Changing Kinetic Properties of Fructose-1,6-bisphosphatase from Pea Chloroplasts during Photosynthetic Induction | Zendy

Ivano A. Marques | Zendy; Louise E. Anderson | Zendy

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Changing Kinetic Properties of Fructose-1,6-bisphosphatase from Pea Chloroplasts during Photosynthetic Induction

Author(s) -

Ivano A. Marques,

Louise E. Anderson

Publication year - 1985

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.77.4.807

Subject(s) - photosynthesis , fructose 1,6 bisphosphatase , chloroplast , fructose , c4 photosynthesis , biophysics , enzyme , biochemistry , biology , kinetic energy , botany , chemistry , physics , quantum mechanics , gene

After dark-light transitions, there is a delay in photosynthetic CO(2) fixation by isolated pea chloroplasts in the range of some minutes. In order to assess the physiological significance of light modulation of enzyme activity in the control of induction, we made estimates of the kinetic parameters of fructose-1,6-bisphosphatase immediately upon release from pea chloroplasts in the dark and after illumination for various time periods. The Michaelis constant for fructose-1,6-bisphosphate decreased and maximal velocities increased during induction. It seems likely that light activation of this enzyme is one of the factors contributing to the overcoming of the lag period in photosynthetic CO(2) fixation.

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