Kinetics of binding of multisubstrate analogue inhibitor (2-amino-9-[2-(phosphonomethoxy)ethyl]-6-sulfanylpurine) with trimeric purine nucleoside phosphorylase |
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Authors: | Antosiewicz Jan Wielgus-Kutrowska Beata D?ugosz Maciej Holy Antonin Bzowska Agnieszka |
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Institution: | Department of Biophysics, Institute of Experimental Physics, Warsaw University, Warsaw, Poland. |
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Abstract: | Complex formation of multisubstrate analogue inhibitor--2-amino-9-2-(phosphonomethoxy)ethyl]-6-sulfanylpurine (PME-6-thio-Gua) with trimeric purine nucleoside phosphorylase from Cellulomonas sp. was investigated using a stopped-flow spectrofluorimetric approach. Results obtained indicate that, in contrast to binding of guanine, i.e., the transition-state conformation trapping ligand, for which binding at each active site is followed by the enzyme conformational change, association of the ground-state analogue PME-6-thio-Gua is a one-step process. |
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