HAL will be down for maintenance from Friday, June 10 at 4pm through Monday, June 13 at 9am. More information
Skip to Main content Skip to Navigation
Journal articles

Purification, crystallization and preliminary X-ray characterization ofBacillus cereusarylamineN-acetyltransferase 3 [(BACCR)NAT3]

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 , = 103.8 .
Document type :
Journal articles
Complete list of metadata

https://hal-pasteur.archives-ouvertes.fr/pasteur-03525338
Contributor : Hélène Ribierre Connect in order to contact the contributor
Submitted on : Thursday, January 13, 2022 - 5:47:06 PM
Last modification on : Thursday, April 7, 2022 - 10:10:29 AM

Links full text

Identifiers

Citation

Xavier Kubiak, Benjamin Pluvinage, Inès Li de la Sierra-Gallay, Patrick Weber, Ahmed Haouz, et al.. Purification, crystallization and preliminary X-ray characterization ofBacillus cereusarylamineN-acetyltransferase 3 [(BACCR)NAT3]. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, International Union of Crystallography, 2012, 68 (2), pp.196 - 198. ⟨10.1107/s1744309111053942⟩. ⟨pasteur-03525338⟩

Share

Metrics

Record views

13