Sandbox Reserved 772: Difference between revisions
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<Structure load=' | <Structure load='1k75' size='500' frame='true' align='right' caption='Crystal structure of L-histidinol dehydrogenase with a functional homodimer in the asymmetric unit.' /> | ||
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[[Image:pathways.jpg]] | [[Image:pathways.jpg]] | ||
This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 | This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 and Glu-326 are the active sites (proton acceptors) of HDH.<ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref> | ||
The reaction above is catalyzed by HisD. The structure allows thebidentification of residues Glu-326 as being base B2 and His-327 as B1, B3, and B4. Glu-326 activates the water molecule that attacks the reactive carbon in step 2 of the reaction mechanism.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> | The reaction above is catalyzed by HisD. The structure allows thebidentification of residues Glu-326 as being base B2 and His-327 as B1, B3, and B4. Glu-326 activates the water molecule that attacks the reactive carbon in step 2 of the reaction mechanism.<ref name="pnas">http://www.pnas.org.prox.lib.ncsu.edu/content/99/4/1859.full.pdf</ref> | ||
