PMID: 675Nov 1, 1975

Identification of NADPH-thioredoxin reductase system in Euglena gracillis

Proceedings of the National Academy of Sciences of the United States of America
S MunavalliF D Hamilton

Abstract

Euglena gracilis contains a protein system which can utilize the reducing power of NADPH in the ribonucleotide reductase-catalyzed reduction of CTP. The proteins required for this reaction are a flavoprotien with a molecular weight of approximately 185,000 which is functionally similar to thioredoxin reductase (NADPH), EC 1.6.4.5, and another protein (Protein I) whose function in the reaction is unknown. This new protein does not appear to contain a prosthetic group and has a molecular weight of approximately 240,000. In addition, the ribonucleotide reductase active in the Euglena NADPH-thioredoxin reductase system is more complex than the protein reported in a previous publication [(1974) j. Biol. Chem. 249, 4428-4434]. The enzyme preparation described in this report contains four different types of polypeptide chains which may complex to form the active enzyme.

References

Jun 1, 1973·European Journal of Biochemistry·A Larsson
Oct 5, 1966·Biochemical and Biophysical Research Communications·M D Orr, E Vitols
Sep 14, 1972·Biochimica Et Biophysica Acta·F K Gleason, H P Hogenkamp
Mar 15, 1972·European Journal of Biochemistry·G Larson, A Larsson

Citations

Jan 1, 1976·Advances in Enzyme Regulation·E C Moore
Aug 8, 1977·Biochemical and Biophysical Research Communications·W Wanger, H Follmann
Aug 7, 1985·Biochimica Et Biophysica Acta·B Gómez-Silva, J A Schiff
Aug 1, 1980·Biological Reviews of the Cambridge Philosophical Society·J A Bryant

Related Concepts

Cytosine Nucleotides
Euglena gracilis
NADH, NADPH Oxidoreductases
NADP
Protein Conformation
Ribonucleotide Reductase
Thioredoxin Reductase (NADPH)

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