User:Cameron Evans/Sandbox 1: Difference between revisions

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Reductive amination of α-ketoglutarate (α-KG) is the process by which the ketone is converted to an amine via an imine intermediate. The reverse reaction, oxidative deamination, is the conversion of the amine functional group to a ketone.

In vertebrates the produced ammonia is usually utilized in the urea cycle and in bacteria the ammonia is assimilated to amino acids and amidotransferases.<ref name="Lightfoot_1988">~~{{cite journal | author =~~ Lightfoot DA, Baron AJ, Wootton JC ~~| year =~~ 1988 ~~| title =~~ Expression of the Escherichia coli glutamate dehydrogenase gene in the cyanobacterium Synechococcus PCC6301 causes ammonium tolerance ~~| journal =~~ Plant Molecular Biology ~~| volume =~~ 11 ~~| issue =~~ 3 ~~| pages =~~ 335-344 | doi = 10.1007/BF00027390 }}</ref>

In vertebrates the produced ammonia is usually utilized in the urea cycle and in bacteria the ammonia is assimilated to amino acids and amidotransferases.<ref name="Lightfoot_1988">Lightfoot DA, Baron AJ, Wootton JC (1988). "Expression of the Escherichia coli glutamate dehydrogenase gene in the cyanobacterium Synechococcus PCC6301 causes ammonium tolerance". Plant Molecular Biology 11 (3): 335-344. [http://www.springerlink.com/content/w2721u62r8021510/ doi 10.1007/BF00027390]</ref>

Glutamate dehydrogenase shares sequence homology and structural homology to the superfamily of amino acid dehydrogenases, which supports the idea that this superfamily formed by divergent evolution. <ref name="1bgv" /> Because of the homology among all proteins in this superfamily, many dehydrogenases can work on multiple substrates. Nonetheless, GluDH appears to be very specific towards its substrates.

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 Reductive amination of α-ketoglutarate (α-KG) is the process by which the ketone is converted to an amine via an imine intermediate. The reverse reaction, oxidative deamination, is the conversion of the amine functional group to a ketone.
-In vertebrates the produced ammonia is usually utilized in the urea cycle and in bacteria the ammonia is assimilated to amino acids and amidotransferases.<ref name="Lightfoot_1988">{{cite journal | author = Lightfoot DA, Baron AJ, Wootton JC | year = 1988 | title = Expression of the Escherichia coli glutamate dehydrogenase gene in the cyanobacterium Synechococcus PCC6301 causes ammonium tolerance | journal = Plant Molecular Biology | volume = 11 | issue = 3 | pages = 335-344 | doi = 10.1007/BF00027390 }}</ref>
+In vertebrates the produced ammonia is usually utilized in the urea cycle and in bacteria the ammonia is assimilated to amino acids and amidotransferases.<ref name="Lightfoot_1988">Lightfoot DA, Baron AJ, Wootton JC (1988). "Expression of the Escherichia coli glutamate dehydrogenase gene in the cyanobacterium Synechococcus PCC6301 causes ammonium tolerance". Plant Molecular Biology 11 (3): 335-344. [http://www.springerlink.com/content/w2721u62r8021510/ doi 10.1007/BF00027390]</ref>
 Glutamate dehydrogenase shares sequence homology and structural homology to the superfamily of amino acid dehydrogenases, which supports the idea that this superfamily formed by divergent evolution. <ref name="1bgv" /> Because of the homology among all proteins in this superfamily, many dehydrogenases can work on multiple substrates. Nonetheless, GluDH appears to be very specific towards its substrates.