Sandbox Reserved 315: Difference between revisions
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==TIM Barrel== | ==TIM Barrel== | ||
==Active Site== | ==Active Site== | ||
*first bullet | *first bullet | ||
**sub-bullet | **sub-bullet | ||
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##2 | ##2 | ||
[http://www.wikipedia.org Wikipedia] | [http://www.wikipedia.org Wikipedia] | ||
=Function= | =Function= | ||
<Structure load=1dv7 size='200' frame='true' align='left' caption='Insert caption here' scene='Sandbox_Reserved_315/Odcase_dimer/1'/> | |||
==UMP Synthase== | ==UMP Synthase== | ||
In multicellular eukaryotes, orotidine monophosphate decarboxylase associates with orotate phosphoribosyltransferase to form a bifunctional protein, [[UMP synthase]]<Ref name = "Lee"/><Ref name = "Yablonski"/>. UMP synthase carries out the last two steps in pyrimidine biosynthesis, converting orotate to uridine 5'-monophosphate<Ref name = "Yablonski">PMID:8631878</ref>. This reaction involves first adding ribose-P to orotate to form orotidine 5'-monophosphate, followed by a decarboxylation reaction to form uridine 5'-monophosphate<Ref name = "Yablonski"/>. In microorganisms these two enzymes are separate and coded by distinct genes. However research has shown that all multicellular eukaryotes so far code the genes for these two enzymes together and as a result they are covalently bonded as a bifunctional protein with two distinct catalytic domains<Ref name = "Yablonski"/>. | |||
=Rate of Catalysis= | =Rate of Catalysis= | ||
==Substrate Destabilization== | ==Substrate Destabilization== | ||
