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Structural and dynamical origins of catalytic differences between OXA-143 and OXA-231

Grant number: 17/22822-3
Support type:Scholarships abroad - Research
Effective date (Start): August 01, 2018
Effective date (End): July 31, 2019
Field of knowledge:Biological Sciences - Biochemistry
Principal Investigator:Denize Cristina Favaro
Grantee:Denize Cristina Favaro
Host: Anthony Mittermaier
Home Institution: Instituto de Química (IQ). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil
Local de pesquisa : McGill University, Montreal, Canada  

Abstract

²-lactams have been the drug of choice for the treatment of bacterial infection for many decades. However, due in part to the misuse of these antimicrobial agents, drug-resistant bacteria are posing a growing threat to global health. According to the WHO, 9 of the 12 most dangerous families of bacteria are resistant to ²-lactam antibiotics, due to the presence of ²-lactamase enzymes. Preliminary results involving ²-lactamases of the subclass oxacilinase (OXAs) suggest that both enzyme structure and internal dynamics are essential for its antibiotic resistance activity. The main goal of the present project is to elucidate the role of conformational dynamics in OXA-CHDL function and understand how they arose during evolution.

Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
ANTUNES, VICTOR U.; LLONTOP, EDGAR E.; VASCONCELOS, FERNANDA N. DA COSTA; DE LOS SANTOS, YOSSEF LOPEZ; OLIVEIRA, RONALDO J.; LINCOPAN, NILTON; FARAH, CHUCK S.; DOUCET, NICOLAS; MITTERMAIER, ANTHONY; FAVARO, DENIZE C. Importance of the beta 5-beta 6 Loop for the Structure, Catalytic Efficiency, and Stability of Carbapenem-Hydrolyzing Class D beta-Lactamase Subfamily OXA-143. BIOCHEMISTRY, v. 58, n. 34, p. 3604-3616, AUG 27 2019. Web of Science Citations: 0.

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