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Literature summary extracted from
- Formation and function of the manganese(IV)/iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase (2008), Biochemistry, 47, 13736-13744.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.17.4.1 | additional information | enzyme activation mechanism and kinetics, overview | Escherichia coli |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.17.4.1 | Fe2+ | assembly, maintenance, and role in catalysis of the Fe2 III/III-Y radical cofactor of Ecbeta2 subunit, structure modelling, detailed overview | Escherichia coli |  |
| 1.17.4.1 | Fe2+ | unusual cofactor instead of Fe-Fe cofactor in other RNRs. Assembly, maintenance, and role in catalysis of the MnIV/FeIII cofactor of Ctbeta2 subunit, structure modelling, detailed overview | Chlamydia trachomatis | |
| 1.17.4.1 | Mn2+ | unusual cofactor instead of Fe-Fe cofactor in other RNRs. Assembly, maintenance, and role in catalysis of the MnIV/FeIII cofactor of Ctbeta2 subunit, structure modelling, detailed overview | Chlamydia trachomatis | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.17.4.1 | additional information | Escherichia coli | ribonucleotide reductases catalyze the reduction of ribonucleotides to deoxyribonucleotides for DNA synthesis | ? | - |
? | |
| 1.17.4.1 | additional information | Chlamydia trachomatis | ribonucleotide reductases catalyze the reduction of ribonucleotides to deoxyribonucleotides for DNA synthesis | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.17.4.1 | Chlamydia trachomatis | O84835 | - |
- |
| 1.17.4.1 | Escherichia coli | P69924 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.17.4.1 | additional information | ribonucleotide reductases catalyze the reduction of ribonucleotides to deoxyribonucleotides for DNA synthesis | Escherichia coli | ? | - |
? | |
| 1.17.4.1 | additional information | ribonucleotide reductases catalyze the reduction of ribonucleotides to deoxyribonucleotides for DNA synthesis | Chlamydia trachomatis | ? | - |
? | |
| 1.17.4.1 | additional information | the RNR reaction involves replacement by hydrogen of the hydroxyl group on the 2'-carbon of the nucleoside diphosphate substrate. This chemically difficult replacement occurs by a free-radical mechanism. The enzyme employs a heterobinuclear MnIV/FeIII cluster for radical initiation. In essence, the MnIV ion of the cluster functionally replaces the Y radical of the conventional class I RNR. The Ct beta2 protein also autoactivates by reaction of its reduced MnII/FeII metal cluster with O2. In this reaction, an unprecedented MnIV/FeIV intermediate accumulates almost stoichiometrically and decays by one-electron reduction of the FeIV site. This reduction is mediated by the near-surface residue, Y222, overview | Escherichia coli | ? | - |
? | |
| 1.17.4.1 | additional information | the RNR reaction involves replacement by hydrogen of the hydroxyl group on the 2'-carbon of the nucleoside diphosphate substrate. This chemically difficult replacement occurs by a free-radical mechanism. The enzyme employs a heterobinuclear MnIV/FeIII cluster for radical initiation. In essence, the MnIV ion of the cluster functionally replaces the Y radical of the conventional class I RNR. The Ct beta2 protein also autoactivates by reaction of its reduced MnII/FeII metal cluster with O2. In this reaction, an unprecedented MnIV/FeIV intermediate accumulates almost stoichiometrically and decays by one-electron reduction of the FeIV site. This reduction is mediated by the near-surface residue, Y222, overview | Chlamydia trachomatis | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.17.4.1 | More | interaction of the alpha2 and beta2 subunits during the reaction, comparison to the RNR from Chlamydia trachomatis, overview | Escherichia coli |
| 1.17.4.1 | More | interaction of the alpha2 and beta2 subunits during the reaction, comparison to the RNR from Escherichia coli, overview | Chlamydia trachomatis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.17.4.1 | class I RNR | - |
Escherichia coli |
| 1.17.4.1 | class I RNR | - |
Chlamydia trachomatis |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.17.4.1 | Fe2 III/III-Y radical cofactor | assembly, maintenance, and role in catalysis of the Fe2 III/III-Y radical cofactor of Ecbeta2 subunit, structure modelling, detailed overview | Escherichia coli | |
| 1.17.4.1 | Mn/Fe redox cofactor | unusual cofactor instead of Fe-Fe cofactor in other RNRs. Assembly, maintenance, and role in catalysis of the MnIV/FeIII cofactor of Ctbeta2 subunit, structure modelling, detailed overview | Chlamydia trachomatis |
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