Understanding the molecular determinants of substrate and inhibitor specificities in the carbapenemase KPC-2: Exploring the roles of Arg220 and Glu276

Antimicrobial Agents and Chemotherapy

Volumn 56, Issue 8, 2012, Pages 4428-4438

  Papp Wallace, Krisztina M ^a,b   Taracila, Magdalena A ^b   Smith, Kerri M ^c   Xu, Yan ^c   Bonomo, Robert A ^a,b  

^a LOUIS STOKES CLEVELAND VA MEDICAL CENTER   (United States)

^b CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c CLEVELAND STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMPICILLIN; ARGININE; CARBAPENEMASE; CARBAPENEMASE KPC2; CEFALOTIN; CEFOTAXIME; CEFTAZIDIME; CLAVULANIC ACID; DORIPENEM; ERTAPENEM; GLUTAMINE; IMIPENEM; MEROPENEM; NITROCEFIN; PIPERACILLIN; SULBACTAM; TAZOBACTAM; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME INHIBITION; ENZYME SPECIFICITY; ESCHERICHIA COLI; KLEBSIELLA PNEUMONIAE; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; PRIORITY JOURNAL; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BETA-LACTAM RESISTANCE; BETA-LACTAMASES; BETA-LACTAMS; CATALYTIC DOMAIN; CLAVULANIC ACID; KLEBSIELLA PNEUMONIAE; MICROBIAL SENSITIVITY TESTS; PROTEIN STRUCTURE, QUATERNARY; SEQUENCE ANALYSIS, PROTEIN; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84864394566     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.05769-11     Document Type: Article

References (26)

1. Ambler RP. 1980. The structure of β-lactamases. Philos. Trans. R. Soc. Lond. B Biol. Sci. 289:321-331.
2. Braine T. 2011. Race against time to develop new antibiotics. Bull. World Health Organ. 89:88-89.
3. Brown RP, Aplin RT, Schofield CJ. 1996. Inhibition of TEM-2 β-lactamase from Escherichia coli by clavulanic acid: observation of intermediates by electrospray ionization mass spectrometry. Biochemistry 35:12421-12432. (Pubitemid 26318037)
4. Carmeli Y, et al. 2010. Controlling the spread of carbapenemase-producing Gram-negatives: therapeutic approach and infection control. Clin. Microbiol. Infect. 16:102-111.
5. Clinical and Laboratory Standards Institute. 2008. Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically. Approved standard - 1st ed. Clinical and Laboratory Standards Institute, Wayne, PA.
6. Drawz SM, Bonomo RA. 2010. Three decades of β-lactamase inhibitors. Clin. Microbiol. Rev. 23:160-201.
7. KPC- containing Klebsiella pneumoniae isolates detected in different institutions in the Eastern USA. J. Antimicrob. Chemother. 63:427-437.
8. Fisher J, Charnas RL, Knowles JR. 1978. Kinetic studies on the inactivation of Escherichia coli RTEM β-lactamase by clavulanic acid. Biochemistry 17:2180-2184. (Pubitemid 8341143)
9. Imtiaz U, et al. 1993. Inactivation of class A β-lactamases by clavulanic acid: the role of arginine-244 in a proposed nonconcerted sequence of events. J. Am. Chem. Soc. 115:4435-4442. (Pubitemid 23197971)
10. Ishii Y, et al. 1995. Cloning and sequence of the gene encoding a cefotaxime-hydrolyzing class A β-lactamase isolated from Escherichia coli. Antimicrob. Agents Chemother. 39:2269-2275.
11. Jacob-Dubuisson F, Lamotte-Brasseur J, Dideberg O, Joris B, Frere JM. 1991. Arginine 220 is a critical residue for the catalytic mechanism of the Streptomyces albus G β-lactamase. Protein Eng. 4:811-819.
12. Ke W, et al. 2012. Crystal structures of KPC-2 β-lactamase in complex with 3-NPBA and PSR-3-226. Antimicrob. Agents Chemother. 56:2713-2718.
13. Ke W, Bethel CR, Thomson JM, Bonomo RA, van den Akker F. 2007. Crystal structure of KPC-2: insights into carbapenemase activity in class A β-lactamases. Biochemistry 46:5732-5740. (Pubitemid 46764122)
14. Kelly JA, Frere JM, Duez C, Ghuysen JM. 1981. Interactions between non-classical β-lactam compounds and the β-lactamases of Actinomadura R39 and Streptomyces albus G. Biochem. J. 199:137-143. (Pubitemid 12198619)
15. Marciano DC, Brown NG, Palzkill T. 2009. Analysis of the plasticity of location of the Arg244 positive charge within the active site of the TEM-1 β-lactamase. Protein Sci. 18:2080-2089.
16. Papp-Wallace KM, et al. 2010. Inhibitor resistance in the KPC-2 β-lactamase, a preeminent property of this class A β-lactamase. Antimicrob. Agents Chemother. 54:890-897.
17. Papp-Wallace KM, et al. 2010. Substrate selectivity and a novel role in inhibitor discrimination by residue 237 in the KPC-2 β-lactamase. Antimicrob. Agents Chemother. 54:2867-2877.
18. Papp-Wallace KM, et al. 2010. Elucidating the role of Trp105 in the KPC-2 β-lactamase. Protein Sci. 19:1714-1727.
19. Paterson DL, Bonomo RA. 2005. Extended-spectrum β-lactamases: a clinical update. Clin. Microbiol. Rev. 18:657-686.
20. Perez F, Endimiani A, Hujer KM, Bonomo RA. 2007. The continuing challenge of ESBLs. Curr. Opin. Pharmacol. 7:459-469. (Pubitemid 47560222)
21. Queenan AM, Bush K. 2007. Carbapenemases: the versatile β-lactamases. Clin. Microbiol. Rev. 20:440-458.
22. Thomson JM, Distler AM, Prati F, Bonomo RA. 2006. Probing active site chemistry in SHV β-lactamase variants at Ambler position 244. Understanding unique properties of inhibitor resistance. J. Biol. Chem. 281:26734-26744. (Pubitemid 44401882)
23. Walsh TR. 2010. Emerging carbapenemases: a global perspective. Int. J. Antimicrob. Agents 36(Suppl. 3):S8-S14.
24. Weerasuriya K, Stelling J, O'Brien TF. 2010. Containing antimicrobial resistance: a renewed effort. Bull. World Health Organ. 88:878. doi: 10.2471/BLT.10.084236.
25. Yigit H, et al. 2001. Novel carbapenem-hydrolyzing β-lactamase, KPC-1, from a carbapenem-resistant strain of Klebsiella pneumoniae. Antimicrob. Agents Chemother. 45:1151-1161. (Pubitemid 32230996)
26. Zafaralla G, Manavathu EK, Lerner SA, Mobashery S. 1992. Elucidation of the role of arginine-244 in the turnover processes of class A β-lactamases. Biochemistry 31:3847-3852.