Effect of disulfide-bond introduction on the activity and stability of the extended-spectrum class A β-lactamase Toho-1

2006 ◽  
Vol 1764 (8) ◽  
pp. 1349-1355 ◽  
Author(s):  
Akiko Shimizu-Ibuka ◽  
Hiroshi Matsuzawa ◽  
Hiroshi Sakai
Keyword(s):  
Disulfide Bond ◽  
Class A ◽  
Extended Spectrum

scholarly journals Characterization of beta-lactamase gene blaPER-2, which encodes an extended-spectrum class A beta-lactamase.

1996 ◽  
Vol 40 (3) ◽  
pp. 616-620 ◽  
Author(s):  
A Bauernfeind ◽  
I Stemplinger ◽  
R Jungwirth ◽  
P Mangold ◽  
S Amann ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Beta Lactamase ◽  
Reading Frame ◽  
Beta Lactamases ◽  
Class A ◽  
Extended Spectrum ◽  
The Family ◽  
Extended Spectrum Beta Lactamases ◽  
Lactamase Gene

Plasmidic extended-spectrum beta-lactamases of Ambler class A are mostly inactive against ceftibuten. Salmonella typhimurium JMC isolated in Argentina harbors a bla gene located on a plasmid (pMVP-5) which confers transferable resistance to oxyiminocephalosporins, aztreonam, and ceftibuten. The beta-lactamase PER-2 (formerly ceftibutenase-1; CTI-1) is highly susceptible to inhibition by clavulanate and is located at a pI of 5.4 after isoelectric focusing. The blaPER-2 gene was cloned and sequenced. The nucleotide sequence of a 2.2-kb insert in vector pBluescript includes an open reading frame of 927 bp. Comparison of the deduced amino acid sequence of PER-2 with those of other beta-lactamases indicates that PER-2 is not closely related to TEM or SHV enzymes (25 to 26% homology). PER-2 is most closely related to PER-1 (86.4% homology), an Ambler class A enzyme first detected in Pseudomonas aeruginosa. An enzyme with an amino acid sequence identical to that of PER-1, meanwhile, was found in various members of the family Enterobacteriaceae isolated from patients in Turkey. Our data indicate that PER-2 and PER-1 represent a new group of Ambler class A extended-spectrum beta-lactamases. PER-2 so far has been detected only in pathogens (S. typhimurium, Escherichia coli, Klebsiella pneumoniae, Proteus mirabilis) isolated from patients in South America, while the incidence of PER-1-producing strains so far has been restricted to Turkey, where it occurs both in members of the family Enterobacteriaceae and in P. aeruginosa.

scholarly journals Frequency and diversity of Class A extended-spectrum β-lactamases in hospitals of the Auvergne, France: a 2 year prospective study

2004 ◽  
Vol 54 (3) ◽  
pp. 634-639 ◽  
Author(s):  
C. De Champs ◽  
C. Chanal ◽  
D. Sirot ◽  
R. Baraduc ◽  
J. P. Romaszko ◽  
...  
Keyword(s):  
Prospective Study ◽  
Class A ◽  
Extended Spectrum

Prevalence of Class A Extended-Spectrum β-Lactamases in Clinical Isolates of Acinetobacter baumannii and Pseudomonas aeruginosa

2006 ◽  
Vol 26 (1) ◽  
pp. 14-20 ◽  
Author(s):  
Se Jin Oh ◽  
Sang Uk Lee ◽  
Hyun Yong Hwang ◽  
Il Kwon Bae ◽  
Hyun Soo Jo ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Acinetobacter Baumannii ◽  
Clinical Isolates ◽  
Class A ◽  
Extended Spectrum

scholarly journals Acyl-intermediate Structures of the Extended-spectrum Class A β-Lactamase, Toho-1, in Complex with Cefotaxime, Cephalothin, and Benzylpenicillin

2002 ◽  
Vol 277 (48) ◽  
pp. 46601-46608 ◽  
Author(s):  
Tatsuro Shimamura ◽  
Akiko Ibuka ◽  
Shinya Fushinobu ◽  
Takayoshi Wakagi ◽  
Masaji Ishiguro ◽  
...  
Keyword(s):  
Class A ◽  
Extended Spectrum

Genetic and biochemical characterization of GES-5, an extended-spectrum class A β-lactamase from Klebsiella pneumoniae

2007 ◽  
Vol 58 (4) ◽  
pp. 465-468 ◽  
Author(s):  
Il Kwon Bae ◽  
You-Nae Lee ◽  
Seok Hoon Jeong ◽  
Seong Geun Hong ◽  
Jung Hun Lee ◽  
...  
Keyword(s):  
Klebsiella Pneumoniae ◽  
Biochemical Characterization ◽  
Class A ◽  
Extended Spectrum

scholarly journals Interactions of Ceftobiprole with β-Lactamases from Molecular Classes A to D

2007 ◽  
Vol 51 (9) ◽  
pp. 3089-3095 ◽  
Author(s):  
Anne Marie Queenan ◽  
Wenchi Shang ◽  
Malgosia Kania ◽  
Malcolm G. P. Page ◽  
Karen Bush
Keyword(s):  
Functional Groups ◽  
Hydrolytic Stability ◽  
Enterobacter Cloacae ◽  
Class A ◽  
Extended Spectrum ◽  
Class D ◽  
The Family ◽  
Class B ◽  
The Common ◽  
Antibacterial Spectrum

