Rhodobacter sphaeroides phosphoribulokinase: binary and ternary complexes with nucleotide substrate analogs and effectors

Biochemistry
J A RunquistHenry M Miziorko

Abstract

Rhodobacter sphaeroides phosphoribulokinase (PRK) binds ATP substrate, as well as spectroscopically active ATP analogs (trinitrophenyl-ATP and ATP gamma S-acetamidoproxyl), to form stable binary complexes. Stoichiometric binding of these nucleotide triphosphates in PRK's substrate site is observed not only with wild-type enzyme but also with D42A and D169A mutants. The demonstration that these mutants contain a full complement of functional substrate binding sites indicates their substantial structural integrity and underscores the significance of their markedly diminished catalytic activity [Charlier et al. (1994) Biochemistry 33, 9343-9350]. Similarly, PRK forms a stable binary complex with the allosteric activator NADH. The negative allosteric effector AMP displaces activator NADH but not substrate from their respective binary complexes with enzyme. When trinitrophenyl-ATP, a fluorescent nucleotide triphosphate that functions as an alternative PRK substrate, forms a binary complex with enzyme, its fluorescence emission is enhanced and lambda max shifted from approximately 557 to 545 nm. Upon formation of a binary PRK-NADH complex, the fluorescence emission of the dinucleotide effector is also enhanced and the lambda max shif...Continue Reading

Citations

Aug 16, 2003·European Journal of Biochemistry·Toshiaki Hiratsuka
Sep 11, 2002·Archives of Biochemistry and Biophysics·Jennifer A Runquist, Henry M Miziorko
Oct 30, 2007·Biochimica Et Biophysica Acta·Xiusheng ChuDing Li
Jun 1, 2004·Protein Science : a Publication of the Protein Society·Dmitriy Krepkiy, Henry M Miziorko
Jan 14, 2017·Nature Communications·Takunari KonoHiroki Ashida
Feb 28, 1997·The Journal of Biological Chemistry·D PotterH M Miziorko

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