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

Reaction

ribonucleoside 5'-triphosphate
+
formate
=
2'-deoxyribonucleoside 5'-triphosphate
+
CO2
+
H2O

Synonyms

anaerobic ribonucleoside-triphosphate reductase, anaerobic ribonucleotide reductase, class III ribonucleoside-triphosphate reductase, nrdD

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.98 With other, known, physiological acceptors
                1.1.98.6 ribonucleoside-triphosphate reductase (formate)

Engineering

Engineering on EC 1.1.98.6 - ribonucleoside-triphosphate reductase (formate)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
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
C543S
residue is essential for formation of the glycyl radical
C546S
residue is essential for formation of the glycyl radical
C561S
residue is essential for formation of the glycyl radical
C564S
residue is essential for formation of the glycyl radical
C579S
mutant is able to undergo truncation at the site of the glycyl radical when the radical-containing enzyme is exposed to oxygen
C79S
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
oxygen-dependent cleavage is not possible in this mutant since no radical can be formed at Ala580
N311A
about 20% of wild-type activtiy
N311C
less than 1% of wild-type activtiy
N78A
less than 10% of wild-type activtiy
N78A/N311A
less than 1% of wild-type activtiy
N78C
1% of wild-type activtiy
N78D
1% of wild-type activtiy