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• W2034148066 startingPage "263" @default.
• W2034148066 abstract "The recent isolation of a catalytically competent recombinant octameric core of the hexadecameric ribulose-1, 5-bisphosphate carboxylase/oxygenase from the cyanobacterium Anacystis nidulans (Synechocoecus) (B. Lee and F. R. Tabita, 1990, Biochemistry29, 9352–9357) has provided a useful system for examining the properties of this enzyme in the absence of small subunits. Unlike most sources of hexadecameric ribulose bisphosphate carboxylase, the nonactivated Anacystis holoenzyme was not inhibited markedly by preincubation with ribulose 1,5-bisphosphate. This was also true for the Anacystis octameric core and a heterologous recombinant enzyme that comprised large subunits from Anacystis and small subunits from the bacterium Alcaligenes eutrophus, suggesting that substrate-mediated inactivation is not influenced by small subunits. In addition, the CO2O2 specificity factor was not affected by the source of the small subunits incorporated into the structure of the hexadecameric protein, in agreement with previous in vitro heterologous reconstitution studies. The activated octameric Anacystis enzyme, however, was significantly more sensitive to inhibition by the phosphorylated effector 6-phosphogluconate than were the hexadecameric Alcaligenes and Anacystis enzymes and the heterologous Anacystis-Alcaligenes hybrid." @default.
• W2034148066 created "2016-06-24" @default.
• W2034148066 creator A5027138214 @default.
• W2034148066 creator A5079909538 @default.
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• W2034148066 date "1991-12-01" @default.
• W2034148066 modified "2023-10-16" @default.
• W2034148066 title "Catalytic properties of recombinant octameric, hexadecameric, and heterologous cyanobacterial/ bacterial ribulose-1,5-bisphosphate carboxylase/oxygenase" @default.
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• W2034148066 doi "https://doi.org/10.1016/0003-9861(91)90133-4" @default.
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