Transient state kinetic studies of the MutT-catalyzed nucleoside triphosphate pyrophosphohydrolase reaction

Biochemistry

Volumn 44, Issue 46, 2005, Pages 15334-15344

  Xia, Zuyong ^a   Azurmendi, Hugo F ^a   Mildvan, Albert S ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CATALYSIS; ENZYME KINETICS; FREE ENERGY; HYDROLYSIS; RATE CONSTANTS; SUBSTITUTION REACTIONS;

DISSOCIATION CONSTANTS; NUCLEOPHILIC SUBSTITUTIONS; NUCLEOSIDES; TRANSIENT STATE KINETICS;

ENZYMES;

8 HYDROXYDEOXYGUANOSINE; BACTERIAL ENZYME; DEOXYGUANOSINE TRIPHOSPHATE; INORGANIC PYROPHOSPHATASE; MAGNESIUM ION; MUTT PYROPHOSPHOHYDROLASE; NUCLEOSIDE TRIPHOSPHATE; NUCLEOSIDE TRIPHOSPHATE PYROPHOSPHATASE; UNCLASSIFIED DRUG;

ARTICLE; COMPLEX FORMATION; DIFFUSION; DISSOCIATION; ENERGY; ENZYME BINDING; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SUBSTRATE; MUTAGENICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN HYDROLYSIS; STEADY STATE;

DEOXYCYTOSINE NUCLEOTIDES; DEOXYGUANINE NUCLEOTIDES; ENZYME ACTIVATION; ESCHERICHIA COLI PROTEINS; KINETICS; MAGNESIUM; MANGANESE; MODELS, CHEMICAL; PYROPHOSPHATASES; THERMODYNAMICS; VISCOSITY;

BACTERIA (MICROORGANISMS);

EID: 27944467189     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0513599     Document Type: Article

References (35)

