Punching holes in an enzyme.
Schramm and coworkers have punched holes into human purine nucleoside phosphorylase by substitution of glycine for aromatic amino acid residues at a protein lid. The results of studies on the enzymes with holes illuminate hidden chemistry that occurs at the enzyme active site.
Department of Chemistry, The State University of New York at Buffalo, Buffalo, NY 14260-3000, USA. jrichard@buffalo.edu
John P
JP
Richard
D055162:Biocatalysis; D020134:Catalytic Domain; D006801:Humans; D006868:Hydrolysis; D007288:Inosine / Q000737:chemistry / Q000378:metabolism; D011684:Purine Nucleosides / Q000378:metabolism; D011683:Purine-Nucleoside Phosphorylase / Q000737:chemistry* / Q000378:metabolism; D012267:Ribosemonophosphates / Q000378:metabolism
D011684:Purine Nucleosides; D012267:Ribosemonophosphates; C031154:ribose 1-phosphate; D007288:Inosine; D011683:Purine-Nucleoside Phosphorylase