Abstract
The turnover time of enzymes, when saturated with their substrates, may be of the order of 10−5 to 0.1 s. This time is taken up by the need of the protein to undergo changes in conformation. In the cell, however, enzymes are virtually never saturated with substrate, indeed the concentration of an enzyme may exceed that of its substrate. The rate of metabolic processes is strongly dependent on diffusion, so that the actual turnover times of enzymes may be measured in seconds, and complete pathways may take 10–100 s to adjust to changes in the supply of feedstock.
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References
Further reading
Edwards, G.E. and Walker, D.A. (183) C3, C4: mechanisms, and cellular and environmental regulation, of photosynthesis Blackwell, Oxford, part B, 107–495.
Halliwell, B. (1984) Chloroplast Metabolism. The structure and function of chloroplasts in green leaf cells Oxford University Press, Chapters 4, 6 and 7.
Macdonald, F.D. and Buchanan, B.B. (1987) Carbon dioxide assimilation. In Amesz, J., ed., Photosynthesis. New Comprehensive Biochemistry Vol. 15, Elsevier, Amsterdam, 175–197.
Ohyama, K., Kohchi, T., Sano, T. and Yamada, Y. (1988) Newly identified groups of genes in chloroplasts. Trends Biochem. Sci. 13, 19–22.
Cited references
Bennet, J. (1981) Biosynthesis of the light-harvesting chlorophyll a/b protein. Europ. J. Biochem. 118, 61–70.
Berry, J.A., Lorimer, G.H.; Pierce, J., Seemann, J.R., Meek, J. and Freas, S. (1987) Isolation, identification and synthesis of 2-carboxyarabinitol-l-phosphate, a diurnal regulator of ribulose-bisphosphate carboxylase activity. Proc. Natl. Acad. Sri., USA 84, 734–738.
Black, C.C. and Mollenhauer, H.H. (1971) Structure and distribution of chloroplasts and other organelles in leaves with various rates of photosynthesis. Plant Physiol. 47, 15–23.
Bowes, G., Ogren, W.L. and Hagemen, R.H. (1971) Phosphoglycollate production catalysed by ribulose diphosphate carboxylase. Biochem. Biophys. Res. Commun. 45, 716–722.
Crouse, E. J., Schmitt, J.M. and Bohnert, H-J. (1985) Chloroplast and cyanobacterial genomes, genes and RNAs: a compilation. Plant Mol. Biol. Reporter 3, 43–89.
Douce, R. and Joyard, J. (1979) Structure and function of the plastid envelope. Adv. Bot. Res. 7, 1–116.
Ellis, R.J. (1977) Protein synthesis by isolated chloroplasts. Biochim. Biophys. Acta 463, 185–215.
Harwood, J. (1988) The site of action of some selective graminaceous herbicides is identified as acetyl-CoA carboxylase. Trends Biochem. Sci. 330–331.
Husic, D.W., Husic, H.D. and Tolbert, N.E. (1987) The oxidative Carbon cycle or C2 cycle. Critical Revs. Plt. Sci. 5, 45–100.
Kelly, G.J. (1984) The capture of carbon by aquatic plants. Trends Biochem. Sci. 9, 255–256.
Mayer, F. (1971) Light-induced chloroplast contraction and movement. In Gibbs, M., ed., Structure and Function of Chloroplasts Springer-Verlag, Berlin, 35–49.
Mullet, J.E. (1988) Chloroplast development and gene expression. Ann. Rev. Plant Physiol. 39, 475–502.
Schuster, G., Schochat, S., Adir, N., Even, D., Ish-Shalom, D., Grimm, B., Kloppstech, K. and Ohad, I. (1988) The synergistic effect of light and heat stress on the inactivation of photosystem II. In Harwood, J.L. and Walton, T.J., eds., Plant Membranes—Structure, Assembly and Function Biochemical Society, London, 133–138.
Ohyama, K., Kohchi, T., Fukuzawa, H., Sano, T., Umesono, K. and Ozeki, H. (1988) Gene organisation and newly identified groups of genes of the chloropast genome from a liverwort, Marchantia polymorpha. Photosynthesis Res. 16, 7–22.
Salvucci, M.E., Portis, A.R. and Ogren, W.L. (1986) A soluble chloroplast protein catalyses ribulosebisphosphate carboxylase/oxygenase activation in vivo. Photosynthesis Res. 7, 193–201.
Shinozaki, K., Hayashida, N. and Sugiura, M. (1988) Nicotiana chloroplast genes for components of the photosynthetic apparatus. Photosynthesis Res. 18, 7–31.
Woodrow, I.E. and Berry, J.A. (1988) Enzymic regulation of photosynthetic CO2 fixation in C3 plants. Ann. Rev. Plant Physiol. 39, 533–594.
Zelitch, I. (1979) Photorespiration: studies with whole tissues. In Gibbs, M. and Latzko H, eds., Photosynthesis II. Photosynthetic Carbon Metabolism. Encycl. Plant Physiol. new series, Vol. 6, Springer-Verlag, Berlin, 174–180.
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Gregory, R.P.F. (1989). Metabolic Processes and Physiological Adjustments. In: Photosynthesis. Tertiary Level Biology. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-0391-3_7
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DOI: https://doi.org/10.1007/978-94-009-0391-3_7
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