Mechanistic diversity of β-lactamases

被引:30
作者
Frère, JM [1 ]
Dubus, A
Galleni, M
Matagne, A
Amicosante, G
机构
[1] Univ Liege, Ctr Prot Engn, Inst Chem B6, B-4000 Liege, Belgium
[2] Univ Aquila, Dipartimento Sienze & Technol Biomed, I-67100 Laquila, Italy
关键词
D O I
10.1042/bst0270058
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
引用
收藏
页码:58 / 63
页数:6
相关论文
共 28 条
[1]   A STANDARD NUMBERING SCHEME FOR THE CLASS-A BETA-LACTAMASES [J].
AMBLER, RP ;
COULSON, AFW ;
FRERE, JM ;
GHUYSEN, JM ;
JORIS, B ;
FORSMAN, M ;
LEVESQUE, RC ;
TIRABY, G ;
WALEY, SG .
BIOCHEMICAL JOURNAL, 1991, 276 :269-270
[2]   CHANGES IN THE COORDINATION GEOMETRY OF THE ACTIVE-SITE METAL DURING CATALYSIS OF BENZYLPENICILLIN HYDROLYSIS BY BACILLUS-CEREUS BETA-LACTAMASE-II [J].
BICKNELL, R ;
SCHAFFER, A ;
WALEY, SG ;
AULD, DS .
BIOCHEMISTRY, 1986, 25 (22) :7208-7215
[3]   THE PRODUCTION AND MOLECULAR-PROPERTIES OF THE ZINC BETA-LACTAMASE OF PSEUDOMONAS-MALTOPHILIA IID-1275 [J].
BICKNELL, R ;
EMANUEL, EL ;
GAGNON, J ;
WALEY, SG .
BIOCHEMICAL JOURNAL, 1985, 229 (03) :791-797
[4]   The mechanism of catalysis and the inhibition of the Bacillus cereus zinc-dependent β-lactamase [J].
Bounaga, S ;
Laws, AP ;
Galleni, M ;
Page, MI .
BIOCHEMICAL JOURNAL, 1998, 331 :703-711
[5]   EXCITEMENT IN THE BETA-LACTAMASE ARENA [J].
BUSH, K .
JOURNAL OF ANTIMICROBIAL CHEMOTHERAPY, 1989, 24 (06) :831-836
[6]   1.85 A resolution structure of the zincII β-lactamase from Bacillus cereus [J].
Carfi, A ;
Duee, E ;
Galleni, M ;
Frere, JM ;
Dideberg, O .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1998, 54 :313-323
[7]   THE 3-D STRUCTURE OF A ZINC METALLO-BETA-LACTAMASE FROM BACILLUS-CEREUS REVEALS A NEW-TYPE OF PROTEIN FOLD [J].
CARFI, A ;
PARES, S ;
DUEE, E ;
GALLENI, M ;
DUEZ, C ;
FRERE, JM ;
DIDEBERG, O .
EMBO JOURNAL, 1995, 14 (20) :4914-4921
[8]   Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis [J].
Concha, NO ;
Rasmussen, BA ;
Bush, K ;
Herzberg, O .
STRUCTURE, 1996, 4 (07) :823-836
[9]   Characterization of the metal-binding sites of the beta-lactamase from Bacteroides fragilis [J].
Crowder, MW ;
Wang, ZG ;
Franklin, SL ;
Zovinka, EP ;
Benkovic, SJ .
BIOCHEMISTRY, 1996, 35 (37) :12126-12132
[10]   The catalytic mechanism of beta-lactamases: NMR titration of an active-site lysine residue of the TEM-1 enzyme [J].
Damblon, C ;
Raquet, X ;
Lian, LY ;
LamotteBrasseur, J ;
Fonze, E ;
Charlier, P ;
Roberts, GCK ;
Frere, JM .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (05) :1747-1752