Literature summary for 2.4.2.1 extracted from

Afshar, S.; Sawaya, M.R.; Morrison, S.L.
Structure of a mutant human purine nucleoside phosphorylase with the prodrug, 2-fluoro-2-deoxyadenosine and the cytotoxic drug, 2-fluoroadenine (2009), Protein Sci., 18, 1107-1114.

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant E201Q/N243D in complex with prodrug 2-fluoro-2'-deoxyadenosine and with 2-fluoroadenine. The overall fold of the mutant is nearly identical to the wild type enzyme. The residues Gln201 and Asp243 introduced by the mutation form hydrogen bond contacts with 2-fluoro-2'-deoxyadenosine that result in its binding and catalysis. Comparison of complexes suggest that the side chains of Gln201 and Asp243 as well as the purine base rotate during catalysis possibly facilitating cleavage of the glycosidic bond	Homo sapiens

Crystallization (Comment)

Organism

mutant E201Q/N243D in complex with prodrug 2-fluoro-2'-deoxyadenosine and with 2-fluoroadenine. The overall fold of the mutant is nearly identical to the wild type enzyme. The residues Gln201 and Asp243 introduced by the mutation form hydrogen bond contacts with 2-fluoro-2'-deoxyadenosine that result in its binding and catalysis. Comparison of complexes suggest that the side chains of Gln201 and Asp243 as well as the purine base rotate during catalysis possibly facilitating cleavage of the glycosidic bond

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
E201Q/N243D	crystallization data	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P00491	-	-

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Release 2023.1 (January 2023)