| Autor: |
Lenzini MV; Service de Microbiologie, Université de Liège, Sart Tilman, Belgium., Frère JM |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of enzyme inhibition [J Enzyme Inhib] 1985; Vol. 1 (1), pp. 25-34. |
| DOI: |
10.3109/14756368509031279 |
| Abstrakt: |
Cefoxitin was a very poor substrate for the beta-lactamase of Streptomyces cacaoi (kcat = 2.7 x 10(-4) s-1). In the presence of nitrocefin, a good substrate, cefoxitin behaved as a transient inactivator by immobilizing a large proportion of the enzyme as the acyl enzyme intermediate. The enzyme was also inactivated by beta-iodopenicillanate. In this case, the acyl enzyme rearranged into an alpha-beta unsaturated ester and inactivation was irreversible. In contrast to the situation prevailing with the Streptomyces albus G beta-lactamase, no turn-over of beta-iodopenicillanate was observed. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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