Sandbox Reserved 342: Difference between revisions

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== '''Xanthine-guanine Phosphoribosyltransferase''' ==
== '''XANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE''' ==
   
   


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=STRUCTURE=
=Structure=
PRTase structures fall into two groups, type I and Type II<ref name="Vos"/>.
XGTPase has a conserved sequence, 85-IVIDDLVDTG-94, which is called the PRib-PP (5-phospho-a-D-ribosyl-1-pyrophosphate) binding site<ref name="Vos"/>.  This binding site features two adjacent acidic residues, which are surrounded by hydrophobic residues<ref name="Vos"/>.  There s five-stranded b-sheet surrounded by three or four a-helices that creates a conserved structural core containing the PRib-PP binding site<ref name="Vos"/>




 
=Function=
=FUNCTION=
XGRT is an enzyme that catalyzes the conversion of guanine, xanthine, and sometimes hypoxanthine, to GMP, XMP, and IMP <ref name="Vos"/>.
XGRT is an enzyme that catalyzes the conversion of guanine, xanthine, and sometimes hypoxanthine, to GMP, XMP, and IMP <ref name="Vos"/>.


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<scene name='Sandbox_Reserved_342/Trial/1'>TextToBeDisplayed</scene>=MECHANISM=
<scene name='Sandbox_Reserved_342/Trial/1'>TextToBeDisplayed</scene>=MECHANISM=
==RECOGNITION==
==Recognition==
==CATALYSIS==  
==Catalysis==  
Magnesium and other divalent cations are necessary for catalysis<ref name="Vos"/>.
Magnesium and other divalent cations are necessary for catalysis<ref name="Vos"/>.


=IMPORTANCE=
=Importance=
<Structure load='1a96' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<Structure load='1a96' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
='''ADDITIONAL RESOURCES'''=
='''Additional Resources'''=


=References=
=References=
<references/>
<references/>

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