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Tryptophan-free human PNP reveals catalytic site interactions.
Ghanem M, Saen-oon S, Zhadin N, Wing C, Cahill SM, Schwartz SD, Callender R, Schramm VL. Ghanem M, et al. Biochemistry. 2008 Mar 11;47(10):3202-15. doi: 10.1021/bi702491d. Epub 2008 Feb 13. Biochemistry. 2008. PMID: 18269249
Altered thermodynamics from remote mutations altering human toward bovine purine nucleoside phosphorylase.
Ghanem M, Li L, Wing C, Schramm VL. Ghanem M, et al. Biochemistry. 2008 Feb 26;47(8):2559-64. doi: 10.1021/bi702132e. Biochemistry. 2008. PMID: 18281956
Thermodynamic parameters obtained from the temperature dependence studies of the chemical step establish E:R-PNP to be catalytically more efficient than the parent enzyme and reveal differences in the entropic component of catalysis. The two companion manuscripts (Luo, M., …
Thermodynamic parameters obtained from the temperature dependence studies of the chemical step establish E:R-PNP to be catalytically more ef …
596 results