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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Engineering
Engineering on EC 1.1.98.6 - ribonucleoside-triphosphate reductase (formate)
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C644A
mutation in a residue of the Zn(Cys)4 center, almost complete loss of activity due to inability to generate the catalytically essential glycyl radical
C647A
mutation in a residue of the Zn(Cys)4 center, almost complete loss of activity due to inability to generate the catalytically essential glycyl radical
C662A
mutation in a residue of the Zn(Cys)4 center, almost complete loss of activity due to inability to generate the catalytically essential glycyl radical
C665A
mutation in a residue of the Zn(Cys)4 center, almost complete loss of activity due to inability to generate the catalytically essential glycyl radical
C260S
Tequatrovirus T4
activity comparable to wild-type, mutant is able to undergo truncation at the site of the glycyl radical when the radical-containing enzyme is exposed to oxygen
C290S
C453S
Tequatrovirus T4
activity comparable to wild-type, mutant is able to undergo truncation at the site of the glycyl radical when the radical-containing enzyme is exposed to oxygen
C579S
Tequatrovirus T4
mutant is able to undergo truncation at the site of the glycyl radical when the radical-containing enzyme is exposed to oxygen
C79S
Tequatrovirus T4
residue participates in the actual reduction of the substrate. Mutant is able to undergo truncation at the site of the glycyl radical when the radical-containing enzyme is exposed to oxygen
G580A
Tequatrovirus T4
oxygen-dependent cleavage is not possible in this mutant since no radical can be formed at Ala580
Tequatrovirus T4
mutation in conserved residua, less than 10% of wild-type activity