1. Bessman, M. J., Frick, D. N., and O'Handley, S. F. (1996) The MutT proteins or "nudix" hydrolases, a family of versatile, widely distributed "housecleaning" enzymes, J. Biol. Chem. 271, 25059-25062.
2. Weber, D. J., Bhatnagar, S. K., Bullions, L. C., Bessman, M. J., and Mildvan, A. S. (1992) NMR and isotopic exchange studies of the site of bond cleavage in the MutT reaction, J. Biol. Chem. 267, 16939-16942.
3. Maki, H., and Sekiguchi, M. (1992) MutT protein specifically hydrolyzes a potent mutagenic substrate for DNA synthesis, Nature 355, 273-275.
4. Cheng, K. C., Cahill, D. S., Kasai, H., Nishimura, S., and Loeb, L. A. (1992) 8-Hydroxyguanine, an abundant form of oxidative DNA damage, causes G----T and A----C substitutions, J. Biol. Chem. 267, 166-172.
5. Treffers, H. P., Spinelli, V., and Belser, N. O. (1954) A factor (or mutator gene) influencing mutation rates in Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 40, 1064-1071.
6. Yanofsky, C., Cox, E. C., and Horn, V. (1966) The unusual mutagenic specificity of an E. coli mutator gene, Proc. Natl. Acad. Sci. U.S.A. 55, 274-281.
7. Tsuzuki, T., Egashira, A., Igarashi, H., Iwakuma, T., Nakatsuru, Y., Tominaga, Y., Kawate, H., Nakao, K., Nakamura, K., Ide, F., Kura, S., Nakabeppu, Y., Katsuki, M., Ishikawa, T., and Sekiguchi, M. (2001) Spontaneous tumorigenesis in mice defective in the MTH1 gene encoding 8-oxo-dGTPase, Proc. Natl. Acad. Sci. U.S.A. 98, 11456-11461.
8. Tassotto, M. L., and Mathews, C. K. (2002) Assessing the metabolic function of the MutT 8-oxo-dGTPase in Escherichia coli by nucleotide pool analysis, J. Biol. Chem. 277, 15807-15812.
9. Mildvan, A. S., Weber, D. J., and Abeygunawardana, C. (1999) Solution structure and mechanism of the MutT pyrophosphohydrolase, Adv. Enzymol. Relat. Areas Mol. Biol. 73, 183-207.
10. Mildvan, A. S., Xia, Z., Azurmendi, H. F., Saraswat, V., Legler, P. M., Massiah, M. A., Gabelli, S. B., Bianchet, M. A., Kang, L.-W., and Amzel, L. M. (2005) Structures and mechanisms of Nudix hydrolases, Arch. Biochem. Biophys. 433, 129-143.
11. Abeygunawardana, C., Weber, D. J., Gittis, A. G., Frick, D. N., Lin, J., Miller, A.-F., Bessman, M. J., and Mildvan, A. S. (1995) Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase, Biochemistry 34, 14997-15005.
12. 2+ complex and mechanism of its pyrophosphohydrolase action, Biochemistry 36, 1199-1211.
13. 2+-8-oxo- dGMP complex, Biochemistry 42, 10140-10154.
14. Frick, D. N., Weber, D. J., Gillespie, J. R., Bessman, M. J., and Mildvan, A. S. (1994) Dual divalent cation requirement of the MutT dGTPase, J. Biol. Chem. 269, 1794-1803.
15. Harris, T. K., Wu, G., Massiah, M. A., and Mildvan, A. S. (2000) Mutational, kinetic, and NMR studies of the roles of conserved glutamate residues and of Lys-39 in the mechanism of the MutT pyrophosphohydrolase, Biochemistry 39, 1655-1674.
16. Saraswat, V., Azurmendi, H. F., and Mildvan, A. S. (2004) Mutational, NMR, and NH exchange studies of the tight and selective binding of 8-oxo-dGMP by the MutT pyrophosphohydrolase, Biochemistry 43, 3404-3414.
17. Saraswat, V., Massiah, M. A., Lopez, G., Amzel, L. M., and Mildvan, A. S. (2002) Interactions of the products 8-oxo-dGMP, dGMP, and pyrophosphate with the MutT nucleoside triphosphate pyrophosphohydrolase, Biochemistry 41, 15566-15577.
18. Rebholz, K. L., and Northrop, D. B. (1995) Kinetics of iso mechanisms, Methods Enzymol. 249, 211-240.
19. Cleland, W. W. (1977) Determining the chemical mechanisms of enzyme catalyzed reactions by kinetic studies, Adv. Enzymol. 45, 273-387.
20. Rose, I. A. (1998) How fumarase recycles after the malate → fumarate reaction. Insights into the reaction mechanism, Biochemistry 37, 17651-17658.
21. Rose, I. A. (1997) Restructuring the active site of fumarase for the fumarate to malate reaction, Biochemistry 36, 12346-12354.
22. Johnson, K. A. (1992) Transient-state kinetic analysis of enzyme reaction pathways, Methods Enzymol. 134, 677-705.
23. 15N resonances of the MutT enzyme by heteronuclear multidimensional NMR, Biochemistry 32, 13071-13080.
24. Mo, J.-Y., Maki, H., and Sekiguchi, M. (1992) Hydrolytic elimination of a mutagenic nucleotide, 8-oxo-dGTP, by human 18-kilodalton protein: Sanitization of nucleotide pool, Proc. Natl. Acad. Sci. U.S.A. 89, 11021-11025.
25. Kasai, H., and Nishimura, S. (1984) Hydroxylation of deoxyguanosine at the C-8 position by ascorbic acid and other reducing agents, Nucleic Acids Res. 12, 2137-2145.
26. Trilink Biotechnologies, Inc. (1999) Product Data Sheet, San Diego.
27. Zhang, H., Wood, O. L., Papermaster, S. F., Nielsen, C. J., and Ussery, M. A. (1997) Palindromic oligonucleotide-directed enzymatic determination of 2′-deoxythymidine 5′-triphosphate and 2′-deoxycytidine 5′-triphosphate in human cells, Anal. Biochem. 252, 143-152.
28. Kuzmic, P. (1996) Program DynaFit for the Analysis of Enzyme Kinetic Data: Application to HIV Proteinase, Anal. Biochem. 237, 260-273.
29. Cole, P. A., Burn, P., Takacs, B., and Walsh, C. T. (1994) Evaluation of the catalytic mechanism of recombinant human Csk (C-terminal Src kinase) using nucleotide analogs and viscosity effects, J. Biol. Chem. 269, 30880-30887.
30. CRC Handbook of Chemistry and Physics, 58th ed, (1978) p D-261, CRC Press Inc., Cleveland, OH.
31. Cleland, W. W., and Northrop, D. B. (1999) Energetics of substrate binding, catalysis, and product release, Methods Enzymol. 308, 3-27.
32. Segal, I. H. (1975) Enzyme Kinetics, pp 113-114, John Wiley and Sons, New York.
33. Traut, T. W. (1994) Physiological concentrations of purines and pyrimidines, Mol. Cell. Biochem. 140, 1-22.
34. i concentration is not directly dependent on amount of inorganic pyrophosphatase in Escherichia coli K-12 cells, J. Bacteriol. 171, 4498-4500.
35. Frey, P. A., and Arabshahi, A. (1995) Standard free energy change for the hydrolysis of the α,β-phosphoanhydride bridge in ATP, Biochemistry 34, 11307-11310.