Activation of Orotidine 5‘-Monophosphate Decarboxylase by Phosphite Dianion:  The Whole Substrate is the Sum of Two Parts

We report that the binding of phosphite dianion to orotidine 5‘-monophosphate decarboxylase (OMPDC) results in an 80 000-fold increase in k cat/K m for decarboxylation of the truncated substrate, 1-(β-d-erythrofuranosyl)orotic acid (EO), which lacks a 5‘-phosphodianion moiety. The intrinsic binding...

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Veröffentlicht in:	Journal of the American Chemical Society 2005-11, Vol.127 (45), p.15708-15709
Hauptverfasser:	Amyes, Tina L, Richard, John P, Tait, James J
Format:	Artikel
Sprache:	eng
Schlagworte:	Anions - chemistry Anions - pharmacology Biological and medical sciences Enzyme Activation Fundamental and applied biological sciences. Psychology Mechanisms. Catalysis. Electron transfer. Models Molecular biophysics Orotidine-5'-Phosphate Decarboxylase - chemistry Orotidine-5'-Phosphate Decarboxylase - drug effects Phosphites - chemistry Phosphites - pharmacology Physical chemistry in biology Substrate Specificity
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