P174E Substitution in GES-1 and GES-5 β-Lactamases Improves Catalytic Efficiency toward Carbapenems
نویسندگان
چکیده
منابع مشابه
Kinetic and crystallographic studies of extended-spectrum GES-11, GES-12, and GES-14 β-lactamases.
GES-1 is a class A extended-spectrum β-lactamase conferring resistance to penicillins, narrow- and expanded-spectrum cephalosporins, and ceftazidime. However, GES-1 poorly hydrolyzes aztreonam and cephamycins and exhibits very low k(cat) values for carbapenems. Twenty-two GES variants have been discovered thus far, differing from each other by 1 to 3 amino acid substitutions that affect substra...
متن کاملNomenclature of GES-Type Extended-Spectrum -Lactamases
In two recently published articles, Wachino et al. designated a novel ceftazidime-hydrolyzing class A extended-spectrum -lactamase (ESBL) (GES-a) as GES-3 (4), and a new cephamycin-hydrolyzing and inhibitor-resistant class A ESBL (GESb) as GES-4 (5). In actuality, their articles are fraught with misleading nomenclature of GES-type ESBLs and controvertible conclusions on the relationship between...
متن کاملKinetic and Structural Requirements for Carbapenemase Activity in GES-Type β-Lactamases
Carbapenems are the last resort antibiotics for treatment of life-threatening infections. The GES β-lactamases are important contributors to carbapenem resistance in clinical bacterial pathogens. A single amino acid difference at position 170 of the GES-1, GES-2, and GES-5 enzymes is responsible for the expansion of their substrate profile to include carbapenem antibiotics. This highlights the ...
متن کاملA plasmid-encoded class 1 integron contains GES-type extended-spectrum β-lactamases in Enterobacteriaceae clinical isolates in Mexico.
Plasmid-located extended-spectrum-lactamase (ESBL) genes are mostly found in Enterobacteriaceae (6). A new class A ESBL was identified in Klebsiella pneumoniae. It was named GES-1, and it corresponds to the ceftazidime-hydrolyzing enzyme (8). GES-type ESBLs have emerged in a variety of countries, and there are 18 known variants (http://www.lahey.org/Studies/). In the present study, we investiga...
متن کاملIn vitro prediction of the evolution of GES-1 β-lactamase hydrolytic activity.
Resistance to β-lactams is constantly increasing due to the emergence of totally new enzymes but also to the evolution of preexisting β-lactamases. GES-1 is a clinically relevant extended-spectrum β-lactamase (ESBL) that hydrolyzes penicillins and broad-spectrum cephalosporins but spares monobactams and carbapenems. However, several GES-1 variants (i.e., GES-2 and GES-5) previously identified a...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Antimicrobial Agents and Chemotherapy
سال: 2018
ISSN: 0066-4804,1098-6596
DOI: 10.1128/aac.01851-17