Binding of the anti-tubercular drug isoniazid to the arylamine N-acetyltransferase protein from Mycobacterium smegmatis

Protein Science

Volumn 14, Issue 3, 2005, Pages 775-782

  Sandy, James ^a   Holton, Simon ^a   Fullam, Elizabeth ^a   Sim, Edith ^a   Noble, Martin ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

Arylamine N acetyltransferase; Drug design; Isoniazid; Tuberculosis

Indexed keywords

ACETYL COENZYME A; ARYLAMINE ACETYLTRANSFERASE; DRUG METABOLIZING ENZYME; ISONIAZID; NITROGEN;

ARTICLE; BACTERIAL CELL; CRYSTALLIZATION; DRUG ACETYLATION; DRUG BINDING; DRUG DESIGN; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; GENE EXPRESSION; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; TERMINAL SEQUENCE;

ANTITUBERCULAR AGENTS; ARYLAMINE N-ACETYLTRANSFERASE; CATALASE; CATALYTIC DOMAIN; CRYSTALLIZATION; ISONIAZID; KINETICS; MYCOBACTERIUM SMEGMATIS; PEROXIDASE; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 14144256365     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041163505     Document Type: Article

References (27)

1. Barry 3rd, C.E., Lee, R.E., Mdluli, K., Sampson, A.E., Schroeder, B.G., Slayden, R.A., and Yuan, Y. 1998. Mycolic acids: Structure, biosynthesis and physiological functions. Prog. Lipid Res. 37: 143-179.
2. Bertrand, T., Eady, N.A.J., Jones, J.N., Jesmin Nagy, J.M., Jamart-Gregoire, B., Raven, E.L., and Brown, K.A. 2004. Crystal structure of Mycobacterium tuberculosis catalase-peroxidase. J. Biol. Chem. 279: 38991-38999.
3. Bhakta, S., Besra, G.S., Upton, A.M., Parish, T., Sholto-Douglas-Vernon, C., Gibson, K.J.C., Knutton, S., Gordon, S., daSilva, R.P., Anderton, M.C., et al. 2004. Arylamine N-acetyltransferase is required for synthesis of mycolic acids and complex lipids in Mycobacterium bovis BCG and represents a novel drug target. J. Exp. Med. 199: 1191-1199.
4. Bodiguel, J., Nagy, J.M., Brown, K.A., and Jamart-Gregoire, B. 2001. Oxidation of isoniazid by manganese and Mycobacterium tuberculosis catalase-peroxidase yields a new mechanism of activation. J. Am. Chem. Soc. 123: 3832-3833.
5. Brennan, P. and Nikaido, H. 1995. The envelope of mycobacteria. Annu. Rev. Biochem. 64: 29-63.
6. Brooke, E., Davies, S.G., Mulvaney, A.W., Pompeo, F., Sim, E., and Vickers, R.J. 2003a. An approach to identifying novel substrates of bacterial arylamine N-acetyltransferases. Bioorg. Med. Chem. 11: 1227-1234.
7. Brooke, E., Davies, S.G., Mulvaney, A.W., Okada, M., Pompeo, F., Sim, E., Vickers, R.J., and Westood, I.M. 2003b. Synthesis and in vitro evaluation of novel small molecule inhibitors of bacterial arylamine N-acetyltransferases (NATs). Bioorg. Med. Chem. 13: 2527-2530.
8. Butcher, N.J., Arulpragasam, A., and Minchin, R.F. 2004. Proteasomal degradation of N-acetyltransferase 1 is prevented by acetylation of the active site cysteine: A mechanism for the slow acetylator phenotype and substrate-dependent down-regulation. J. Biol. Chem. 279: 22131-22137.
9. Collaborative Computational Project, Number 4. 1994. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D50: 760-763.
10. Delgoda, R., Lian, L.Y., Sandy, J., and Sim, E. 2003. NMR investigation of the catalytic mechanism of arylamine N-acetyltransferase from Salmonella typhimurium. Biochim. Biophys. Acta 1620: 8-14.
11. Heym, B., Zhang, Y., Poulet, S., Young, D., and Cole, S. 1993. Characterisation of the KatG gene encoding catalase-peroxidase required for the isoniazid susceptibility of Mycobacterium tuberculosis. J. Bacteriol. 175: 4255-4259.
