Identification of NADPH-thioredoxin reductase system in Euglena gracillis.
- 1 November 1975
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 72 (11) , 4233-4237
- https://doi.org/10.1073/pnas.72.11.4233
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.Keywords
This publication has 19 references indexed in Scilit:
- Ribonucleotide reductase from Euglena gracilis. A 5'-deoxyadenoslycobalamin-dependent enzyme.1974
- Bacteriophage‐Induced Ribonucleotide Reductase SystemsEuropean Journal of Biochemistry, 1974
- Thioredoxin Reductase from Rat LiverEuropean Journal of Biochemistry, 1973
- Thioredoxin from Lactobacillusleichmannii and its role as hydrogen donor for ribonucleoside triphosphate reductaseBiochemical and Biophysical Research Communications, 1966
- Deoxycytidylate formation from cytidylate without glycosidic cleavage in LactobacillusLeichmannii extracts containing vitamin B12 coenzymeBiochemical and Biophysical Research Communications, 1965
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964
- ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES. VI. THE CYTIDINE DIPHOSPHATE REDUCTASE SYSTEM FROM NOVIKOFF HEPATOMA.1964
- ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES .6. CYTIDINE DIPHOSPHATE REDUCTASE SYSTEM FROM NOVIKOFF HEPATOMA1964
- ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES .4. ISOLATION + CHARACTERIZATION OF THIOREDOXIN HYDROGEN DONOR FROM ESCHERICHIA COLI B1964
- ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES .1. FORMATION OF DEOXYCYTIDINE DIPHOSPHATE FROM CYTIDINE DIPHOSPHATE WITH ENZYMES FROM ESCHERICHIA COLI1962