Application | Comment | Organism |
---|---|---|
medicine | the enzyme is a target for cancer therapy | Saccharomyces cerevisiae |
Cloned (Comment) | Organism |
---|---|
expression of His-tagged subunits R2 and R4 in Escherichia coli strain BL21(DE3) | Saccharomyces cerevisiae |
Crystallization (Comment) | Organism |
---|---|
purified enzyme, formed by recombinant subunits R2 and R4, complexed with inhibitor peptide P7 or peptide Fmoc-P6, 20 mg/ml protein in 0.1 M HEPES, pH 7.5, with 20 mM TTP, 5% glycerol, 5mM DTT, 0.1 M KCL, and 25 mm MgCl2, is mixed with a reservoir solution containing 20-25% PEG 3350, 0.2 M NaCl, and 100 mM HEPES, pH 7.5, soaking of crystals for 4 h in reservoir solution with added inhibitor peptide P6 or P7, followed by soaking of crystals in 25% PEG 3350, 0.2 M NaCl, and 100 mM HEPES, pH 7.5, supplemented with 15% glycerol, X-ray diffraction structure determination and analysis at 2.6 and 2.5 A resolution, respectively | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of heterochimeric enzymes as heterocomplexes containing mammalian R2 C-terminal heptapeptide P7, Ac-1FTLDADF7, and its peptidomimetic P6, 1Fmoc(Me)PhgLDChaDF7, bound to Saccharomyces cerevisiae R1, ScR1, overview | Saccharomyces cerevisiae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
mammalian R2 C-terminal heptapeptide P7 | Ac-1FTLDADF7, the inhibitor binds at bind at a contiguous site containing residues that are highly conserved among eukaryotes, binding structure, overview | Saccharomyces cerevisiae | |
peptide P6 | 1Fmoc(Me)PhgLDChaDF7, the inhibitor binds at a contiguous site containing residues that are highly conserved among eukaryotes. The Fmoc group in P6 peptide forms several hydrophobic interactions that contribute to its enhanced potency in binding to ScR1, binding structure, overview | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
GDP + thioredoxin | Saccharomyces cerevisiae | - |
2'-deoxyGDP + thioredoxin disulfide + H2O | - |
? | |
ribonucleoside diphosphate + thioredoxin | Saccharomyces cerevisiae | - |
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P21524 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged subunits R2 and R4 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
GDP + thioredoxin | - |
Saccharomyces cerevisiae | 2'-deoxyGDP + thioredoxin disulfide + H2O | - |
? | |
ribonucleoside diphosphate + thioredoxin | - |
Saccharomyces cerevisiae | 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | the enzyme activity requires formation of a complex between subunits R1 and R2 in which the R2 C-terminal peptide binds to R1 | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
ribonucleotide reductase | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
thioredoxin | - |
Saccharomyces cerevisiae |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.0026 | - |
yeast enzyme | Saccharomyces cerevisiae | peptide Fmoc-P6 | |
0.031 | - |
yeast enzyme | Saccharomyces cerevisiae | peptide P7 |