Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.17.4.1 extracted from

  • Zhang, Z.; Yang, K.; Chen, C.C.; Feser, J.; Huang, M.
    Role of the C terminus of the ribonucleotide reductase large subunit in enzyme regeneration and its inhibition by Sml1 (2007), Proc. Natl. Acad. Sci. USA, 104, 2217-2222.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.17.4.1

Protein Variants

Protein Variants Comment Organism
C428S mutantion is lethal. Cells carrying both the C428S and the SX2S mutation of CX2C motif on plasmids are viable and form colonies with an efficiency similar to that of the wild-type control showing interallelic complementation Saccharomyces cerevisiae
C439S the C439S mutant of the Escherichia coli R1 is catalytically inactive in vitro Escherichia coli
additional information deletion of C-terminal domain of subunit R1 is lethal. Mutation of CX2C motif to SX2S results in viable, but slowly growing cells. Mutant cells exhibit a prolonged S phase Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
Sml1 inhibitor protein Sml1 competes with the C-terminal domain of subunit R1 for association with its N-terminal domain to hinder the accessibility of the CX2C motif to the active site for R1 regeneration during the catalytic cycle Saccharomyces cerevisiae
Sml1 protein a 104-residue Saccharomyces cerevisiae protein, inhibits ribonucleotide reductase activity by binding to the R1 subunit interacting with the N-terminal domain of R1, R1-NTD, which involves a conserved two-residue sequence motif in the R1-NTD, the Sml1-R1 interaction causes SML1-dependent lethality, overview Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus
-
 Escherichia coli 5634
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli the Sml1-R1 interaction causes SML1-dependent lethality, the CX2C motif of Rnr1 Is essential for viability. overview ?
-
 ?
ribonucleoside 5'-diphosphate + thioredoxin Escherichia coli
-
 2'-deoxyribonuleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the Sml1-R1 interaction causes SML1-dependent lethality, the CX2C motif of Rnr1 Is essential for viability. overview Escherichia coli ?
-
 ?
ribonucleoside 5'-diphosphate + thioredoxin
-
 Escherichia coli 2'-deoxyribonuleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
ribonucleoside 5'-diphosphate + thioredoxin at the completion of each turnover cycle, the active site of R1 becomes oxidized and subsequently regenerates by a cysteine pair at its C-terminal domain R1-CTD, that acts in trans to reduce the active site of its neighboring monomer, R1-CTD interacts with the N-terminal domain of R1, R1-NTD, which involves a conserved two-residue sequence motif in the R1-NTD, overview Escherichia coli 2'-deoxyribonuleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?

Subunits

Subunits Comment Organism
More C-terminal domain of subunit R1 acts in trans to reduce the active site of its neighbouring monomer and interacts with the N-terminal domain of neighbouring R1. Inhibitor protein Sml1 competes with the C-terminal domain of R1 for association with the N-terminal domain to hinder the accessibility of the CX2C motif to the active site for R1 regeneration during the catalytic cycle Saccharomyces cerevisiae
More 2 * R1 subunit + 2 * R2 subunit, cross-talk Between the C-terminus of one subunit R1 monomer and the active site of its neighboring monomer, overview Escherichia coli

Synonyms

Synonyms Comment Organism
ribonucleotide reductase
-
 Escherichia coli
RNR
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
thioredoxin
-
 Escherichia coli