Substrate Spectrum Extension of PenA in Burkholderia thailandensis with a Single Amino Acid Deletion, Glu168del
- Authors
- Yi, Hyojeong; Kim, Karan; Cho, Kwang-Hwi; Jung, Oksung; Kim, Heenam Stanley
- Issue Date
- 7월-2012
- Publisher
- AMER SOC MICROBIOLOGY
- Keywords
- A BETA-LACTAMASES; ANTIMICROBIAL SUSCEPTIBILITY; PSEUDOMALLEI; CEFTAZIDIME; DIVERSITY
- Citation
- ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, v.56, no.7, pp.4005 - 4008
- Indexed
- SCIE
SCOPUS
- Journal Title
- ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
- Volume
- 56
- Number
- 7
- Start Page
- 4005
- End Page
- 4008
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/108103
- DOI
- 10.1128/AAC.00598-12
- ISSN
- 0066-4804
- Abstract
- We describe a deletion mutation in a class A beta-lactamase, PenA, of Burkholderia thailandensis that extended the substrate spectrum of the enzyme to include ceftazidime. Glu168del was located in a functional domain called the omega loop causing expansion of the space in the loop, which in turn increased flexibility at the active site. This deletion mutation represents a rare but significant alternative mechanical path to substrate spectrum extension in PenA besides more common substitution mutations.
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Collections - College of Health Sciences > School of Biosystems and Biomedical Sciences > 1. Journal Articles
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