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.
Richard
John P
JP
Department of Chemistry, The State University of New York at Buffalo, Buffalo, NY 14260-3000, USA. jrichard@buffalo.edu
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