scholarly journals Capnocytophaga ochracea: Characterization of a Plasmid-Encoded Extended-Spectrum TEM-17 β-Lactamase in the Phylum Flavobacter-Bacteroides

2000 ◽  
Vol 44 (3) ◽  
pp. 760-762 ◽  
Author(s):  
Agnes Rosenau ◽  
Blandine Cattier ◽  
Nathalie Gousset ◽  
Patrick Harriau ◽  
Alain Philippon ◽  
...  
Keyword(s):  
Amino Acid ◽  
Clinical Isolate ◽  
Amino Acid Substitution ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid ◽  
Extended Spectrum

ABSTRACT A plasmid-encoded extended-spectrum TEM β-lactamase with a pI of 5.5 was detected in a Capnocytophaga ochracea clinical isolate. The bla gene was associated with a strong TEM-2 promoter and was derived from bla TEM-1a with a single-amino-acid substitution: Glu104→Lys, previously assigned to TEM-17, which is thus the first TEM β-lactamase to be reported in the phylum Flavobacter-Bacteroides.

scholarly journals A New SHV-Derived Extended-Spectrum β-Lactamase (SHV-24) That Hydrolyzes Ceftazidime through a Single-Amino-Acid Substitution (D179G) in the Ω-Loop

2000 ◽  
Vol 44 (6) ◽  
pp. 1725-1727 ◽  
Author(s):  
Hiroshi Kurokawa ◽  
Tetsuya Yagi ◽  
Naohiro Shibata ◽  
Keigo Shibayama ◽  
Kazunari Kamachi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Clinical Isolate ◽  
Amino Acid Substitution ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid ◽  
Extended Spectrum ◽  
High Level ◽  
Level Resistance

ABSTRACT A new SHV-derived extended-spectrum β-lactamase (SHV-24) conferring high-level resistance to ceftazidime but not cefotaxime and cefazolin was identified in Japan. This enzyme was encoded by a transferable 150-kb plasmid from an Escherichia coliclinical isolate. The pI and Km for CAZ of this enzyme were 7.5 and 30 μM, respectively. SHV-24 was found to have a D179G substitution in the Ω-loop of the enzyme.

scholarly journals TEM-89 β-Lactamase Produced by a Proteus mirabilis Clinical Isolate: New Complex Mutant (CMT 3) with Mutations in both TEM-59 (IRT-17) and TEM-3

2001 ◽  
Vol 45 (12) ◽  
pp. 3591-3594 ◽  
Author(s):  
Catherine Neuwirth ◽  
Stephanie Madec ◽  
Eliane Siebor ◽  
Andre Pechinot ◽  
Jean-Marie Duez ◽  
...  
Keyword(s):  
Amino Acid ◽  
Clinical Isolate ◽  
Amino Acid Substitution ◽  
Proteus Mirabilis ◽  
Hydrolytic Activity ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid ◽  
Clinical Strain ◽  
Almost All

ABSTRACT TEM-89 (CMT-3) is the first complex mutant β-lactamase produced by a clinical strain of Proteus mirabilis (strain Pm 631). This new enzyme, which has a pI of 6.28, is derived from TEM-3 and has a single amino acid substitution also encountered in TEM-59 (inhibitor-resistant TEM β-lactamase IRT-17): Ser-130 to Gly. TEM-89 hydrolyzed penicillins to the same extent that TEM-3 did but lost almost all hydrolytic activity for cephalosporins and, like TEM-59, was highly resistant to inhibitors.

scholarly journals A large compressibility change of protein induced by a single amino acid substitution

1996 ◽  
Vol 5 (3) ◽  
pp. 542-545 ◽  
Author(s):  
Kunihiko Gekko ◽  
Youjiro Tamura ◽  
Eiji Ohmae ◽  
Hideyuki Hayashi ◽  
Hiroyuki Kagamiyama ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid
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