Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Elisabet Pontis"'
Publikováno v:
Journal of Biological Chemistry. 274:7182-7189
Three separate classes of ribonucleotide reductases are known, each with a distinct protein structure. One common feature of all enzymes is that a single protein generates each of the four deoxyribonucleotides. Class I and III enzymes contain an allo
Publikováno v:
Journal of Biological Chemistry. 272:18044-18050
Ribonucleotides are converted to deoxyribonucleotides by ribonucleotide reductases. Either thioredoxin or glutaredoxin is a required electron donor for class I and II enzymes. Glutaredoxins are reduced by glutathione, thioredoxins by thioredoxin redu
Publikováno v:
Journal of Biological Chemistry. 271:26582-26587
Enterobacteriaceae contain genes for three separate ribonucleotide reductases: nrdAB code for a class Ia enzyme, active during aerobiosis, nrdDG for a class III enzyme, active during anaerobiosis, and nrdEF for a cryptic class Ib enzyme. The NrdEF en
Publikováno v:
Journal of Biological Chemistry. 271:8779-8785
Escherichia coli contains the genetic information for three separate ribonucleotide reductases. Two of them (class I enzymes), coded by the nrdAB and nrdEF genes, respectively, contain a tyrosyl radical, whose generation requires oxygen. The NrdAB en
Autor:
Peter Reichard, Britt-Marie Sjöberg, Rolf Eliasson, Girbe Buist, Jessica Andersson, Elisabet Pontis, Xueyin Sun
Publikováno v:
Journal of Biological Chemistry. 270:2443-2446
The anaerobic ribonucleotide reductase from Escherichia coli contains a glycyl radical as part of its polypeptide structure. The radical is generated by an enzyme system present in E. coli. The reductase is coded for by the nrdD gene located at 96 mi
Autor:
Albert Jordan, Peter Reichard, Elisabet Pontis, Mohamed G. Atta, Maria Krook, Isidre Gibert, Jordi Barbé
Publikováno v:
Proceedings of the National Academy of Sciences. 91:12892-12896
The nrdA and nrdB genes of Escherichia coli and Salmonella typhimurium encode the R1 and R2 proteins that together form an active class I ribonucleotide reductase. Both organisms contain two additional chromosomal genes, nrdE and nrdF, whose correspo
Publikováno v:
Journal of Biological Chemistry. 269:26116-26120
The anaerobic Escherichia coli ribonucleotide reductase (class III reductase) responsible for the synthesis of the deoxyribonucleotides required for anaerobic DNA replication contains an oxygen-sensitive glycyl radical (Gly-681) suggesting involvemen
Autor:
Peter Reichard, E Haggård-Ljungquist, Maria Krook, Elisabet Pontis, Hans Jörnvall, Rolf Eliasson, Vera Bianchi
Publikováno v:
Journal of Bacteriology. 175:1590-1595
A specific ribonucleoside triphosphate reductase is induced in anaerobic Escherichia coli. This enzyme, as isolated, lacks activity in the test tube and can be activated anaerobically with S-adenosylmethionine, NADPH, and two previously uncharacteriz
Publikováno v:
Experimental Cell Research. 199:120-128
Conditions for labeling the dATP pool of V79 and 3T3 cells from [3H]deoxyadenosine (salvage) or [3H]adenine (via ribonucleotide reduction) were established. With deoxyadenosine the specific radioactivity of dATP reached a constant value after 60 min.
Publikováno v:
Biochemical and Biophysical Research Communications. 180:1222-1226
Two proteins, called alpha and beta 3, copurify with the anaerobic ribonucleotide reductase from Escherichia coli (Eliasson et al. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 3314-3318). Both are now identified as products of the clpB gene that is presu