Sandbox Reserved 772: Difference between revisions

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'''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref>
'''Classification''': Oxidoreductase <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref>


'''Length''': 434 Amino Acids <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref>   
'''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref>
 
'''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref>
 
'''Length''': 434 Residues <ref name="info">http://www.uniprot.org/uniprot/P06988#section_terms</ref>   


'''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref>
'''Chains''': A, B <ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref>
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'''Ligands''': [http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL], [http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE], [http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4]<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref>
'''Ligands''': [http://oca.weizmann.ac.il/oca-bin/send-het?GOL GOL], [http://oca.weizmann.ac.il/oca-bin/send-het?MSE MSE], [http://oca.weizmann.ac.il/oca-bin/send-het?SO4 SO4]<ref name="cite2">http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75</ref>


'''Molecular Weight''': 46107.65 Da <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref>
'''Isoelectric Point''': 5.06 <ref name="cite3">http://www.topsan.org/Proteins/BSGI/1k75</ref>


==Structure==
==Structure==
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[[Image:pathways.jpg]]
[[Image:pathways.jpg]]


This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate.
This bifunctional enzyme converts L-histidinol to L-histidine through a L-histidinaldehyde intermediate. His-327 is the active site and Glu-326 activates water molecule
The process is as follows:
 
1. extraction of one proton and one hydride from L-histidinol
 
2. reduced NADH leaves and replaced by NAD+
 
3. repeat the first step
 
4. His-327 abstracts a proton from the hydroxyl group, and the second NAD+ molecule is reduced by a hydride


5. formation of l-histidine<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>


==Implications or Possible Applications==
==Implications or Possible Applications==

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OCA, Jah Ia Yang