EC Number   |
Natural Substrates |
|---|
    1.17.4.1 | more |
RNR is an essential enzyme that provides dNTPs for DNA replication and repair, regulation in response to genotoxic stress, overview |
| 1.17.4.1 | more |
catalysis by a class I RNR begins when a cysteine residue in the alpha2 subunit is oxidized to a thiyl radical by a cofactor about 35 A away in the beta2 subunit. In a class Ia or Ib RNR, a stable tyrosyl radical is the C oxidant, whereas a MnIV/FeIII cluster serves this function in the class Ic enzyme from Chlamydia trachomatis |
| 1.17.4.1 | more |
class Ia and Ib RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor. Class II RNRs catalyze the same reaction but also convert nucleoside triphosphates to the correspondent 2'deoxy products, EC 1.17.4.2, overview |
| 1.17.4.1 | more |
class Ia RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor |
| 1.17.4.1 | more |
the enzyme catalyzes the conversion of nucleoside 5'-diphosphates, NDPs, to deoxynucleotides, dNDPs. The active site for NDP reduction resides in the alpha2 subunit, and the essential diferric-tyrosyl radical, Y122 radical, cofactor that initiates transfer of the radical to the active site cysteine in R2 (C439), 35A ° removed, is located in subunit beta2. The oxidation involves a hopping mechanism through aromatic amino acids, Y122, W48, and Y356 in subunit beta2 to Y731, Y730, and C439 in subunit alpha2, and a reversible proton-coupled electron transfer |
| 1.17.4.1 | nucleoside 5'-diphosphate + glutaredoxin |
class I RNRs |
| 1.17.4.1 | nucleoside 5'-diphosphate + glutaredoxin |
class Ia RNRs |
| 1.17.4.1 | nucleoside 5'-diphosphate + NrdH-redoxin |
only class Ib RNRs |
| 1.17.4.1 | nucleoside 5'-diphosphate + thioredoxin |
class I and class II RNRs |
| 1.17.4.1 | nucleoside 5'-diphosphate + thioredoxin |
class Ia RNRs |
