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2iup
From Proteopedia
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Revision as of 15:11, 30 October 2007
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CRYSTAL STRUCTURE OF DITHIONITE-REDUCED AROMATIC AMINE DEHYDROGENASE (AADH) FROM ALCALIGENES FAECALIS
Overview
The quinoprotein aromatic amine dehydrogenase (AADH) uses a covalently, bound tryptophan tryptophylquinone (TTQ) cofactor to oxidatively deaminate, primary aromatic amines. Recent crystal structures have provided insight, into the reductive half-reaction. In contrast, no atomic details are, available for the oxidative half-reaction. The TTQ O7 hydroxyl group is, protonated during reduction, but it is unclear how this proton can be, removed during the oxidative half-reaction. Furthermore, compared with the, electron transfer from the N-quinol form, electron transfer from the, non-physiological O-quinol form to azurin is significantly slower. Here we, report crystal structures of the O-quinol, N-quinol, and N-semiquinone, forms of AADH. A comparison of oxidized and substrate reduced AADH ... [(full description)]
About this Structure
2IUP is a [Single protein] structure of sequence from [Alcaligenes faecalis]. Active as [Aralkylamine dehydrogenase], with EC number [1.4.99.4]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Atomic level insight into the oxidative half-reaction of aromatic amine dehydrogenase., Roujeinikova A, Scrutton NS, Leys D, J Biol Chem. 2006 Dec 29;281(52):40264-72. Epub 2006 Sep 27. PMID:17005560
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