'pH-jump' crystallographic analyses of gamma-lactam-porcine pancreatic elastase complexes.

Journal article

beta-Lactams inhibit a range of enzymes via acylation of nucleophilic serine residues. Certain gamma-lactam analogues of monocyclic beta-lactams have also been shown to be reversible inhibitors of porcine pancreatic elastase (PPE), forming acyl-enzyme complexes that are stable with respect to hydrolysis. Crystallographic analysis at pH 5 of an acyl-enzyme complex formed with PPE and one of these inhibitors revealed the ester carbonyl located in the oxyanion hole in a similar conformation to t...

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Authors: Wright, P; Wilmouth, R; Clifton, I; Schofield, C

• Publication status: Published
• Journal: Biochemical journal
• Volume: 351 Pt 2
• Issue: 2
• Pages: 335-340
• Publication date: 2000-10-01
• DOI: 10.1042/0264-6021:3510335
• EISSN: 1470-8728
• ISSN: 0264-6021
• Language: English
• Keywords: Histidine; Models, Molecular; Protein Conformation; Hydrogen-Ion Concentration; Models, Chemical; Protein Binding; Lactams; Hydrolysis; Kinetics; Swine; Binding Sites; Pancreatic Elastase; Catalysis; Time Factors; Animals; Electrons; Crystallography, X-Ray; Serine Endopeptidases