Interactions of coenzyme a with the aminoglycoside acetyltransferase (3)-IIIb and thermodynamics of a ternary system

Biochemistry

Volumn 49, Issue 19, 2010, Pages 4036-4042

  Norris, Adrianne L ^a   Serpersu, Engin H ^a,b  

^a UNIVERSITY OF TENNESSEE   (United States)

^b OAK RIDGE NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2-DEOXYSTREPTAMINE; ACETYL COENZYME A; AMINOGLYCOSIDE ACETYLTRANSFERASE; AMINOGLYCOSIDE ANTIBIOTICS; AMINOGLYCOSIDES; ANTIBIOTIC BINDING; CATALYTIC SITES; CO-SUBSTRATE; COENZYME A; COFACTORS; DYNAMIC NATURE; ENTROPIC CONTRIBUTIONS; EXPERIMENTAL TECHNIQUES; HIGH-AFFINITY SITES; KINETIC CHARACTERIZATION; MALONYL-COA;

ANTIBIOTICS; ENTHALPY; ENZYMES; HUMAN REHABILITATION ENGINEERING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SLOW LIGHT; SUBSTRATES; TERNARY SYSTEMS; THERMODYNAMICS;

BINDING SITES;

2 DEOXYSTREPTAMINE; ACETYL COENZYME A; ACYLTRANSFERASE; AMINOGLYCOSIDE ACETYLTRANSFERASE IIIB; COENZYME A; FRAMYCETIN; KANAMYCIN A; KANAMYCIN B; PAROMOMYCIN; RIBOSTAMYCIN; TOBRAMYCIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING SITE; ENZYME DEGRADATION; ENZYME SUBSTRATE; ESCHERICHIA COLI; FLUORESCENCE; KINETICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; THERMODYNAMICS;

ACETYLTRANSFERASES; COENZYME A; ENTROPY; ESCHERICHIA COLI; HEXOSAMINES; KINETICS; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

EID: 77952351391     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1001568     Document Type: Article

References (26)

