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Literature summary extracted from

  • Knappenberger, A.J.; Ahmad, M.F.; Viswanathan, R.; Dealwis, C.G.; Harris, M.E.
    Nucleoside analogue triphosphates allosterically regulate human ribonucleotide reductase and identify chemical determinants that drive substrate specificity (2016), Biochemistry, 55, 5884-5896 .
    View publication on PubMed

Activating Compound

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

Cloned(Commentary)

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

Protein Variants

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

Organism

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
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.17.4.1
-
Saccharomyces cerevisiae
1.17.4.1
-
Homo sapiens

Substrates and Products (Substrate)

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
-
?

Synonyms

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

General Information

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