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Literature summary for 1.17.4.1 extracted from

  • Seyedsayamdost, M.R.; Yee, C.S.; Stubbe, J.
    Use of 2,3,5-F(3)Y-beta2 and 3-NH(2)Y-alpha2 to study proton-coupled electron transfer in Escherichia coli ribonucleotide reductase (2011), Biochemistry, 50, 1403-1411.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.17.4.1

Activating Compound

Activating Compound Comment Organism Structure
ATP
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information pre-steady state kinetics, overview Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli 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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 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 Escherichia coli ?
-
 ?
additional information substrate is CDP with ATP as effector, detection of NH2Y radical intermediates capable of dNDP formation Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
tetramer alpha2beta2 Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.4
-
 assay at Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
6.5 9.2 stable intermediate formation, change in the rate-limiting step at elevated pH, profiles, overview Escherichia coli

General Information

General Information Comment Organism
additional information as the pH is elevated, the rate-determining step of RNR can be altered from a conformational change to proton-coupled electron transfer, and the altered driving force for F3Y oxidation, by residues adjacent to it in the pathway, is responsible for this change Escherichia coli