| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10537152 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2013 | 14 Pages |
Abstract
⺠The substrate gating mechanism of POP was investigated via protein engineering. ⺠The mutations markedly changed specificity, catalytic power and inhibitor binding. ⺠The interaction of loop A with the N-terminus controls substrate gating.
Keywords
DLS5,5'-dithiobis(2-nitrobenzoic acid)EDDnpβ-naphthylamideBNANi-NTAABZPAGEDTNBGSSGGSHDTTPBSDSCSEC2-aminobenzoylEDTAEthylenediaminetetraacetic acid4-morpholineethanesulfonic acidpolyacrylamide gel electrophoresisSize-exclusion chromatographyResidueX-ray crystallographyTevMelting TemperatureMolecular dynamicsdithiothreitolcircular dichroismEnzyme structurePhosphate buffered salineMeSProtein engineeringnickel-nitrilotriacetic acidpolymerase chain reactionPCRTobacco etch viruspopDynamic Light Scatteringprolyl oligopeptidaseEnzyme catalysisDifferential scanning calorimetryreduced glutathioneoxidized glutathione
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Zoltán Szeltner, Tünde Juhász, Ilona Szamosi, Dean Rea, Vilmos Fülöp, Károly Módos, Luiz Juliano, László Polgár,