
%0 Journal Article
%A Robert, S. 
%A Simier, P. 
%A Fer, A. 
%T Purification and characterization of mannose 6-phosphate reductase, a potential target for the control of <emph type="2">Striga hermonthica</emph> and <emph type="2">Orobanche ramosa</emph>
%J Functional Plant Biology
%D 1999/05/19
%V 26
%N 3
%P 233-237
%K mannose 6-phosphate reductase, mannitol, Orobanche ramosa, parasitic angiosperms, Striga hermonthica.
%R https://doi.org/10.1071/PP98138
%U https://www.publish.csiro.au/paper/PP98138 
%X Mannose 6-phosphate reductase (M6PR, EC 1.1.1.224), a potential target for the chemical control of the parasitic angiosperms that produce mannitol, was purified from the photosynthetic parasite Striga hermonthica (Del.) Benth. and the achlorophyllous parasite Orobanche ramosa L. Except for the Km values for NADPH, most of the characteristics of the enzymes are similar in these species, i.e. a monomeric structure of 38&#8211;39 kDa molecular mass, a pH optimum of 7.0&#8211;7.5 suggesting a cytosolic location, a relatively high optimum temperature (35&#8211;45&#x02DA;C), a low Km value for mannose 6-phosphate of 5.9&#8211;8.6 mM and, lastly, a significant preference for NADPH as nucleotidic cofactor. 
