Thymidine phosphorylase fromEscherichia coli: Tight-binding inhibitors as enzyme active-site titrants
Year: 2006
Type: article
Abstract: Thymidine phosphorylase (EC 2.4.2.4) catalyses the reversible phosphorolysis of pyrimidine 2'-deoxynucleosides, forming 2-deoxyribose-1-phosphate and pyrimidine. 5-Chloro-6-(2-imino-pyrrolidin-1-yl)methyl-uracil hydrochloride (TPI, 1) and its 5-bromo analogue (2), 6-(2-amino-imidazol-1-yl)methyl-5-bromo-uracil (3) and its 5-chloro analogue (4) act as tight-binding stoichiometric inhibitors of recombinant E. coli thymidine phosphorylase, and thus can be used as the first active-site titrants for it using either thymidine or 5-nitro-2'-deoxyuridine as substrate.
Institution: University of Manchester
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: bronze
Funder: AstraZeneca
OpenAlex ID: W2114767579