User:Cameron Evans/Sandbox 1: Difference between revisions

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==General Information==

Glutamate Dehydrogenase (GluDH) is a member of the superfamily of amino acid dehydrogenase and functions in the cell to dehydrate α-ketoglutarate to the amino acid glutamate and also to perform the reverse reaction.<ref name="1bgv">PMID:8263917</ref> GluDH feeds α-ketoglutarate into the tricarboxylic acid cycle (TCA) and the amine product is thought to be utilized by other biosynthetic pathways.<ref name="~~hwxy~~">PMID:11254391</ref>

Glutamate Dehydrogenase (GluDH) is a member of the superfamily of amino acid dehydrogenase and functions in the cell to dehydrate α-ketoglutarate to the amino acid glutamate and also to perform the reverse reaction.<ref name="1bgv">PMID:8263917</ref> GluDH feeds α-ketoglutarate into the tricarboxylic acid cycle (TCA) and the amine product is thought to be utilized by other biosynthetic pathways.<ref name="1hwxyz">PMID:11254391</ref>

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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.

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.~~<ref name="hwxy" />~~

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.

NAD(P)H are cofactors for the reaction and serve to reduce α-KG/ oxidize Glu when they have been oxidized. Though procaryotic GluDH has not been found to be allosterically inhibited, Mammalian GluDH has been found to accomodate allosteric inhibition from GTP and ATP.<ref name="1hwxyz" />

NAD(P)H are cofactors for the reaction and serve to reduce α-KG/ oxidize Glu when they have been oxidized. Though procaryotic GluDH has not been found to be allosterically inhibited, Mammalian GluDH has been found to accomodate allosteric inhibition from GTP and ATP.<ref name="~~1hw~~" />

==Prokaryote==

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 ==General Information==
-Glutamate Dehydrogenase (GluDH) is a member of the superfamily of amino acid dehydrogenase and functions in the cell to dehydrate α-ketoglutarate to the amino acid glutamate and also to perform the reverse reaction.<ref name="1bgv">PMID:8263917</ref> GluDH feeds α-ketoglutarate into the tricarboxylic acid cycle (TCA) and the amine product is thought to be utilized by other biosynthetic pathways.<ref name="hwxy">PMID:11254391</ref>
+Glutamate Dehydrogenase (GluDH) is a member of the superfamily of amino acid dehydrogenase and functions in the cell to dehydrate α-ketoglutarate to the amino acid glutamate and also to perform the reverse reaction.<ref name="1bgv">PMID:8263917</ref> GluDH feeds α-ketoglutarate into the tricarboxylic acid cycle (TCA) and the amine product is thought to be utilized by other biosynthetic pathways.<ref name="1hwxyz">PMID:11254391</ref>
 <gallery>
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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.
-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.<ref name="hwxy" />
+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.
+NAD(P)H are cofactors for the reaction and serve to reduce α-KG/ oxidize Glu when they have been oxidized. Though procaryotic GluDH has not been found to be allosterically inhibited, Mammalian GluDH has been found to accomodate allosteric inhibition from GTP and ATP.<ref name="1hwxyz" />
-NAD(P)H are cofactors for the reaction and serve to reduce α-KG/ oxidize Glu when they have been oxidized. Though procaryotic GluDH has not been found to be allosterically inhibited, Mammalian GluDH has been found to accomodate allosteric inhibition from GTP and ATP.<ref name="1hw" />
 ==Prokaryote==