| Autor: |
Damblon, Christian, Ledent, Philippe, Zhao, Guo-Hua, Jamin, Marc, Dubus, Alain, Vanhove, Marc, Raquet, Xavier, Christiaens, Léon, Frère, Jean-Marie |
| Zdroj: |
Letters in Peptide Science; Nov1995, Vol. 2 Issue 3/4, p212-216, 5p |
| Abstrakt: |
With peptide substrates, the penicillin-sensitive dd-peptidases exhibit a strict specificity for d-Ala- d-Xaa C-termini. Only glycine is tolerated as the C-terminal residue, but with a significantly decreased activity. These enzymes also hydrolyse various ester and thiolester analogues of their natural substrates. Some of the thiolesters whose C-terminal leaving group exhibited an l stereochemistry were significantly hydrolysed by some of the studied enzymes, particularly by the Actinomadura R39 dd-peptidase. By contrast, the strict specificity for a d residue in the penultimate position was fully retained. The same esters and thiolesters also behaved as substrates for β-lactamases. In this case, thiolesters exhibiting l stereochemistry in the C-terminal position could also be hydrolysed, mainly by the class C and class D enzymes. But, more surprisingly, the class C Enterobacter cloacae P99 β-lactamase also hydrolysed thiolesters containing an l residue in the penultimate position, sometimes more efficiently than the d isomer. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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