ABSTRACT The interactions of ceftobiprole with purified β-lactamases from molecular classes A, B, C, and D were determined and compared with those of benzylpenicillin, cephaloridine, cefepime, and ceftazidime. Enzymes were selected from functional groups 1, 2a, 2b, 2be, 2d, 2e, and 3 to represent β-lactamases from organisms within the antibacterial spectrum of ceftobiprole. Ceftobiprole was refractory to hydrolysis by the common staphylococcal PC1 β-lactamase, the class A TEM-1 β-lactamase, and the class C AmpC β-lactamase but was labile to hydrolysis by class B, class D, and class A extended-spectrum β-lactamases. Cefepime and ceftazidime followed similar patterns. In most cases, the hydrolytic stability of a substrate correlated with the MIC for the producing organism. Ceftobiprole and cefepime generally had lower MICs than ceftazidime for AmpC-producing organisms, particularly AmpC-overexpressing Enterobacter cloacae organisms. However, all three cephalosporins were hydrolyzed very slowly by AmpC cephalosporinases, suggesting that factors other than β-lactamase stability contribute to lower ceftobiprole and cefepime MICs against many members of the family Enterobacteriaceae.

scholarly journals Incidence of class A extended-spectrum -lactamases in Champagne-Ardenne (France): a 1 year prospective study

2007 ◽  
Vol 61 (1) ◽  
pp. 231-232 ◽  
Author(s):  
L. Brasme ◽  
P. Nordmann ◽  
F. Fidel ◽  
M. F. Lartigue ◽  
O. Bajolet ◽  
...  
Keyword(s):  
Prospective Study ◽  
Class A ◽  
Extended Spectrum

scholarly journals Identification of Novel VEB β-Lactamase Enzymes and Their Impact on Avibactam Inhibition

2016 ◽  
Vol 60 (5) ◽  
pp. 3183-3186 ◽  
Author(s):  
Sushmita D. Lahiri ◽  
Richard A. Alm
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Binding Pocket ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Content Type ◽  
Class A ◽  
Extended Spectrum ◽  
Class C

ABSTRACTCeftazidime-avibactam has activity againstPseudomonas aeruginosaandEnterobacteriaceaeexpressing numerous class A and class C β-lactamases, although the ability to inhibit many minor enzyme variants has not been established. Novel VEB class A β-lactamases were identified during characterization of surveillance isolates. The cloned novel VEB β-lactamases possessed an extended-spectrum β-lactamase phenotype and were inhibited by avibactam in a concentration-dependent manner. The residues that comprised the avibactam binding pocket were either identical or functionally conserved. These data demonstrate that avibactam can inhibit VEB β-lactamases.

Cloning of a Chryseobacterium(Flavobacterium) meningosepticum Chromosomal Gene (blaACME) Encoding an Extended-Spectrum Class A β-Lactamase Related to the BacteroidesCephalosporinases and the VEB-1 and PER β-Lactamases

1999 ◽  
Vol 43 (9) ◽  
pp. 2193-2199 ◽  
Author(s):  
Gian Maria Rossolini ◽  
Nicola Franceschini ◽  
Laura Lauretti ◽  
Berardo Caravelli ◽  
Maria Letizia Riccio ◽  
...  
Keyword(s):  
Kinetic Parameters ◽  
Genomic Library ◽  
Expression System ◽  
Plasmid Vector ◽  
Gel Permeation Chromatography ◽  
Exchange Chromatography ◽  
Class A ◽  
Extended Spectrum ◽  
Cloned Gene ◽  
Chromatography Step

ABSTRACT In addition to the BlaB metallo-β-lactamase,Chryseobacterium (Flavobacterium)meningosepticum CCUG 4310 (NCTC 10585) constitutively produces a 31-kDa active-site serine β-lactamase, named CME-1, with an alkaline isoelectric pH. The blaA CME gene that encodes the latter enzyme was isolated from a genomic library constructed in the Escherichia coli plasmid vector pACYC184 by screening for cefuroxime-resistant clones. Sequence analysis revealed that the CME-1 enzyme is a new class A β-lactamase structurally divergent from the other members of this class, being most closely related to the VEB-1 (also named CEF-1) and PER β-lactamases and the Bacteroides chromosomal cephalosporinases. TheblaA CME determinant is located on the chromosome and exhibits features typical of those of C. meningosepticum resident genes. The CME-1 protein was purified from an E. coli strain that overexpresses the cloned gene via a T7-based expression system by means of an anion-exchange chromatography step followed by a gel permeation chromatography step. Kinetic parameters for several substrates were determined. CME-1 is a clavulanic acid-susceptible extended-spectrum β-lactamase that hydrolyzes most cephalosporins, penicillins, and monobactams but that does not hydrolyze cephamycins and carbapenems. The enzyme exhibits strikingly different kinetic parameters for different classes of β-lactams, with both Km andk cat values much higher for cephalosporins than for penicillins and monobactams. However, the variability of both kinetic parameters resulted in overall similar acylation rates (k cat/Km ratios) for all types of β-lactam substrates.

Ultrahigh Resolution Structure of a Class A β-Lactamase: On the Mechanism and Specificity of the Extended-spectrum SHV-2 Enzyme

2003 ◽  
Vol 328 (1) ◽  
pp. 289-301 ◽  
Author(s):  
Michiyoshi Nukaga ◽  
Kayoko Mayama ◽  
Andrea M. Hujer ◽  
Robert A. Bonomo ◽  
James R. Knox
Keyword(s):  
Ultrahigh Resolution ◽  
Class A ◽  
Extended Spectrum ◽  
Resolution Structure
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