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Characterization of a light-dependent glutamate synthase activity in Chlamydomonas reinhardtii by Antonio J. Márquez; M. Angeles Serra; José M. Vega is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Characterization of a light-dependent glutamate synthase activity in Chlamydomonas reinhardtii about?

Photosynthetically active vesicles prepared from Chlamydomonas reinhardtii retained a light-dependent glutamate synthase activity which was highly specific for 2-oxoglutarate (Kin = 2.1 raM) and L-glutamine (Kin = 0.9 mM) as amido group acceptor and donor respectively. This activity was inhibited by azaserine, p-hydroxymercuribenzoate and 3-(p-chlorophenyl)-l,1dimethyl urea. Light-dependent synthesis of glutamate was also obtained by coupling Chlamydomonas photosynthetic particles to purified ferredoxin-glutamate synthase, using ascorbate and 2,6-dichlorophenol-indophenol as electron donor. This system was also specific for 2-oxoglutarate (Km = l raM) and L-glutamine (K m = 0.8raM) as substrates, and was stimulated by dithioerythritol. Azaserine and p-hydroxymercuribenzoate, but not 3-(p-chlorophenyl)-l,l-dimethyl urea, inhibited the reconstituted activity; high concentrations of 2-oxoglutarate were inhibitory.

Who reads Characterization of a light-dependent glutamate synthase activity in Chlamydomonas reinhardtii?

Author

Antonio J. Márquez; M. Angeles Serra; José M. Vega

Publisher

Springer; Springer-Verlag; Kluwer Academic Publishers; Springer Science and Business Media LLC; Society for Mining, Metallurgy and Exploration Inc. (ISSN 0166-8595)

Published

1987

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)