Purification, crystallization and preliminary X-ray characterization of Bacillus cereus arylamine N-acetyltransferase 3 [(BACCR)NAT3].
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°.
Université Paris Diderot, Sorbonne Paris Cité, Unité de Biologie Fonctionnelle et Adaptative, CNRS EAC 4413, Paris, France.
Xavier
X
Kubiak
Benjamin
B
Pluvinage
Inès
I
Li de la Sierra-Gallay
Patrick
P
Weber
Ahmed
A
Haouz
Jean-Marie
JM
Dupret
Fernando
F
Rodrigues-Lima
D001191:Arylamine N-Acetyltransferase / Q000737:chemistry* / Q000302:isolation & purification; D001409:Bacillus cereus / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray
D001191:Arylamine N-Acetyltransferase