Summary
The thermodynamics and mechanism of reactions catalyzed by penicillin acylase-type enzymes, as seen at present, are outlined. Most if not all that is known about these proteins is consistent with the view that they are hydrolases of both esters and amides of α-aminoacids like phenyglycine and, in some cases, also of structurally related compounds like phenylacetic acid. They apparently react, like chymotrypsin, via an acyl-enzyme intermediate which then transfers the acyl group to water, amines or alcohols as receptors.
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© 1983 Springer-Verlag, Berlin, Heidelberg
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Konecny, J. (1983). Kinetics and Thermodynamics of Reactions Catalyzed by Penicillin Acylase — Type Enzymes. In: Lafferty, R.M. (eds) Enzyme Technology. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-69148-5_25
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DOI: https://doi.org/10.1007/978-3-642-69148-5_25
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-12479-5
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