Deletion Mutations Conferring Substrate Spectrum Extension in the Class A beta-Lactamase
- Authors
- Hwang, Junghyun; Cho, Kwang-Hwi; Song, Han; Yi, Hyojeong; Kim, Heenam Stanley
- Issue Date
- 10월-2014
- Publisher
- AMER SOC MICROBIOLOGY
- Citation
- ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, v.58, no.10, pp.6265 - 6269
- Indexed
- SCIE
SCOPUS
- Journal Title
- ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
- Volume
- 58
- Number
- 10
- Start Page
- 6265
- End Page
- 6269
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/97327
- DOI
- 10.1128/AAC.02648-14
- ISSN
- 0066-4804
- Abstract
- We describe four new deletion mutations in a class A beta-lactamase PenA in Burkholderia thailandensis, each conferring an extended substrate spectrum. Single-amino-acid deletions T171del, I173del, and P174del and a two-amino-acid deletion, R165_T167delinsP, occurred in the omega loop, increasing the flexibility of the binding cavity. This rare collection of mutations has significance, allowing exploration of the diverse evolutionary trajectories of beta-lactamases and as potential future mutations conferring high-level ceftazidime resistance on isolates from clinical settings, compared with amino acid substitution mutations.
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Collections - College of Health Sciences > School of Biosystems and Biomedical Sciences > 1. Journal Articles
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