Mechanism of aminoglycoside 3'-phosphotransferase type IIIa: His188 is not a phosphate-accepting residue

Chemistry and Biology

Volumn 3, Issue 9, 1996, Pages 747-755

  Thompson, Paul R ^a   Hughes, Donald W ^b   Wright, Gerard D ^a  

^a MCMASTER UNIVERSITY   (Canada)

^b MCMASTER UNIVERSITY   (Canada)

Author keywords

aminoglycoside; antibiotic resistance; mutagenesis; PIX

Indexed keywords

ENTEROCOCCUS; STAPHYLOCOCCUS;

EID: 0030250627     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(96)90251-3     Document Type: Article

References (38)

1. Howe, R.A., Brown, N.M. & Spencer, R.C. (1996). The new threats from Gram-positive pathogens: re-emergence of things past. J. Clin. Pathol. 49, 444-449.
2. Murray, B.E. (1990). The life and times of the Enterococcus. Clin. Microbiol. Rev. 3, 46-65.
3. Moellering, R.C., Jr (1991). The Enterococcus: a classic example of the impact of antimicrobial resistance on therapeutic options. J. Antimicrob. Chemother. 28, 1-12.
4. Neu, H.C. (1992). The crisis in antibiotic resistance. Science 257, 1064-1073.
5. Davies, J. (1994). Inactivation of antibiotics and the dissemination of resistance genes. Science 264, 375-382.
6. Davies, J.E. (1991). Aminoglycoside-aminocyclitol antibiotics and their modifying enzymes. In Antibiotics in Laboratory Medicine. (Lorian, V. ed.), pp. 691-713, Williams & Wilkins, Baltimore.
7. Umezawa, H. & Kondo, S. (1982). Mechanisms of resistance to aminoglycoside antibiotics. In Aminoglycoside Antibiotics. (Umezawa, H. & Hooper, I.R., eds), pp. 267-292, Springer-Verlag, Berlin.
8. Shaw, K.J., Rather, P.N., Hare, R.S. & Miller, G.H. (1993). Molecular genetics of aminoglycoside resistance genes and familial relationships of the aminoglycoside-modifying enzymes. Microbiol. Rev. 57, 138-163.
9. Leclerq, R., et al., & Courvalin, P. (1992). Resistance of Enterococci to aminoglycosides and glycopeptides. Clin. Infect. Dis. 15, 495-501.
10. Trieu-Cuot, P. & Courvalin, P. (1983). Nucleotide sequence of the Streptococcus faecalis plasmid gene encoding the 3′5″-aminoglycoside phosphotransferase type III. Gene 23, 331-341.
11. McKay, G.A., Thompson, RR. & Wright, G.D. (1994). Broad spectrum aminoglycoside phosphotransferase type III from Enterococcus: overexpression, purification, and substrate specificity. Biochemistry 33, 6936-6944.
12. Thompson, PR., Hughes, D.W. & Wright, G.D. (1996). Regiospecificity of aminoglycoside phosphotransferase from Enterococci and Staphylococci (APH(3′)-IIIa). Biochemistry 35, 8686-8695.
13. Martin, P., Jullien, E. & Corvalin, R (1988). Nucleotide sequence of Acinetobacter baumannii aphA-6 gene: evolutionary and functional implications of sequence homologies with nucleotide-binding proteins, kinases and other aminoglycoside-modifying enzymes. Mol. Microbiol. 2, 615-625.
14. McKay, G.A. & Wright, G.D. (1995). Kinetic mechanism of aminoglycoside phosphotransferase type IIIa: evidence for a Theorell-Chance mechanism. J. Biol. Chem. 270, 24686-24692.
15. McKay, G.A. & Wright, G.D. (1996). Catalytic mechanism of enteroccal kanamycin kinase (APH(3′)-IIIa): viscosity, thio and solvent isotope effects support a Theorell-Chance mechanism. Biochemistry 35, 8680-8685.
16. Knowles, J.R. (1980). Enzyme-catalyzed phosphoryl transfer reactions. Annu. Rev. Biochem. 49, 877-919.
