Abstract：
:The interaction of the TEM-2 beta-lactamase with 9-deoxyclavulanic acid (3) and with both extensively labeled (2) and specifically labeled (1) clavulanic acid has been studied. The close similarity between 9-doexyclavulanate and clavulanate in kinetics, spectroscopic, and protein chemical terms show that the allyl alcohol group of clavulanate is irrelevant to its action as a beta-lactamase inactivator. Use of the radiolabeled samples of clavulanate shows that, of three irreversibly inactivated forms of the enzymes, two contain the whole clavulanate skeleton and the third only retains the carbon atoms of the original beta-lactam ring. These findings allow the complex interaction between clavulanic acid and the beta-lactamase to be defined more narrowly in chemical terms.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Charnas RL,Knowles JRdoi
10.1021/bi00514a035subject
Has Abstractpub_date
1981-05-26 00:00:00pages
3214-9issue
11eissn
0006-2960issn
1520-4995journal_volume
20pub_type
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