1h83
STRUCTURE OF POLYAMINE OXIDASE IN COMPLEX WITH 1,8-DIAMINOOCTANE
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OverviewOverview
Polyamine oxidase (PAO) carries out the FAD-dependent oxidation of the, secondary amino groups of spermidine and spermine, a key reaction in the, polyamine catabolism. The active site of PAO consists of a 30 A long, U-shaped catalytic tunnel, whose innermost part is located in front of the, flavin ring. To provide insight into the PAO substrate specificity and, amine oxidation mechanism, we have investigated the crystal structure of, maize PAO in the reduced state and in complex with three different, inhibitors, guazatine, 1,8-diaminooctane, and, N(1)-ethyl-N(11)-[(cycloheptyl)methyl]-4,8-diazaundecane (CHENSpm). In the, reduced state, the conformation of the isoalloxazine ring and the, surrounding residues is identical to that of the oxidized enzyme. Only, Lys300 moves away from the ... [(full description)]
About this StructureAbout this Structure
1H83 is a [Single protein] structure of sequence from [Zea mays] with NAG, FAD and DIA as [ligands]. Active as [Polyamine oxidase], with EC number [1.5.3.11]. Structure known Active Sites: DIA, DIB, DIC, FAA, FAB and FAC. Full crystallographic information is available from [OCA].
ReferenceReference
Structural bases for inhibitor binding and catalysis in polyamine oxidase., Binda C, Angelini R, Federico R, Ascenzi P, Mattevi A, Biochemistry. 2001 Mar 6;40(9):2766-76. PMID:11258887
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