17. Frey, P.A. (1992). Nucleotidyltransferases and phosphotransferases: stereochemistry and covalent intermediates. In The Enzymes. (Sigman, D.S., ed.), Vol. XX, pp. 141-186, Academic Press, San Diego.
18. Blázquez, J., Davies, J. & Moreno, F. (1991). Mutations in the aphA-2 gene of transposon Tn5 mapping within the regions highly conserved in aminoglycoside-phosphotransferases strongly reduce aminoglycoside resistance. Mol. Microbiol. 5, 1511-1518.
19. Kocabiyik, S. & Perlin, M.H. (1992). Site-specific mutations of conserved C-terminal residues in aminoglycoside 3′-phosphotransferase II: phenotypic and structural analysis of mutant enzymes. Biochem. Biophys. Res. Commun. 185, 925-931.
20. Midelfort, C.F. & Rose, I.A. (1976). A stereochemical method for the detection of ATP terminal phosphate transfer in enzymatic reactions. J. Biol. Chem. 251, 5881-5887.
21. Raushel, F.M. & Villafranca, J.J. (1988). Positional isotope exchange. Crit Rev. Biochem. 23, 1-26.
22. Lundblad, R.L. (1991). Chemical Reagents for Protein Modification. (2nd edn), CRC Press, Boca Raton.
23. Villafranca, J.J. (1989). Positional isotope exchange using phosphorus-31 nuclear magnetic resonance. Methods Enzymol. 177, 390-403.
24. Spera, R.V., Jr & Farber, B.F. (1994). Multidrug-resistant Enterococcus faecium: an untreatable nosocomial pathogen. Drugs 48, 678-688.
25. Pai, E.F., Sachsenheimer, W., Schirmer, R.H. & Schulz, G.E. (1977). Substrate positions and induced-fit in crystalline adenylate kinase. J. Mol. Biol. 114, 37-45.
26. Kjeldgaard, M. & Nyborg, J. (1992). Refined structure of elongation factor EF-Tu from Escherichia coli. J. Mol. Biol. 223, 721-742.
27. Czworkowski, J., Wang, J., Steitz, T.A. & Moore, P.B. (1994). The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution. EMBO J. 13, 3661-3668.
28. Heinzel, R, Werbitzky, O., Distler, J. & Piepersberg, W. (1988). A second streptomycin-resistance gene from Streptomyces griseus codes for streptomycin-3″-phosphotransferase. Arch. Microbiol, 150, 184-192.
29. De Bondt, H., Rosenblatt, J., Jancarik, J., Jones, H.D., Morgan, D.O. & Kim, S.-H. (1993). Crystal structure of the cyclin-dependent kinase 2. Nature 363, 595-602.
30. Zhang, F., Strand, A., Robbins, D., Cobb, M.H. & Goldsmith, E.J. (1994). Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution. Nature 367, 704-711.
31. Hubbard, S.R., Wei, L., Ellis, L & Hendrickson, W.A. (1994). Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372, 746-754.
32. Zheng, J., et al., & Sowadski, J.M. (1993). Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor. Biochemistry 32, 2154-2161.
33. 4 (monobasic) of high isotopic purity. J. Label. Compounds Radiopharm. 15, 533-538.
34. 32-nucleoside 5′-triphosphates. J. Am. Chem. Soc. 87, 2265-2277.
35. Kunkel, T.A. (1985). Rapid and efficient site specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82, 488-492.
36. Sarkar, G. & Sommer, S.S. (1990). The 'megaprimer' method of site-directed mutagenesis. Biotechniques 8, 404-407.
37. Miles, E.W. (1977). Modification of histidyl residues in proteins by diethylpyrocarbonate. Methods Enzymol. 47, 431-442.
38. McKay, G.A., Robinson, R.A., Lane, W.S. & Wright, G.D. (1994). Active-site labeling of an aminoglycoside antibiotic phosphotransferase (APH(3′)-IIIa). Biochemistry 33, 14115-14120.