In bacteria, isocitrate dehydrogenase is regulated by phosphorylation of a specific Ser residue in the enzyme active site. X-ray structures of the phosphorylated and the nonphosphorylated enzyme show no significant conformational differences. How does phosphorylation regulate isocitrate dehydrogenase activity? O The phosphoryl group sterically hinders the substrate. O The phosphorylation bears a negative charge, which repels the substrate. O The phosphoryl group attracts positively charged Ca2* cations, which block the active site on the enzyme. None of the above.

Biochemistry
6th Edition
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Reginald H. Garrett, Charles M. Grisham
Chapter18: Glycolysis
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In bacteria, isocitrate dehydrogenase is regulated by phosphorylation of a specific Ser residue in the enzyme active site. X-ray
structures of the phosphorylated and the nonphosphorylated enzyme show no significant conformational differences. How does
phosphorylation regulate isocitrate dehydrogenase activity?
O The phosphoryl group sterically hinders the substrate.
O The phosphorylation bears a negative charge, which repels the substrate.
O The phosphoryl group attracts positively charged Ca2* cations, which block the active site on the enzyme.
None of the above.
Transcribed Image Text:In bacteria, isocitrate dehydrogenase is regulated by phosphorylation of a specific Ser residue in the enzyme active site. X-ray structures of the phosphorylated and the nonphosphorylated enzyme show no significant conformational differences. How does phosphorylation regulate isocitrate dehydrogenase activity? O The phosphoryl group sterically hinders the substrate. O The phosphorylation bears a negative charge, which repels the substrate. O The phosphoryl group attracts positively charged Ca2* cations, which block the active site on the enzyme. None of the above.
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