fe-4S]2+, [3Fe-4S]+/0, and to the stable [2Fe-2S]2+ form. The oxidized protein retains full activity. The [2Fe-2S] form of the protein can be converted into a [3Fe-4S] form during chromatography on dATP-Sepharose