protein

Recombinant Escherichia coli Ribonucleoside-diphosphate reductase 1 subunit alpha

MBS1264323

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Escherichia coli Ribonucleoside-diphosphate reductase 1 subunit alpha

Ribonucleoside-diphosphate reductase 1 subunit alpha

Protein B1; Ribonucleoside-diphosphate reductase 1 R1 subunit; Ribonucleotide reductase 1

ribonucleoside-diphosphate reductase 1, alpha subunit; Ribonucleoside-diphosphate reductase 1 subunit alpha; ribonucleoside-diphosphate reductase 1, alpha subunit; Protein B1; Ribonucleoside-diphosphate reductase 1 R1 subunit; Ribonucleotide reductase 1

nrdA

nrdA; nrdA; dnaF; ECK2226; JW2228; dnaF

RIR1_ECOLI

E Coli or Yeast or Baculovirus or Mammalian Cell

1-761

761

MNQNLLVTKRDGSTERINLDKIHRVLDWAAEGLHNVSIS
QVELRSHIQFYDGIKTSDIHETIIKAAADLISRDAPDYQ
YLAARLAIFHLRKKAYGQFEPPALYDHVVKMVEMGKYDN
HLLEDYTEEEFKQMDTFIDHDRDMTFSYAAVKQLEGKYL
VQNRVTGEIYESAQFLYILVAACLFSNYPRETRLQYVKR
FYDAVSTFKISLPTPIMSGVRTPTRQFSSCVLIECGDSL
DSINATSSAIVKYVSQRAGIG

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. R1 contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide. It also provides redox-active cysteines.

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) Nucleotide sequence of the gene coding for the large subunit of ribonucleotide reductase of Escherichia coli. Correction.Nilsson O., Aaberg A., Lundqvist T., Sjoeberg B.-M.Nucleic Acids Res. 16:4174-4174(1988) Sjoeberg B.-M.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) Protein B1 of ribonucleotide reductase. Direct analytical data and comparisons with data indirectly deduced from the nucleotide sequence of the Escherichia coli nrdA gene.Sjoeberg B.-M., Eriksson S., Joernvall H., Carlquist M., Eklund H.Eur. J. Biochem. 150:423-427(1985) Evidence for two different classes of redox-active cysteines in ribonucleotide reductase of Escherichia coli.Aaberg A., Hahne S., Karlsson M., Larsson A., Ormoe M., Aahgren A., Sjoeberg B.-M.J. Biol. Chem. 264:12249-12252(1989) Two conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase.Ekberg M., Sahlin M., Eriksson M., Sjoberg B.M.J. Biol. Chem. 271:20655-20659(1996) Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.Mol. Cell. Proteomics 8:215-225(2009) Structure of ribonucleotide reductase protein R1.Uhlin U., Eklund H.Nature 370:533-539(1994) A new mechanism-based radical intermediate in a mutant R1 protein affecting the catalytically essential Glu441 in Escherichia coli ribonucleotide reductase.Persson A.L., Eriksson M., Katterle B., Potsch S., Sahlin M., Sjoberg B.M.J. Biol. Chem. 272:31533-31541(1997) 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) Binding specificity and mechanistic insight into glutaredoxin-catalyzed protein disulfide reduction.Berardi M.J., Bushweller J.H.J. Mol. Biol. 292:151-161(1999)

16130169

NP_416737.1

NC_000913.3

P00452

101.72kD

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: EG10660]. The B1 protein of ribonucleoside-diphosphate reductase consists of two polypeptide chains of similar or identical size. [More information is available at EcoCyc: EG10660].

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

1 mg (E-Coli)

1180

0.05 mg (Baculovirus)

1575