2ix6: Difference between revisions

Plants produce a unique peroxisomal short chain-specific acyl-CoA oxidase, (ACX4) for beta-oxidation of lipids. The short chain-specific oxidase has, little resemblance to other peroxisomal acyl-CoA oxidases but has an, approximately 30% sequence identity to mitochondrial acyl-CoA, dehydrogenases. Two biochemical features have been linked to structural, properties by comparing the structures of short chain-specific Arabidopsis, thaliana ACX4 with and without a substrate analogue bound in the active, site to known acyl-CoA oxidases and dehydrogenase structures: (i) a, solvent-accessible acyl binding pocket is not required for oxygen, reactivity, and (ii) the oligomeric state plays a role in substrate pocket, architecture but is not linked to oxygen reactivity. The structures, indicate that the acyl-CoA oxidases may encapsulate the electrons for, transfer to molecular oxygen by blocking the dehydrogenase substrate, interaction site with structural extensions. A small binding pocket, observed adjoining the flavin adenine dinucleotide N5 and C4a atoms could, increase the number of productive encounters between flavin adenine, dinucleotide and O2.

2IX6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with FAD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Acyl-CoA_oxidase Acyl-CoA oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.3.6 1.3.3.6] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IX6 OCA].  

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