1. Spotts, C. R. and Stanier, R. Y. (1961) Mechanism of Streptomycin Action on Bacteria: Unitary Hypothesis Nature 192, 633-637
2. Moazed, D. and Noller, H. F. (1987) Interaction of Antibiotics with Functional Sites in 16s Ribosomal-RNA Nature 327, 389-394
3. Fong, D. H. and Berghuis, A. M. (2002) Substrate promiscuity of an aminoglycoside antibiotic resistance enzyme via target mimicry EMBO J. 21, 2323-2331
4. Nurizzo, D., Shewry, S. C., Perlin, M. H., Brown, S. A., Dholakia, J. N., Fuchs, R. L., Deva, T., Baker, E. N., and Smith, C. A. (2003) The crystal structure of aminoglycoside-3′-phosphotransferase-IIa, an enzyme responsible for antibiotic resistance J. Mol. Biol. 327, 491-506
5. Pedersen, L. C., Benning, M. M., and Holden, H. M. (1995) Structural Investigation of the Antibiotic and ATP-Binding Sites in Kanamycin Nucleotidyltransferase Biochemistry 34, 13305-13311
6. Vetting, M. W., Hegde, S. S., Javid-Majd, F., Blanchard, J. S., and Roderick, S. L. (2002) Aminoglycoside 2′-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates Nat. Struct. Biol. 9, 653-658
7. Wolf, E., Vassilev, A., Makino, Y., Sali, A., Nakatani, Y., and Burley, S. K. (1998) Crystal structure of a GCN5-related N -acetyltransferase: Serratia marcescens aminoglycoside 3- N -acetyltransferase Cell 94, 439-449
8. Wybenga-Groot, L. E., Draker, K., Wright, G. D., and Berghuis, A. M. (1999) Crystal structure of an aminoglycoside 6′-N-acetyltransferase: Defining the GCN5-related N-acetyltransferase superfamily fold Struct. Folding Des. 7, 497-507
9. Young, P. G., Walanj, R., Lakshmi, V., Byrnes, L. J., Metcalf, P., Baker, E. N., Vakulenko, S. B., and Smith, C. A. (2009) The Crystal Structures of Substrate and Nucleotide Complexes of Enterococcus faecium Aminoglycoside- 2′-Phosphotransferase-IIa [APH(2′)-IIa] Provide Insights into Substrate Selectivity in the APH(2′) Subfamily J. Bacteriol. 191, 4133-4143
10. Ozen, C., Malek, J. M., and Serpersu, E. H. (2006) Dissection of aminoglycoside-enzyme interactions: A calorimetric and NMR study of neomycin B binding to the aminoglycoside phosphotransferase(3′)-IIIa J. Am. Chem. Soc. 128, 15248-15254
11. Ozen, C., Norris, A. L., Land, M. L., Tjioe, E., and Serpersu, E. H. (2008) Detection of specific solvent rearrangement regions of an enzyme: NMR and ITC studies with aminoglycoside phosphotransferase(3′)-IIIa Biochemistry 47, 40-49
12. Ozen, C. and Serpersu, E. H. (2004) Thermodynamics of aminoglycoside binding to aminoglycoside-3′-phosphotransferase IIIa studied by isothermal titration calorimetry Biochemistry 43, 14667-14675
13. Wright, E. and Serpersu, E. H. (2005) Enzyme-Substrate Interactions with an Antibiotic Resistance Enzyme: Aminoglycoside Nucleotidyltransferase(2′) -Ia Characterized by Kinetic and Thermodynamic Methods Biochemistry 44, 11581-11591
14. Wright, E. and Serpersu, E. H. (2006) Molecular Determinants of Affinity for Aminoglycoside Binding to the Aminoglycoside Nucleotidyltransferase(2′ )-Ia Biochemistry 45, 10243-10250
15. Hegde, S. S., Dam, T. K., Brewer, C. F., and Blanchard, J. S. (2002) Thermodynamics of aminoglycoside and acyl-coenzyme A binding to the Salmonella enterica AAC(6′)-Iy aminoglycoside N-acetyltransferase Biochemistry 41, 7519-7527
16. Hedge, S. S., Dam, T. K., Brewer, C. F., and Blanchard, J. S. (2002) Thermodynamics of aminoglycoside and acyl-coenzyme A binding to the Salmonella enterica AAC(6′)-Iy aminoglycoside N-acetyltransferase Biochemistry 41, 7519-7527
17. 2+-Liganding Amino Acid in Staphylococcal Nuclease Biochemistry 25, 68-77
18. Serpersu, E. H., Shortle, D., and Mildvan, A. S. (1987) Kinetic and magnetic resonance studies of active-site mutants of staphylococcal nuclease: Factors contributing to catalysis Biochemistry 26, 1289-1300
19. Owston, M. A. and Serpersu, E. H. (2002) Cloning, overexpression, and purification of aminoglycoside antibiotic 3-acetyltransferase-IIIb: Conformational studies with bound substrates Biochemistry 41, 10764-10770
20. Cox, J. R. and Serpersu, E. H. (1997) Biologically important conformations of aminoglycoside antibiotics bound to an aminoglycoside 3′-phosphotransferase as determined by transferred nuclear Overhauser effect spectroscopy Biochemistry 36, 2353-2359
21. Williams, J. W. and Northrop, D. B. (1978) Kinetic Mechanisms of Gentamicin Acetyltransferase-I: Antibiotic-Dependent Shift from Rapid to Nonrapid Equilibrium Random Mechanisms J. Biol. Chem. 253, 5902-5907
22. Bodenhausen, G. and Ruben, D. J. (1980) Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy Chem. Phys. Lett. 69, 185-188
23. 1H]-TROSY elements in triple resonance experiments J. Biomol. NMR 15, 181-184
24. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) Nmrpipe: A Multidimensional Spectral Processing System Based on Unix Pipes J. Biomol. NMR 6, 277-293
25. Miller, J. R., Ohren, J., Sarver, R. W., Mueller, W. T., de Dreu, P., Case, H., and Thanabal, V. (2007) Phosphopantetheine adenylyltransferase from Escherichia coli: Investigation of the kinetic mechanism and role in regulation of coenzyme a biosynthesis J. Bacteriol. 189, 8196-8205
26. Norris, A. L. and Serpersu, E. H. (2009) NMR Detected Hydrogen-Deuterium Exchange Reveals Differential Dynamics of Antibiotic- and Nucleotide-Bound Aminoglycoside Phosphotransferase 3′-IIIa J. Am. Chem. Soc. 131, 8587-8594