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Literature summary extracted from

  • Zimanyi, C.M.; Chen, P.Y.; Kang, G.; Funk, M.A.; Drennan, C.L.
    Molecular basis for allosteric specificity regulation in class Ia ribonucleotide reductase from Escherichia coli (2016), eLife, 5, e07141 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.17.4.1 dATP the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell Escherichia coli
1.17.4.1 dGTP the binding of effector dGTP alters the active site to select for ADP and GDP. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell Escherichia coli
1.17.4.1 TTP the binding of effector TTP alters the active site to select for ADP and GDP. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.17.4.1 crystals are grown using the hanging drop vapor diffusion technique Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.17.4.1 ADP + thioredoxin Escherichia coli the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair 2'-dADP + thioredoxin disulfide + H2O
-
 ?
1.17.4.1 CDP + thioredoxin Escherichia coli the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair 2'-dCDP + thioredoxin disulfide + H2O
-
 ?
1.17.4.1 UDP + thioredoxin Escherichia coli the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair 2'-dUDP + thioredoxin disulfide + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.17.4.1 Escherichia coli P00452 and P69924 P00452: subunit NrdA, P69924: subunit NrdB
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.17.4.1
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.4.1 ADP + thioredoxin
-
 Escherichia coli 2'-dADP + thioredoxin disulfide + H2O
-
 ?
1.17.4.1 ADP + thioredoxin the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair Escherichia coli 2'-dADP + thioredoxin disulfide + H2O
-
 ?
1.17.4.1 CDP + thioredoxin
-
 Escherichia coli 2'-dCDP + thioredoxin disulfide + H2O
-
 ?
1.17.4.1 CDP + thioredoxin the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair Escherichia coli 2'-dCDP + thioredoxin disulfide + H2O
-
 ?
1.17.4.1 UDP + thioredoxin
-
 Escherichia coli 2'-dUDP + thioredoxin disulfide + H2O
-
 ?
1.17.4.1 UDP + thioredoxin the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair Escherichia coli 2'-dUDP + thioredoxin disulfide + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.17.4.1 class Ia RNR
-
 Escherichia coli
1.17.4.1 ribonucleotide reductase
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
1.17.4.1 physiological function the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair Escherichia coli