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1.17.4.2: ribonucleoside-triphosphate reductase (thioredoxin)

This is an abbreviated version!
For detailed information about ribonucleoside-triphosphate reductase (thioredoxin), go to the full flat file.

Word Map on EC 1.17.4.2

Reaction

2'-deoxyribonucleoside 5'-triphosphate
+
thioredoxin disulfide
+
H2O
=
ribonucleoside 5'-triphosphate
+
thioredoxin

Synonyms

2'-deoxyribonucleoside-triphosphate:oxidized-thioredoxin 2'-oxidoreductase, adenosylcobalamin-dependent ribonucleoside-triphosphate reductase, class Ib ribonucleotide reductase, class Ib RNR, class II ribonucleotide reductase, class II RNR, class III ribonucleotide reductase, class III RNR, More, nrdD, nucleoside triphosphate reductase, ribonucleoside triphosphate reductase, ribonucleotide diphosphate reductase, ribonucleotide reductase, RNR, RNR class Ia, RNR2, RTPR

ECTree

     1 Oxidoreductases
         1.17 Acting on CH or CH2 groups
             1.17.4 With a disulfide as acceptor
                1.17.4.2 ribonucleoside-triphosphate reductase (thioredoxin)

Engineering

Engineering on EC 1.17.4.2 - ribonucleoside-triphosphate reductase (thioredoxin)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C644A
-
mutant enzyme is devoid of significant activity
C647A
-
mutant enzyme displays 2% of wild-type activity
C662A
-
mutant enzyme is devoid of significant activity
C665A
-
mutant enzyme is devoid of significant activity
C644A
-
mutant enzyme is devoid of significant activity
-
C647A
-
mutant enzyme displays 2% of wild-type activity
-
C662A
-
mutant enzyme is devoid of significant activity
-
C665A
-
mutant enzyme is devoid of significant activity
-
C119S
-
site-directed mutagenesis
C408A
-
only wild-type enzyme catalyzes epimerization of the (5'S)-[5'-2H1]- and (5'R)-[5'-2H1]-isotopomers of adenosylcobalamin, no activity of mutant enzyme
C408S
-
only wild-type enzyme catalyzes epimerization of the (5'S)-[5'-2H1]- and (5'R)-[5'-2H1]-isotopomers of adenosylcobalamin, no activity of mutant enzyme
additional information