protein

Recombinant Escherichia coli Ribonucleoside-diphosphate reductase 1 subunit beta

MBS1037102

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Escherichia coli Ribonucleoside-diphosphate reductase 1 subunit beta

Ribonucleoside-diphosphate reductase 1 subunit beta

Protein B2; Protein R2; Ribonucleotide reductase 1

ribonucleoside-diphosphate reductase 1, beta subunit, ferritin-like protein; Ribonucleoside-diphosphate reductase 1 subunit beta; ribonucleoside-diphosphate reductase 1, beta subunit, ferritin-like protein; Protein B2; Protein R2; Ribonucleotide reductase 1

nrdB

nrdB; nrdB; ECK2227; ftsB; JW2229; ftsB

RIR2_ECOLI

E Coli or Yeast or Baculovirus or Mammalian Cell

2-376

376

AYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKL
IEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLK
YQTLLDSIQGRSPNVALLPLISIPELETWVETWAFSETI
HSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSY
YDELIEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYL
CLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLI
ARDEALHLTGTQHMLNLLRSG

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2 contains the tyrosyl radical required for catalysis.

Primary structure of the Escherichia coli ribonucleoside diphosphate reductase operon.Carlson J., Fuchs J.A., Messing J.Proc. Natl. Acad. Sci. U.S.A. 81:4294-4297(1984) Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features.Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.DNA Res. 4:91-113(1997) The complete genome sequence of Escherichia coli K-12.Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.Science 277:1453-1462(1997) Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.Mol. Syst. Biol. 2:E1-E5(2006) Cloning, overproduction, and purification of the B2 subunit of ribonucleoside-diphosphate reductase.Salowe S.P., Stubbe J.J. Bacteriol. 165:363-366(1986) Three-dimensional structure of the free radical protein of ribonucleotide reductase.Nordlund P., Sjoeberg B.-M., Eklund H.Nature 345:593-598(1990) Structure and function of the Escherichia coli ribonucleotide reductase protein R2.Nordlund P., Eklund H.J. Mol. Biol. 232:123-164(1993) Crystal structure of reduced protein R2 of ribonucleotide reductase the structural basis for oxygen activation at a dinuclear iron site.Logan D.T., Su X.-D., Aaberg A., Regnstroem K., Hajdu J., Eklund H., Nordlund P.Structure 4:1053-1064(1996) Binding of allosteric effectors to ribonucleotide reductase protein R1 reduction of active-site cysteines promotes substrate binding.Eriksson M., Uhlin U., Ramaswamy S., Ekberg M., Regnstroem K., Sjoeberg B.-M., Eklund H.Structure 5:1077-1092(1997) Characterization of Y122F R2 of Escherichia coli ribonucleotide reductase by time-resolved physical biochemical methods and X-ray crystallography.Tong W., Burdi D., Riggs-Gelasco P., Chen S., Edmondson D., Huynh B.H., Stubbe J., Han S., Arvai A., Tainer J.Biochemistry 37:5840-5848(1998) Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins.Logan D.T., De;Mare F., Persson B.O., Slaby A., Sjoeberg B.-M., Nordlund P.Biochemistry 37:10798-10807(1998) Crystal structures of oxidized dinuclear manganese centres in Mn-substituted class I ribonucleotide reductase from Escherichia coli carboxylate shifts with implications for O2 activation and radical generation.Hogbom M., Andersson M.E., Nordlund P.J. Biol. Inorg. Chem. 6:315-323(2001)

16130170

NP_416738.1

NC_000913.3

P69924

59.36kD

Metabolic Pathways (131985); Purine Metabolism Pathway (1022); Purine Metabolism Pathway (307); Pyrimidine Deoxyribonuleotide Biosynthesis, CDP/CTP = DCDP/dCTP,dTDP/dTTP Pathway (405192); Pyrimidine Deoxyribonuleotide Biosynthesis, CDP/CTP = DCDP/dCTP,dTDP/dTTP Pathway (468277); Pyrimidine Metabolism Pathway (1023); Pyrimidine Metabolism Pathway (309); Adenosine Deoxyribonucleotides De Novo Biosynthesis Pathway (908078); Adenosine Deoxyribonucleotides De Novo Biosynthesis II Pathway (835396); Adenosine Deoxyribonucleotides De Novo Biosynthesis II Pathway (908077)

Reducing equivalents provided by glutaredoxin or thioredoxin. [More information is available at EcoGene: EG10661]. The B2 protein of ribonucleoside-diphosphate reductase contains the tyrosyl radical-dinuclear iron center, which is thought to initiate catalysis by long-range electron transfer. [More information is available at EcoCyc: EG10661].

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (Yeast)

750