Journal of Experimental Botany, Vol 50, 1-8, Copyright © 1999 by Oxford University Press
C Raines, J Lloyd and T Dyer
The photosynthetic carbon reduction (Calvin) cycle is the primary pathway
for carbon fixation and the enzyme sedoheptulose-1,7-bisphosphatase
functions in the regenerative phase of this cycle where it catalyses the
dephosphorylation of sedoheptulose-1,7-bisphosphate. This enzyme is unique
to the Calvin cycle and has no counterpart in non-photosynthetic organisms.
The isolation and sequence analysis of an SBPase clone has led to a number
of investigations which have yielded interesting and novel information on
this enzyme and in this paper the biochemistry and molecular biology of
SBPase are reviewed. Some recent exciting developments are also reported,
including the analysis of transgenic plants with reduced levels of SBPase
which has shown that SBPase is a key regulator of carbon flux and
mutagenesis studies which have resulted in the identification of the redox
active cysteines responsible for the regulation by light of SBPase
catalytic activity.
ARTICLES
Review article. New insights into the structure and function of sedoheptulose-1,7-bisphosphatase; an important but neglected Calvin cycle enzyme
Department of Biological Sciences, University of Essex, Colchester, CO4 3SQ, UK; Department of Molecular Genetics, JI Centre, Colney Lane, Norwich NR4 7UJ, UK; Corresponding author; Fax: +44 1026 873416; E-mail: rainc@essex.ac.uk
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