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

TitleComplexes of the copper-containing amine oxidase from Arthrobacter globiformis with the inhibitors benzylhydrazine and tranylcypromine
Authors
Langley, David B.Trambaiolo, Daniel M.Duff, Anthony P.Dooley, David M.Freeman, Hans C.Guss, J. Mitchell
KeywordsAmine oxidases
Tranylcypromine
Topaquinone
Copper
Benzylhydrazine
AGAO
Issue Date2008
Citation
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2008, v. 64, n. 7, p. 577-583 How to Cite?
DOI: http://dx.doi.org/10.1107/S174430910801556X
AbstractComplexes 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. © International Union of Crystallography 2008.
Persistent Identifierhttp://hdl.handle.net/10722/219580
ISSN
1744-3091
2014 Impact Factor: 0.524
ISI Accession Number ID
WOS:000257249000002

 

DC FieldValueLanguage
dc.contributor.authorLangley, David B.-
dc.contributor.authorTrambaiolo, Daniel M.-
dc.contributor.authorDuff, Anthony P.-
dc.contributor.authorDooley, David M.-
dc.contributor.authorFreeman, Hans C.-
dc.contributor.authorGuss, J. Mitchell-
dc.date.accessioned2015-09-23T02:57:27Z-
dc.date.available2015-09-23T02:57:27Z-
dc.date.issued2008-
dc.identifier.citationActa Crystallographica Section F: Structural Biology and Crystallization Communications, 2008, v. 64, n. 7, p. 577-583-
dc.identifier.issn1744-3091-
dc.identifier.urihttp://hdl.handle.net/10722/219580-
dc.description.abstractComplexes 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. © International Union of Crystallography 2008.-
dc.languageeng-
dc.relation.ispartofActa Crystallographica Section F: Structural Biology and Crystallization Communications-
dc.subjectAmine oxidases-
dc.subjectTranylcypromine-
dc.subjectTopaquinone-
dc.subjectCopper-
dc.subjectBenzylhydrazine-
dc.subjectAGAO-
dc.titleComplexes of the copper-containing amine oxidase from Arthrobacter globiformis with the inhibitors benzylhydrazine and tranylcypromine-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1107/S174430910801556X-
dc.identifier.pmid18607080-
dc.identifier.scopuseid_2-s2.0-46949107191-
dc.identifier.volume64-
dc.identifier.issue7-
dc.identifier.spage577-
dc.identifier.epage583-
dc.identifier.eissn1744-3091-
dc.identifier.isiWOS:000257249000002-
dc.identifier.issnl1744-3091-

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