Kinetic studies of a beta-lactamase by a computerized microacidimetric method.
On-line computerized treatment of enzyme kinetic data allows the precise measurement of Michaelis--Menten constants (Km and V) from a single progress curve. This method has been used to determine the kinetic constants of a beta-lactamase extracted from an Escherichia coli strain. In the profile of enzymatic activity there obtained, Km and V are a function of the pH. From these results some information is derived about the mechanism of the enzyme--substrate binding.
D000838:Anions; D002414:Cations, Monovalent; D002512:Cephalothin; D003201:Computers; D004926:Escherichia coli / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009862:Online Systems; D009994:Osmolar Concentration; D010405:Penicillinase / Q000378:metabolism*; D010406:Penicillins; D012965:Sodium Chloride / Q000494:pharmacology; D013696:Temperature
D000838:Anions; D002414:Cations, Monovalent; D010406:Penicillins; D012965:Sodium Chloride; D010405:Penicillinase; D002512:Cephalothin