Purification, crystallization and preliminary X-ray characterization ofBacillus cereusarylamineN-acetyltransferase 3 [(BACCR)NAT3]
2012 ◽
Vol 68
(2)
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pp. 196-198
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Keyword(s):
X Ray
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ArylamineN-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 ofBacillus cereusarylamineN-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 groupC121, with unit-cell parametersa= 90.44,b= 44.52,c = 132.98 Å, β = 103.8°.
2014 ◽
Vol 70
(10)
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pp. 1372-1375
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