The conserved glycine/alanine residue of the active-site loop containing the putative acetylCoA-binding motif is essential for the overall structural integrity of Mesorhizobium loti arylamine N-acetyltransferase 1

Biochemical and Biophysical Research Communications

Volumn 361, Issue 1, 2007, Pages 256-262

  Atmane, Noureddine ^a   Dairou, Julien ^a   Flatters, Delphine ^b   Martins, Marta ^a   Pluvinage, Benjamin ^a   Derreumaux, Philippe ^a,c   Dupret, Jean Marie ^a   Rodrigues Lima, Fernando ^a  

^a UNIVERSITÉ PARIS DESCARTES   (France)

^b INSERM   (France)

^c INST DE BIOLOGIE PHYSICO CHIMIQUE   (France)

Author keywords

Active site; Arylamine N acetyltransferase; P loop; Site directed mutagenesis; Steric hindrance

Indexed keywords

ACETYL COENZYME A; ACYLTRANSFERASE; ALANINE; ANAZOLENE SODIUM; ARYLAMINE ACETYLTRANSFERASE; ARYLAMINE ACETYLTRANSFERASE 1; BACTERIUM LYSATE; GLYCINE; POLYCLONAL ANTIBODY; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME PURIFICATION; ESCHERICHIA COLI; MESORHIZOBIUM; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN MOTIF; SALMONELLA TYPHIMURIUM; WESTERN BLOTTING;

ACETYL COENZYME A; ALANINE; ALPHAPROTEOBACTERIA; AMINO ACID MOTIFS; ARYLAMINE N-ACETYLTRANSFERASE; BACTERIAL PROTEINS; BINDING SITES; GLYCINE; ISOENZYMES; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; RECOMBINANT PROTEINS;

MESORHIZOBIUM LOTI;

EID: 34547129832     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.07.034     Document Type: Article

References (19)

1. Riddle B., and Jencks W.P. Acetyl-coenzyme A: arylamine N-acetyltransferase. Role of the acetyl-enzyme intermediate and the effects of substituents on the rate. J. Biol. Chem. 246 (1971) 3250-3258
2. Dupret J.M., and Rodrigues-Lima F. Structure and regulation of the drug-metabolizing enzymes arylamine N-acetyltransferases. Curr. Med. Chem. 12 (2005) 311-318
3. Sandy J., Mushtaq A., Holton S.J., Schartau P., Noble M.E., and Sim E. Investigation of the catalytic triad of arylamine N-acetyltransferases: essential residues required for acetyl transfer to arylamines. Biochem. J. 390 (2005) 115-123
4. Goodfellow G.H., Dupret J.M., and Grant D.M. Identification of amino acids imparting acceptor substrate selectivity to human arylamine acetyltransferases NAT1 and NAT2. Biochem. J. 348 Pt 1 (2000) 159-166
5. Rodrigues-Lima F., Deloménie C., Goodfellow G.H., Grant D.M., and Dupret J.M. Homology modelling and structural analysis of human arylamine N-acetyltransferase NAT1: evidence for the conservation of a cysteine protease catalytic domain and an active-site loop. Biochem. J. 356 (2001) 327-334
6. Westwood I.M., Holton S.J., Rodrigues-Lima F., Dupret J.-M., Bhakta S., Noble M.E.M., and Sim E. Expression, purification, characterisation and structure of Pseudomonas aeruginosa arylamine N-acetyltransferase. Biochem. J. 385 (2005) 605-612
7. Holton S.J., Dairou J., Sandy J., Rodrigues-Lima F., Dupret J.M., Noble M.E.M., and Sim E. Structure of Mesorhizobium loti arylamine N-acetyltransferase 1. Acta Cryst. F61 (2005) 14-16
8. Boukouvala S., and Fakis G. Arylamine N-acetyltransferases: what we learn from genes and genomes. Drug Metab. Rev. 37 (2005) 511-564
9. Sandy J., Holton S., Fullam E., Sim E., and Noble M. Binding of the anti-tubercular drug isoniazid to the arylamine N-acetyltransferase protein from Mycobacterium smegmatis. Protein Sci. 14 (2005) 775-782
10. Zhang N., Liu L., Liu F., Wagner C.R., Hanna P.E., and Walters K.J. NMR-based model reveals the structural determinants of mammalian arylamine N-acetyltransferase substrate specificity. J. Mol. Biol. 363 (2006) 188-200
11. Rodrigues-Lima F., Dairou J., Diaz C.L., Rubio M.C., Sim E., Spaink H.P., and Dupret J.M. Cloning, functional expression and characterization of Mesorhizobium loti arylamine N-acetyltransferases: rhizobial symbiosis supplies leguminous plants with the xenobiotic N-acetylation pathway. Mol. Microbiol. 60 (2006) 505-512
12. Brooke E.W., Davies S.G., Mulvaney A.W., Pompeo F., Sim E., and Vickers R.J. An approach to identifying novel substrates of bacterial arylamine N-acetyltransferases. Bioorg. Med. Chem. 11 (2003) 1227-1234
13. In: Cornish-Bowden A. (Ed). Fundamentals of Enzyme Kinetics (2001), Portland press, Berlin
14. Guerois R., Nielsen J.E., and Serrano L. Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations. J. Mol. Biol. 320 (2002) 369-387
15. Fretland A.J., Leff M.A., Doll M.A., and Hein D.W. Functional characterization of human N-acetyltransferase 2 (NAT2) single nucleotide polymorphisms. Pharmacogenetics 11 (2001) 207-215
16. Dairou J., Flatters D., Chaffotte A.F., Pluvinage B., Sim E., Dupret J.M., and Rodrigues-Lima F. Insight into the structure of Mesorhizobium loti arylamine N-acetyltransferase 2 (MLNAT2): a biochemical and computational study. FEBS Lett. 580 (2006) 1780-1788
17. Baneyx F., and Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 22 (2004) 1399-1408
18. A. Fersht, Structure and mechanism in protein science. A guide to enzyme catalysis and protein folding, first ed., New York, 1999.
19. Kong G.K., Polekhina G., McKinstry W.J., Parker M.W., Dragani B., Aceto A., Paludi D., Principe D.R., Mannervik B., and Stenberg G. Contribution of glycine 146 to a conserved folding module affecting stability and refolding of human glutathione transferase p1-1. J. Biol. Chem. 278 (2003) 1291-1302