2ix5
From Proteopedia
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(New page: 200px<br /> <applet load="2ix5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ix5, resolution 2.70Å" /> '''SHORT CHAIN SPECIFI...)
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Revision as of 17:53, 29 October 2007
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SHORT CHAIN SPECIFIC ACYL-COA OXIDASE FROM ARABIDOPSIS THALIANA, ACX4 IN COMPLEX WITH ACETOACETYL-COA
Overview
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 ... [(full description)]
About this Structure
2IX5 is a [Single protein] structure of sequence from [Arabidopsis thaliana] with CAA and FAD as [ligands]. Active as [[1]], with EC number [1.3.3.6]. Full crystallographic information is available from [OCA].
Reference
Controlling electron transfer in Acyl-CoA oxidases and dehydrogenases: a structural view., Mackenzie J, Pedersen L, Arent S, Henriksen A, J Biol Chem. 2006 Oct 13;281(41):31012-20. Epub 2006 Aug 3. PMID:16887802
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