Abstract
Arylamine N-acetyltransferases (NATs) are xenobiotic metabolizing enzymes (XMEs) that catalyze the acetylation of arylamines. All functional NATs described to date possess a strictly conserved Cys-His-Asp catalytic triad. Here, the purification, crystallization and preliminary X-ray characterization of Bacillus cereus arylamine N-acetyltransferase 3 [(BACCR)NAT3], a putative NAT isoenzyme that possesses a unique catalytic triad containing a glutamate residue, is reported. The crystal diffracted to 2.42 Å resolution and belonged to the monoclinic space group C121, with unit-cell parameters a = 90.44, b = 44.52, c = 132.98 Å, β = 103.8°.
| Original language | English |
|---|---|
| Journal | Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online |
| Volume | 68 |
| Issue number | Pt 2 |
| Pages (from-to) | 196-8 |
| Number of pages | 3 |
| ISSN | 1744-3091 |
| DOIs | |
| Publication status | Published - 1 Feb 2012 |
Keywords
- Arylamine N-Acetyltransferase
- Bacillus cereus
- Crystallization
- Crystallography, X-Ray
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Kubiak, X. J. P., Pluvinage, B., Li de la Sierra-Gallay, I., Weber, P., Haouz, A., Dupret, J.-M., & Rodrigues-Lima, F. (2012). Purification, crystallization and preliminary X-ray characterization of Bacillus cereus arylamine N-acetyltransferase 3 [(BACCR)NAT3]. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 68(Pt 2), 196-8. https://doi.org/10.1107/S1744309111053942