[en] Site-directed mutagenesis of CphA indicated that prolines in the P158-P172 loop are essential for the stability and the catalytic activity of subclass B2 metallo-beta-lactamases against carbapenems. The sequential substitution of proline led to a decrease of the catalytic efficiency of the variant compared to the wild-type (WT) enzyme but also to a higher affinity for the binding of the second zinc ion.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Bottoni, Carlo
Perilli, Mariagrazia
Marcoccia, Francesca
Piccirilli, Alessandra
Pellegrini, Cristina
Colapietro, Martina
Sabatini, Alessia
Celenza, Giuseppe
Kerff, Frédéric ; Université de Liège > Département des sciences de la vie > Centre d'ingénierie des protéines
Amicosante, Gianfranco
Galleni, Moreno ; Université de Liège > Département des sciences de la vie > Macromolécules biologiques
Mercuri, Paola ; Université de Liège > Département des sciences de la vie > Macromolécules biologiques
Language :
English
Title :
Kinetic Studies on CphA Mutants Reveal the Role of the P158-P172 Loop in Activity versus Carbapenems.
Publication date :
2016
Journal title :
Antimicrobial Agents and Chemotherapy
ISSN :
0066-4804
eISSN :
1098-6596
Publisher :
American Society for Microbiology, Washington, United States - District of Columbia
Volume :
60
Issue :
5
Pages :
3123-6
Peer reviewed :
Peer Reviewed verified by ORBi
Commentary :
Copyright (c) 2016, American Society for Microbiology. All Rights Reserved.
scite shows how a scientific paper has been cited by providing the context of the citation, a classification describing whether it supports, mentions, or contrasts the cited claim, and a label indicating in which section the citation was made.
Bibliography
Segatore B, Massidda O, Satta G, Setacci D, Amicosante G. 1993. High specificity of CphA-encoded metallo-β-lactamase from Aeromonas hydrophila AE036 for carbapenems and its contribution to β-lactamase resistance. Antimicrob Agents Chemother 37:1324-1328. http://dx.doi.org/10.1128/AAC.37.6.1324.
Carfi A, Pares S, Duée E, Galleni M, Duez C, Frère JM, Dideberg O. 1995. The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J 14:4914-4921.
Garau G, Garcia-Sàez I, Bebrone C, Anne C, Mercuri P, Galleni M, Frère JM, Dideberg O. 2004. Update of the standard numbering scheme for class B β-lactamases. Antimicrob Agents Chemother 48:2347-2349. http://dx.doi.org/10.1128/AAC.48.7.2347-2349.2004.
Clinical and Laboratory Standards Institute. 2012. Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically; approved standard-9th ed. CLSI document M09-A7. Clinical and Laboratory Standards Institute, Wayne, PA.
Hernandez Valladares M, Felici A, Weber G, Adolph HW, Zeppezauer M, Rossolini GM, Amicosante G, Frère JM, Galleni M. 1997. Zn(II) dependence of the Aeromonas hydrophila AE036 metallo-β-lactamase activity and stability. Biochemistry 36:11534-11541. http://dx.doi.org/10.1021/bi971056h.
Fonseca F, Arthur CJ, Bromley EH, Samyn B, Moerman P, Saavedra MJ, Correia A, Spencer J. 2011. Biochemical characterization of Sfh-I, a subclass B2 metallo-beta-lactamase from Serratia fonticola UTAD54. Antimicrob Agents Chemother 55:5392-5395. http://dx.doi.org/10.1128/AAC.00429-11.21876065.
Fonseca F, Bromley EH, Saavedra MJ, Correia A, Spencer J. 2011. Crystal structure of Serratia fonticola Sfh-I: activation of the nucleophile in monozinc metallo-β-lactamases. J Mol Biol 411:951-959. http://dx.doi.org/10.1016/j.jmb.2011.06.043.
Bebrone C, Delbrück H, Kupper MB, Schlömer P, Willmann C, Frère JM, Fischer R, Galleni M, Hoffmann KM. 2009. The structure of the di-zinc subclass B2 metallo-β-lactamase CphA reveals that the second inhibitory zinc ion binds in the histidine site. Antimicrob Agents Chemother 53:4464-4471. http://dx.doi.org/10.1128/AAC.00288-09.
This website uses cookies to improve user experience. Read more
Save & Close
Accept all
Decline all
Show detailsHide details
Cookie declaration
About cookies
Strictly necessary
Performance
Strictly necessary cookies allow core website functionality such as user login and account management. The website cannot be used properly without strictly necessary cookies.
This cookie is used by Cookie-Script.com service to remember visitor cookie consent preferences. It is necessary for Cookie-Script.com cookie banner to work properly.
Performance cookies are used to see how visitors use the website, eg. analytics cookies. Those cookies cannot be used to directly identify a certain visitor.
Used to store the attribution information, the referrer initially used to visit the website
Cookies are small text files that are placed on your computer by websites that you visit. Websites use cookies to help users navigate efficiently and perform certain functions. Cookies that are required for the website to operate properly are allowed to be set without your permission. All other cookies need to be approved before they can be set in the browser.
You can change your consent to cookie usage at any time on our Privacy Policy page.
