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- W1490617220 abstract "We have established the suitability of adenosine 5'-O-(gamma-thio)triphosphate(ATP gamma S) as an analog of ATP for the nucleoside triphosphatase activity of Escherichia coli transcription termination protein rho (EC 3.6.1.3). Steady-state analysis gives a Vmax of 1.5 mumol min-1 mg-1, 9% of the value with MgATP as substrate, and indicates that ATP gamma S binds as tightly (based on Km and Ki versus ATP) to rho as does ATP. (gamma-S)[beta gamma-17O,gamma-17O,gamma-18O]ATP gamma S was used as substrate to produce chiral product inorganic [17O,18O]thiophosphate and determine the stereochemical course of the hydrolysis. The results of this determination, inversion at the thiophosphoryl phosphorus, indicate that the enzymatic hydrolysis of ATP by rho consists of a direct transfer of the phospho group to water without the existence of a phosphoenzyme or phospho-RNA intermediate." @default.
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- W1490617220 date "1986-12-01" @default.
- W1490617220 modified "2023-10-18" @default.
- W1490617220 title "Absence of a phosphorylated intermediate during ATP hydrolysis by Escherichia coli transcription termination protein rho." @default.
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- W1490617220 doi "https://doi.org/10.1016/s0021-9258(18)66650-5" @default.
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