Purification and properties of a C-1 diphosphatase from Spinacia oleracea

Chakravorty, M. ; Chakrabortty, H. C. ; Burma, D. P. (1959) Purification and properties of a C-1 diphosphatase from Spinacia oleracea Archives of Biochemistry and Biophysics, 82 (1). pp. 21-33. ISSN 0003-9861

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/000398...

Related URL: http://dx.doi.org/10.1016/0003-9861(59)90085-2

Abstract

A C-1 diphosphatase has been purified about 17-fold from Spinacia oleracea. This reacts with both ribulose diphosphate (RuDP) and fructose diphosphate (FDP) and practically at the same rate. From competitive experiments it appears that one enzyme is involved in the two reactions. The properties of the diphosphatase have been studied. Since the diphosphatase is contaminated with phosphoriboisomerase, the reaction product from RuDP is found to he a mixture of ribose 5-phosphate (R5P) and ribulose 5-phosphate (Ru5P). FDP is converted by the enzyme to fructose 6-phosphate (F6P). The role of this enzyme in the photosynthetic cycle has been discussed.

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