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Full-Text Articles in Physical Sciences and Mathematics
The Aminopeptidase From Aeromonas Proteolytica: Structure And Mechanism Of Co-Catalytic Metal Centers Involved In Peptide Hydrolysis, Richard Holz
Richard C. Holz
Enzymes containing multi-metal active sites are central to numerous biological processes and, consequently, characterization of their structure and function is a problem of outstanding importance. One of the least-explored groups of enzymes is the hydrolases that contain dinuclear metal centers. These enzymes play key roles in carcinogenesis, tissue repair, and protein degradation processes. In addition, some of these enzymes can catalyze the hydrolysis of phosphorus(V) compounds found in nerve gases and agricultural neurotoxins. The determination of detailed reaction mechanisms for these enzymes is required for the design of highly potent, specific inhibitors that can function as potential pharmaceuticals. Hydrolytic enzymes …
The Aminopeptidase From Aeromonas Proteolytica Can Function As An Esterase, David Bienvenue, Rebecca Matthew, Dagmar Ringe, Richard Holz
The Aminopeptidase From Aeromonas Proteolytica Can Function As An Esterase, David Bienvenue, Rebecca Matthew, Dagmar Ringe, Richard Holz
Richard C. Holz
The aminopeptidase from Aeromonas proteolytica (AAP) can catalyze the hydrolysis of L-leucine ethyl ester (L-Leu-OEt) with a rate of 96±5 s–1 and a K m of 700 µM. The observed turnover number for L-Leu-OEt hydrolysis by AAP is similar to that observed for peptide hydrolysis, which is 67±5 s–1. The k cat values for the hydrolysis of L-Leu-OEt and L-leucine-p-nitroanilide (L-pNA) catalyzed by AAP were determined at different pH values under saturating substrate concentrations. Construction of an Arrhenius plot from the temperature dependence of AAP-catalyzed ester hydrolysis indicates that the rate-limiting step does not change as a function of temperature …