Complexes of the copper-containing amine oxidase from Arthrobacter globiformis with the inhibitors benzylhydrazine and tranylcypromine

Complexes of Arthrobacter globiformis amine oxidase (AGAO) with the inhibitors benzylhydrazine and tranylcypromine (an antidepressant drug) have been refined at 1.86 and 1.65 Å resolution, respectively. Both inhibitors form covalent adducts with the TPQ cofactor. A tyrosine residue, proposed to act...

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Veröffentlicht in:	Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2008-07, Vol.64 (7), p.577-583
Hauptverfasser:	Langley, David B., Trambaiolo, Daniel M., Duff, Anthony P., Dooley, David M., Freeman, Hans C., Guss, J. Mitchell
Format:	Artikel
Sprache:	eng
Schlagworte:	AGAO Amine Oxidase (Copper-Containing) - antagonists & inhibitors Amine Oxidase (Copper-Containing) - chemistry amine oxidases Arthrobacter - drug effects Arthrobacter - enzymology Bacterial Proteins - antagonists & inhibitors Bacterial Proteins - chemistry benzylhydrazine Catalytic Domain - drug effects copper Crystallography, X-Ray Enzyme Inhibitors - chemistry Hydrazines - chemistry Protein Structure Communications topaquinone tranylcypromine Tranylcypromine - chemistry
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Zusammenfassung:	Complexes of Arthrobacter globiformis amine oxidase (AGAO) with the inhibitors benzylhydrazine and tranylcypromine (an antidepressant drug) have been refined at 1.86 and 1.65 Å resolution, respectively. Both inhibitors form covalent adducts with the TPQ cofactor. A tyrosine residue, proposed to act as a gate to the AGAO active site, is in its open conformation.
ISSN:	1744-3091 1744-3091
DOI:	10.1107/S174430910801556X