EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.17.4.1 | ATP | binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP | Homo sapiens | |
1.17.4.1 | ATP | binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase | Saccharomyces cerevisiae | |
1.17.4.1 | ATP | binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase | Homo sapiens | |
1.17.4.1 | dATP | binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP | Homo sapiens | |
1.17.4.1 | dATP | binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase | Saccharomyces cerevisiae | |
1.17.4.1 | dATP | binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase | Homo sapiens | |
1.17.4.1 | dGTP | binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The O6 and protonated N1 of dGTP direct specificity for ADP | Homo sapiens | |
1.17.4.1 | dGTP | binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop. The O6 and protonated N1 of dGTP direct specificity for ADP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase | Saccharomyces cerevisiae | |
1.17.4.1 | dGTP | binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop. The O6 and protonated N1 of dGTP direct specificity for ADP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase | Homo sapiens | |
1.17.4.1 | dTTP | binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The 5-methyl, O4, and N3 groups of dTTP contributes to specificity for GDP | Homo sapiens | |
1.17.4.1 | dTTP | binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase | Saccharomyces cerevisiae | |
1.17.4.1 | dTTP | binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase | Homo sapiens |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.17.4.1 | expression in Escherichia coli BL-21 (DE3) | Saccharomyces cerevisiae |
1.17.4.1 | expression in Escherichia coli BL-21 (DE3) | Homo sapiens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.17.4.1 | D287A | the mutant enzyme (mutation in the ribonucleoside-diphosphate reductase large subunit RRM1) is deficient in allosteric regulation by dGTP and dTTP, but not ATP/dATP | Homo sapiens |
1.17.4.1 | D287A | the mutant enzyme is deficient in allosteric regulation by dGTP and dTTP, but not ATP/dATP | Homo sapiens |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.17.4.1 | Homo sapiens | P23921 | ribonucleoside-diphosphate reductase large subunit | - |
1.17.4.1 | Homo sapiens | P23921 and P31350 | P23921: ribonucleoside-diphosphate reductase large subunit RRM1, P31350: ribonucleoside-diphosphate reductase subunit RRM2 | - |
1.17.4.1 | Saccharomyces cerevisiae | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.17.4.1 | - |
Saccharomyces cerevisiae |
1.17.4.1 | - |
Homo sapiens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.17.4.1 | ADP + thioredoxin | - |
Saccharomyces cerevisiae | 2'-dADP + thioredoxin disulfide + H2O | - |
? | |
1.17.4.1 | ADP + thioredoxin | - |
Homo sapiens | 2'-dADP + thioredoxin disulfide + H2O | - |
? | |
1.17.4.1 | CDP + thioredoxin | - |
Homo sapiens | 2'-dCDP + thioredoxin disulfide + H2O | - |
? | |
1.17.4.1 | CDP + thioredoxin | CDP is the favored substrate. However, the kcat/Km values for ADP, GDP, and UDP are within 100-fold of the value for CDP | Saccharomyces cerevisiae | 2'-dCDP + thioredoxin disulfide + H2O | - |
? | |
1.17.4.1 | CDP + thioredoxin | for ATP-bound enzyme CDP is the favored substrate | Homo sapiens | 2'-dCDP + thioredoxin disulfide + H2O | - |
? | |
1.17.4.1 | GDP + thioredoxin | - |
Saccharomyces cerevisiae | 2'-dGDP + thioredoxin disulfide + H2O | - |
? | |
1.17.4.1 | GDP + thioredoxin | - |
Homo sapiens | 2'-dGDP + thioredoxin disulfide + H2O | - |
? | |
1.17.4.1 | UDP + thioredoxin | - |
Saccharomyces cerevisiae | 2'-dUDP + thioredoxin disulfide + H2O | - |
? | |
1.17.4.1 | UDP + thioredoxin | - |
Homo sapiens | 2'-dUDP + thioredoxin disulfide + H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.17.4.1 | class I ribonucleotide reductase | - |
Saccharomyces cerevisiae |
1.17.4.1 | class I ribonucleotide reductase | - |
Homo sapiens |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.17.4.1 | metabolism | the enzyme maintains balanced pools of deoxyribonucleotide substrates for DNA replication by converting ribonucleoside diphosphates to 2'-deoxyribonucleoside diphosphates | Saccharomyces cerevisiae |
1.17.4.1 | metabolism | the enzyme maintains balanced pools of deoxyribonucleotide substrates for DNA replication by converting ribonucleoside diphosphates to 2'-deoxyribonucleoside diphosphates | Homo sapiens |