Enzymatic Hydrolysis of N-Acylated 1-Aminophosphonic Acids
| Autor: | D. A. Mironenko, Valery P. Kukhar, V. A. Solodenko, T.N. Kasheva, A. N. Belozersky, V. K. Svedas, Elena Kozlova |
|---|---|
| Rok vydání: | 1990 |
| Předmět: | |
| Zdroj: | Phosphorus, Sulfur, and Silicon and the Related Elements. 51:411-411 |
| ISSN: | 1563-5325 1042-6507 |
| DOI: | 10.1080/10426509008040938 |
| Popis: | Penicillin acylase from E. coli (FC 3.5.1.11) was found to hydrolyse N-phenylacetylated 1-aminoalkylphosphonic acids and their esters. Enzyme preferentially converts the R-form of the substrates: the ratios of the bimolecular rate constants of penicillin acylase-catalysed hydrolysis of R-and S- forms of 1-(N-phenylacetaminol-ethylphosphonic acid and its dimethyl- and diisopropyl- esters are 58000, 2600, 1800; these derivatives were shown to have the greatest values of the catalytic constants for enzymatic hydrolysis of all known substrates of penicillin acylase: 237, 148, and 134 s; corresponding values of Michaelis constants are 3.7×10−5, 6.8×10−4, and 6.2×10−4 M. The kinetics of the enzymatic hydrolysis of 1-(N-phenylacetaminol-ethylphosphonic acid was investigated up to high degrees of conversion. The inhibition of penicillin acylase by high concentrations of the R-form of the substrate (with substrate inhibition constant 0.07 Ml and competitive inhibition by the reaction product phenylacetic ... |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|