User:Cameron Evans/Sandbox 1: Difference between revisions

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NAD(H) and NADP(H) are cofactors for the reaction and serve to reduce α-KG/ oxidize Glu when they have been oxidized.<ref name="1hwxyz" /> There are three types of GluDH defined by their preference for cofactor and substrate: (1) NAD(H)-specific GluDH, which mainly catabolizes glutamate; (2) NADP(H)-specific GluDH, which plays a mainly anabolic role; and (3) GluDH with mixed specificity that utilizes both cofactors with similar efficacy. Mammalian GluDH are mainly of this third type as they have comprable efficiency for each reaction. Because of the "non-specificity" of mammalian enzymes the protein utilizes allosteric regulation to control metabolic balance. <ref name=1hwx />. Prokaryotes do not have allosteric inhibition.<ref name="1hwxyz" />

===Catalytic Mechanism===

The catalytic mechanism for all crystal complexes of GluDH have not been elucidated; however, a general model has bee proposed by Peterson and Smith (1999) for bovine GluDH.

(1) In the hydrophobic cleft, a lysine (126) has an unusually low pKa. This lysine loses a proton to the solvent and initiates the closing of the catalytic cleft.

==Prokaryote==

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 NAD(H) and NADP(H) are cofactors for the reaction and serve to reduce α-KG/ oxidize Glu when they have been oxidized.<ref name="1hwxyz" /> There are three types of GluDH defined by their preference for cofactor and substrate: (1) NAD(H)-specific GluDH, which mainly catabolizes glutamate; (2) NADP(H)-specific GluDH, which plays a mainly anabolic role; and (3) GluDH with mixed specificity that utilizes both cofactors with similar efficacy. Mammalian GluDH are mainly of this third type as they have comprable efficiency for each reaction. Because of the "non-specificity" of mammalian enzymes the protein utilizes allosteric regulation to control metabolic balance. <ref name=1hwx />. Prokaryotes do not have allosteric inhibition.<ref name="1hwxyz" />
+===Catalytic Mechanism===
+The catalytic mechanism for all crystal complexes of GluDH have not been elucidated; however, a general model has bee proposed by Peterson and Smith (1999) for bovine GluDH.
+(1) In the hydrophobic cleft, a lysine (126) has an unusually low pKa. This lysine loses a proton to the solvent and initiates the closing of the catalytic cleft.
 ==Prokaryote==