12. Jones, T.A., Cowan, S., Zou, J.-Y., and Kjeldgaard, M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47: 110-119.
13. Kawamura, A., Sandy, J., Upton, A., Noble, M., and Sim, E. 2003. Structural investigation of mutant Mycobacterium smegmatis arylamine N-acetyltransferase: A model for a naturally occurring functional polymorphism in Mycobacterium tuberculosis arylamine N-acetyltransferase. Protein Expr. Purif. 27: 75-84.
14. Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26: 283-291.
15. Mushtaq, A., Payton, M., and Sim, E. 2002. The COOH terminus of arylamine N-acetyltransferase from Salmonella typhimurium controls enzymic activity. J. Biol. Chem. 277: 12175-12181.
16. Mushtaq, A., Sandy, J., Holton, S.J., Shartau, P., Sim, E., and Noble, M. 2004. Investigation of the catalytic triad of arylamine N-acetyltransferases: Essential residues required for acetyl transfer to arylamines. Third International NAT Workshop, Vancouver, BC, Canada.
17. Payton, M., Auty, R., Delgoda, R., Everett, M., and Sim, E. 1999. Cloning and characterization of arylamine N-acetyltransferase genes from Mycobacterium smegmatis and Mycobacterium tuberculosis: Increased expression results in isoniazid resistance. J. Bacteriol. 181: 1343-1347.
18. Payton, M., Gifford, C., Schartau, P., Hagemeier, C., Mushtaq, A., Lucas, S., Pinter, K., and Sim, E. 2001. Evidence towards the role of arylamine N-acetyltransferase in Mycobacterium smegmatis and development of a specific antiserum against the homologous enzyme of Mycobacterium tuberculosis. Microbiology 147: 3295-3302.
19. Pompeo, F., Mushtaq, A., and Sim, E. 2002. Expression and purification of the rifamycin amide synthase, RifF, an enzyme homologous to the prokaryotic arylamine N- acetyltransferases. Protein Expr. Purif. 24: 138-151.
20. Riddle, B. and Jencks, W.P. 1971. Acetyl-coenzyme A: Arylamine N-acetyltransferase. Role of the acetyl-enzyme intermediate and the effects of substituents on the rate. J. Biol. Chem. 246: 3250-3258.
21. Rozwarski, D.A., Grant, G.A., Barton, D.H.R., Jacobs, W.R., and Sacchettini, J.C. 1998. Modification of the NADH of the Isoniazid target (InhA) from Mycobacterium tuberculosis. Science 279: 98-102.
22. Sandy, J., Mushtaq, A., Kawamura, A., Sinclair, J., Sim, E., and Noble, M. 2002. The structure of arylamine N-acetyltransferase from Mycobacterium smegmatis - An enzyme which inactivates the anti-tubercular drug, Isoniazid. J. Mol. Biol. 318: 1071-1083.
23. Slayden, R.A. and Barry 3rd, C.E. 2000. The genetics and biochemistry of isoniazid resistance in mycobacterium tuberculosis. Microbes Infect. 2: 659-669.
24. Slayden, R.A., Lee, R.E., and Barry 3rd, C.E. 2000. Isoniazid affects multiple components of the type II fatty acid synthase system of Mycobacterium tuberculosis. Mol. Microbiol. 38: 514-525.
25. Upton, A., Mushtaq, A., Victor, T.C., Sampson, S.L., Sandy, J., Smith, D.-M., van Helden, P.V., and Sim, E. 2001. Arylamine N-acetyltransferase of Mycobacterium tuberculosis is a polymorphic enzyme and a site of isoniazid metabolism. Mol. Microbiol. 42: 309-319.
26. Wallace, A.C., Laskowski, R.A., and Thornton, J.M. 1995. LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8: 127-134.
27. Zhang, Y., Heym, B., Allen, B., Young, D., and Cole, S. 1992. The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis. Nature 358: 591-593.