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Literature summary extracted from

  • Ahmad, M.F.; Kaushal, P.S.; Wan, Q.; Wijerathna, S.R.; An, X.; Huang, M.; Dealwis, C.G.
    Role of arginine 293 and glutamine 288 in communication between catalytic and allosteric sites in yeast ribonucleotide reductase (2012), J. Mol. Biol., 419, 315-329.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.17.4.1
-
 Saccharomyces cerevisiae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.17.4.1 structures of mutanr R293A complexed with dGTP and AMPPNP-CDP reveal that ADP is not bound at the catalytic site, and CDP binds farther from the catalytic site compared to wild type Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
1.17.4.1 Q288A mutation causes severe S phase defects in cells that use the enzyme as the sole source of of ribonucleoside diphosphate activity. Compared to the wild-type enzyme activity, Q288A mutants show 15% of ADP reduction, whereas they show 23% of CDP reduction. There is a 6fold loss of affinity for ADP binding and a 2fold loss of affinity for CDP. Q288A can support mitotic growth, albeit with a severe S phase defect Saccharomyces cerevisiae
1.17.4.1 R293A mutation causes lethality in cells that use the enzyme as the sole source of ribonucleoside diphosphate activity. Compared to the wild-type enzyme activity, R293A mutants show 4% of ADP reduction, whereas they show 20% CDP reduction. The mutant is unable to bind ADP and binds CDP with 2fold lower affinity compared to wild-type. X-ray structures of R293A complexed with dGTP and AMPPNP reveal that ADP is not bound at the catalytic site, and CDP binds farther from the catalytic site compared to wild type. R293A cannot support mitotic growth Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
1.17.4.1 Saccharomyces cerevisiae P21524 large subunit 1
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.17.4.1 10000
-
 substrate ADP, mutant R293A, pH 7.6, 30°C Saccharomyces cerevisiae
1.17.4.1 40000
-
 substrate ADP, mutant Q288A, pH 7.6, 30°C Saccharomyces cerevisiae
1.17.4.1 50000
-
 substrate CDP, mutant R293A, pH 7.6, 30°C Saccharomyces cerevisiae
1.17.4.1 60000
-
 substrate CDP, mutant Q288A, pH 7.6, 30°C Saccharomyces cerevisiae
1.17.4.1 190000
-
 substrate CDP, wild-type, pH 7.6, 30°C Saccharomyces cerevisiae
1.17.4.1 258000
-
 substrate ADP, wild-type, pH 7.6, 30°C Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.4.1 ADP + dithiothreitol
-
 Saccharomyces cerevisiae 2'-dADP + oxidized dithiothreitol + H2O
-
 ?
1.17.4.1 CDP + dithiothreitol
-
 Saccharomyces cerevisiae 2'-dCDP + oxidized dithiothreitol + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.17.4.1 RNR1 rRibonucleoside-diphosphate reductase large chain 1
-
 Saccharomyces cerevisiae