Inhibition constant (Ki) of pyrophosphate, noncompetitive inhibitor of rho poly(c) dependent ATPase

Value 0.07 mM
Organism Bacteria Escherichia coli
Reference Kent RB, Guterman SK. Pyrophosphate inhibition of rho ATPase: a mechanism of coupling to RNA polymerase activity. Proc Natl Acad Sci U S A. 1982 Jul 79(13):3992-6.PubMed ID6125940
Method Preparation of p and Assay of ATPase, [tritium]Poly(C) Binding Assay, Kinetic Measurements, Pyrophosphatase Assays, Protein Determination,
Comments The Ki for inhibition of p ATPase activity by PPi was determined from experiments as shown in Fig. 3. For wild-type rho, researchers obtained a Ki of 0.074 ± 0.004 mM (five experiments), whereas rho-115 p had a Ki of 0.072 + 0.013 mM (seven experiments).
Entered by Uri M
ID 104787