Crystal structure at 1.1 angstrom resolution of an insect myrosinase from Brevicoryne brassicae shows its close relationship to β-glucosidases

The aphid Brevicoryne brassicae is a specialist feeding on Brassicaceae plants. The insect has an intricate defence system involving a β-D-thioglucosidase (myrosinase) that hydrolyses glucosinolates sequestered from the host plant into volatile isothiocyanates. These isothiocyanates act synergistica...

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Veröffentlicht in:	Insect biochemistry and molecular biology 2005-12, Vol.35 (12), p.1311-1320
Hauptverfasser:	Husebye, H, Arzt, S, Burmeister, W.P, Hartel, F.V, Brandt, A, Rossiter, J.T, Bones, A.M
Format:	Artikel
Sprache:	eng
Schlagworte:	active sites amino acid sequences beta-glucosidase binding sites Brevicoryne brassicae catalytic residues crystal structure enzyme activity glucosinolates molecular sequence data protein structure recombinant proteins sequence homology thioglucosidase X-ray diffraction
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