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Re-examining the role of Lys67 in class C β-lactamase catalysis
Article first published online: 11 JAN 2009
DOI: 10.1002/pro.60
Copyright © 2009 The Protein Society
Additional Information
How to Cite
Chen, Y., McReynolds, A. and Shoichet, B. K. (2009), Re-examining the role of Lys67 in class C β-lactamase catalysis. Protein Science, 18: 662–669. doi: 10.1002/pro.60
Publication History
- Issue published online: 23 FEB 2009
- Article first published online: 11 JAN 2009
- Accepted manuscript online: 11 JAN 2009 12:00AM EST
- Manuscript Accepted: 29 DEC 2008
- Manuscript Revised: 19 DEC 2008
- Manuscript Received: 20 OCT 2008
Funded by
- NIH. Grant Number: GM63813
References
- 1( 1994) Inactivation of antibiotics and the dissemination of resistance genes. Science 264: 375–382.
- 2, , ( 2005) Bacterial resistance to β-lactam antibiotics: compelling opportunism, compelling opportunity. Chem Rev 105: 395–424.
- 3, , , , , , , ( 1990) Refined crystal structure of β-lactamase from Citrobacter freundii indicates a mechanism for β-lactam hydrolysis. Nature 343: 284–288.
- 4, , , , , , ( 1995) The enigmatic catalytic mechanism of active-site serine β-lactamases. Biochem Pharmacol 49: 1171–1178.
- 5, , , ( 2002) Structural milestones in the pathway of an amide hydrolase: substrate, acyl, and product complexes of cephalothin with AmpC b-lactamase. Structure 10: 413–424.
- 6, , ( 1994) The role of Lysine-67 in a class C ß-lactamase is mainly electrostatic. Biochem J 302: 1–4.
- 7, , , ( 2004) Mixed quantum mechanical/molecular mechanical (QM/MM) study of the deacylation reaction in a penicillin binding protein (PBP) versus in a class C β-lactamase. J Am Chem Soc 126: 7652–7664.
- 8, , , , ( 2006) The deacylation mechanism of AmpC β-lactamase at ultrahigh resolution. J Am Chem Soc 128: 2970–2976.
- 9, , , , , , ( 1990) Role of lysine-67 in the active site of class C β-lactamase from Citrobacter freundii GN346. Eur J Biochem 188: 15–22.Direct Link:
- 10, , , ( 1994) The role of tyrosine 150 in catalysis of ß-lactam hydrolysis by AmpC ß-Lactamase from Escherichia coli investigated by site-directed mutagenesis. Biochemistry 33: 8577–8586.
- 11, , , ( 1996) The roles of residues Tyr150, Glu272 and His314 in class C ß-Lactamases. Proteins 25: 473–485.
- 12, , , , , ( 1994) Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: mechanistic interpretation of a β-lactamase transition-state analog. Biochemistry 33: 6762–6772.
- 13, , , ( 1997) Nuances of mechanisms and their implications for evolution of the versatile β-lactamase activity: from biosynthetic enzymes to drug resistance factors. J Am Chem Soc 119: 7619–7625.
- 14, , ( 2000) Crystal structures of substrate and inhibitor complexes with AmpC b-lactamase: possible implications for substrate-assisted catalysis. J Am Chem Soc 122: 10504–10512.
- 15, , , ( 1993) Structure of a phosphonate-inhibited β-lactamase. An analog of the tetrahedral transition state/intermediate of β-lactam hydrolysis. J Mol Biol 234: 165–178.
- 16, ( 1997) Effectiveness of tetrahedral adducts as transition-state analogs and inhibitors of the class C β-lactamase of Enterobacter cloacae P99. J Am Chem Soc 119: 1529–1538.
- 17, , , , , ( 1999) The complexed structure and antimicrobial activity of a non-β-lactam inhibitor of AmpC β-lactamase. Protein Sci 8: 2330–2337.Direct Link:
- 18, , , , , ( 2003) Inhibition of class A and class C β-lactamases by penems: crystallographic structures of a novel 1,4-thiazepine intermediate. Biochemistry 42: 13152–13159.
- 19, ( 2001) Reaction of Lys-Tyr-Lys triad mimics with benzylpenicillin: insight into the role of Tyr150 in class C β-lactamase. Bioorg Med Chem Lett 11: 1161–1164.
- 20, , , , ( 2003) pKa measurements from nuclear magnetic resonance of tyrosine-150 in class C β-lactamase. Biochem J 371: 175–181.
- 21, , , , ( 2003) Thermodynamic cycle analysis and inhibitor design against β-lactamase. Biochemistry 42: 14483–14491.
- 22, , ( 1982) The chemical reactivity of penicillins and other β-lactam antibiotics. J Chem Soc Perkin Trans 2: 1185–1192.
- 23, , , ( 1996) Kinetics and mechanism of the hydrolysis of depsipeptides catalyzed by the β-lactamase of Enterobacter cloacae P99. Biochemistry 35: 3595–3603.
- 24, , ( 1998) Catalytic properties of class A β-lactamases: efficiency and diversity. Biochem J 330: 581–598.
- 25, ( 2002) Structure-based approach for binding site identification on AmpC β-lactamase. J Med Chem 45: 3222–3234.
- 26, , , , , , , ( 2004) The importance of a critical protonation state and the fate of the catalytic steps in class A β-lactamases and penicillin-binding proteins. J Biol Chem 279: 34665–34673.
- 27, , , , ( 2007) Catalytic mechanism of penicillin-binding protein 5 of Escherichia coli. Biochemistry 46: 10113–10121.
- 28, , , ( 2008) Investigation of the mechanism of the cell wall DD-carboxypeptidase reaction of penicillin-binding protein 5 of Escherichia coli by quantum mechanics/molecular mechanics calculations. J Am Chem Soc 130: 9293–9303.
- 29, , , ( 2005) Ab initio QM/MM study of class A β-lactamase acylation: dual participation of Glu166 and Lys73 in a concerted base promotion of Ser70. J Am Chem Soc 127: 15397–15407.
- 30, ( 1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307–326.
- 31Collaborative Computational Project Number 4 ( 1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760–763.Direct Link:
- 32, ( 2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126–2132.Direct Link:
- 33, , , ( 1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26: 283–291.Direct Link:

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