1zem
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(New page: 200px<br /><applet load="1zem" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zem, resolution 1.9Å" /> '''Crystal Structure of ...)
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Revision as of 02:43, 25 November 2007
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Crystal Structure of NAD+-Bound Xylitol Dehydrogenase
Overview
Xylitol dehydrogenase (XDH) is one of several enzymes responsible for, assimilating xylose into eukaryotic metabolism and is useful for, fermentation of xylose contained in agricultural byproducts to produce, ethanol. For efficient xylose utilization at high flux rates, cosubstrates, should be recycled between the NAD+-specific XDH and the NADPH-preferring, xylose reductase, another enzyme in the pathway. To understand and alter, the cosubstrate specificity of XDH, we determined the crystal structure of, the Gluconobacter oxydans holoenzyme to 1.9 angstroms resolution. The, structure reveals that NAD+ specificity is largely conferred by Asp38, which interacts with the hydroxyls of the adenosine ribose. Met39 stacked, under the purine ring and was also located near the 2' hydroxyl. Based on, the location of these residues and on sequence alignments with related, enzymes of various cosubstrate specificities, we constructed a double, mutant (D38S/M39R) that was able to exclusively use NADP+, with no loss of, activity.
About this Structure
1ZEM is a Single protein structure of sequence from Gluconobacter oxydans with MG and NAD as ligands. Active as D-xylulose reductase, with EC number 1.1.1.9 Full crystallographic information is available from OCA.
Reference
Structure-guided engineering of xylitol dehydrogenase cosubstrate specificity., Ehrensberger AH, Elling RA, Wilson DK, Structure. 2006 Mar;14(3):567-75. PMID:16531240
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