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Antimicrobial Agents and Chemotherapy, March 2001, p. 878-882, Vol. 45, No. 3
Service de Bactériologie-Virologie, Hôpital de
Bicêtre, Assistance Publique/Hôpitaux de Paris,
Faculté de Médecine Paris-Sud, 94275 Le
Kremlin-Bicêtre Cedex,1 Service de
Bactériologie, Hôpital Lyon-Sud, Hospices Civils de Lyon,
Faculté de Médecine Lyon-Sud, 69921 Oullins
Cedex,2 Laboratoire de mycologie
fondamentale et appliquée aux biotechnologies industrielles,
Institut des Sciences Pharmaceutiques et Biologiques, 69373 Lyon Cedex
08,3 and UMR175 CNRS Chimie et
Biologie des Substances Actives, 29000 Quimper,4
France
Received 22 June 2000/Returned for modification 1 October
2000/Accepted 15 December 2000
A
0066-4804/01/$04.00+0 DOI: 10.1128/AAC.45.3.878-882.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Molecular and Biochemical Analysis of AST-1, a Class A
-Lactamase from Nocardia asteroides Sensu
Stricto
-lactamase gene was cloned from a Nocardia
asteroides sensu stricto clinical isolate. A recombinant plasmid,
pAST-1, expressed the
-lactamase AST-1 in Escherichia
coli JM109. Its pI was 4.8, and its relative molecular mass was
31 kDa. E. coli JM109(pAST-1) was resistant to penicillins
and narrow-spectrum cephalosporins. The
-lactamase AST-1 had a
restricted hydrolytic activity spectrum. Its activity was
partially inhibited by clavulanic acid but not by sulbactam and
tazobactam. AST-1 is an Ambler class A
-lactamase sharing 65% amino
acid identity with
-lactamase FAR-1, the most closely related enzyme.
*
Corresponding author. Mailing address: Service de
Bactériologie-Virologie, Hôpital de Bicêtre, 78 rue
du Général Leclerc, 94275 Le Kremlin-Bicêtre Cedex,
France. Phone: 33-1-45-21-36-32. Fax: 33-1-45-21-63-40. E-mail:
nordmann.patrice{at}bct.ap-hop-paris.fr.
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