Identification of NADPH-thioredoxin reductase system in Euglena gracilis

Journal Article · Sat Nov 01 04:00:00 EST 1975 · Proc. Natl. Acad. Sci. U.S.A.; (United States)

DOI:https://doi.org/10.1073/pnas.72.11.4233· OSTI ID:7296054

Munavalli, S; Parker, D V; Hamilton, F D

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 flavoprotein 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. The enzyme preparation described in this report contains four different types of polypeptide chains which may complex to form the active enzyme. (auth)

• Research Organization: Oak Ridge National Lab., TN
• OSTI ID: 7296054
• Journal Information: Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 72:11; ISSN PNASA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ALGAE
BIOCHEMICAL REACTION KINETICS
BIOMASS
CATALYSIS
COENZYMES
ENERGY SOURCES
ENZYMES
EUGLENA
KINETICS
METABOLISM
MICROORGANISMS
NADP
NUCLEIC ACIDS
NUCLEOTIDES
ORGANIC COMPOUNDS
OXIDOREDUCTASES
PLANTS
PROTEINS
REACTION KINETICS
RENEWABLE ENERGY SOURCES
RNA
UNICELLULAR ALGAE