The relative catalytic specificities of the large subunit core of Synechococcus ribulose bisphosphate carboxylase/oxygenase.
The relative specificities of the carboxylase and oxygenase reactions catalyzed by the recombinant large subunit core (L8) of Synechococcus ribulose 1,5-bisphosphate carboxylase have been determined. The L8 core still retained the ability to catalyze both reactions but at a much reduced turnover rate, about 0.6% of the holoenzyme. The fate of ribulose 1,5-bisphosphate during carboxylation and oxygenation by L8 was compared with the Synechococcus holoenzyme (reconstituted from L8 and recombinant small subunits), the carboxylase from Rhodospirullum rubrum, and that of spinach. The absence of small subunits had no significant effect on the partitioning of the bisphosphate substrate between the two reactions. Thus the course of the two competing reactions is a characteristic of the structural elements that compose the L-subunits, whereas the S-subunits exert their effect on factors common to both reactions such as the specificity of the bisphosphate substrate.
Gutteridge
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Central Research and Development Department, Du Pont Company, Wilmington, Delaware 19880-0402.
D002384:Catalysis; D000458:Cyanobacteria / Q000201:enzymology*; D004926:Escherichia coli / Q000235:genetics; D005786:Gene Expression Regulation; D015971:Gene Expression Regulation, Enzymologic; D010957:Plasmids; D012273:Ribulose-Bisphosphate Carboxylase / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity
D012273:Ribulose-Bisphosphate Carboxylase