User:Cameron Evans/Sandbox 1: Difference between revisions

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GluDH makes non-coavalent and specific contacts with its substrates, cofactors and allosteric inhibitors.

Glutamate and α-KG both bind via hydrogen bonding within the catalytic cleft between the two distinct clamping domains. Both make contact with K126, K90, S381, R211, and N349. However, α-KG binding is thought to be stabilized also by N374 (through a water molecule) and K114 and Glu by K114 in a different crystal structure.

Glutamate and α-KG both bind via hydrogen bonding within the catalytic cleft between the two distinct clamping domains. Both make contact via hydrogen binding with K126, K90, S381, R211, and N349. However, α-KG binding is thought to be stabilized also by N374 (through a water molecule) and K114 and Glu by K114 in a different crystal structure.

Four basic residues are neutralized as the catalytic cleft closes and either reaction begins: K114, 126, 90 and 113. These make specific contacts with the alpha and gamma carboxyl groups of the substrate.

NADH, as it binds within the to the catalytic cleft, makes specific hydrogen bonds with D168, S170, E275, S276, N349, A326 and S327 in all crystal structures. Q250 contacts both NADPH and NADH, but not NAD+. Instead Q330 makes a similar contact to NAD+ in that region.<ref name=1hwxyz />

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 GluDH makes non-coavalent and specific contacts with its substrates, cofactors and allosteric inhibitors.
-Glutamate and α-KG both bind via hydrogen bonding within the catalytic cleft between the two distinct clamping domains. Both make contact with K126, K90, S381, R211, and N349. However, α-KG binding is thought to be stabilized also by N374 (through a water molecule) and K114 and Glu by K114 in a different crystal structure.
+Glutamate and α-KG both bind via hydrogen bonding within the catalytic cleft between the two distinct clamping domains. Both make contact via hydrogen binding with K126, K90, S381, R211, and N349. However, α-KG binding is thought to be stabilized also by N374 (through a water molecule) and K114 and Glu by K114 in a different crystal structure.
+Four basic residues are neutralized as the catalytic cleft closes and either reaction begins: K114, 126, 90 and 113. These make specific contacts with the alpha and gamma carboxyl groups of the substrate.
 NADH, as it binds within the to the catalytic cleft, makes specific hydrogen bonds with D168, S170, E275, S276, N349, A326 and S327 in all crystal structures. Q250 contacts both NADPH and NADH, but not NAD+. Instead Q330 makes a similar contact to NAD+ in that region.<ref name=1hwxyz />