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1ddo
From Proteopedia
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REDUCED D-AMINO ACID OXIDASE FROM PIG KIDNEY IN COMPLEX WITH IMINO-TRP
Overview
D-Amino acid oxidase (DAAO) is the prototype of the flavin-containing, oxidases. It catalyzes the oxidative deamination of various D-amino acids, ranging from D-Ala to D-Trp. We have carried out the X-ray analysis of, reduced DAAO in complex with the reaction product imino tryptophan (iTrp), and of the covalent adduct generated by the photoinduced reaction of the, flavin with 3-methyl-2-oxobutyric acid (kVal). These structures were, solved by combination of 8-fold density averaging and least-squares, refinement techniques. The FAD redox state of DAAO crystals was assessed, by single-crystal polarized absorption microspectrophotometry. iTrp binds, to the reduced enzyme with the N, C alpha, C, and C beta atoms positioned, 3.8 A from the re side of the flavin. The indole side chain points ... [(full description)]
About this Structure
1DDO is a [Single protein] structure of sequence from [Sus scrofa] with FAD, ITR and DTR as [ligands]. Active as [D-amino-acid oxidase], with EC number [1.4.3.3]. Structure known Active Sites: FAA, FAB, FAC, FAD, FAE, FAF, FAG and FAH. Full crystallographic information is available from [OCA].
Reference
Active site plasticity in D-amino acid oxidase: a crystallographic analysis., Todone F, Vanoni MA, Mozzarelli A, Bolognesi M, Coda A, Curti B, Mattevi A, Biochemistry. 1997 May 13;36(19):5853-60. PMID:9153426
Page seeded by OCA on Tue Oct 30 13:17:09 2007
Categories: D-amino-acid oxidase | Single protein | Sus scrofa | Mattevi, A. | Todone, F. | DTR | FAD | ITR | Fad cofactor | Flavoenzyme | Oxidoreductase
