Triose Phosphate Isomerase Structure & Mechanism: Difference between revisions

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Christian Krenk, David Canner, Diamond B. Reese, Michal Harel, Jane S. Richardson, Alexander Berchansky

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 ==Structural Characteristics of TIM==
+The secondary structure consists of 14 alpha helices and 8 beta sheets per monomer. <scene name='Christian_Krenk_Sandbox/Alpha_beta_barrel/1'>The tertiary structure is an alpha-beta barrel.</scene>Alpha/Beta barrel
-Secondary Structure:  Alpha helices and Beta sheets
-Tertiary Structure:
-<scene name='Christian_Krenk_Sandbox/Alpha_beta_barrel/1'>The tertiary structure is an alpha-beta barrel.</scene>Alpha/Beta barrel
 Quaternary Structure:  Homodimer
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 The enzyme aids in catalysis by binding tightly to the enediol transition state.  To convert GAP to the enediol intermediate, a proton is abstracted from C2 by a base and the carbonyl oxygen atom is protonated by an acid.
-<scene name='Christian_Krenk_Sandbox/Active_site/1'>TIM’s Glu 165 acts as the base and grabs GAP’s C2 proton, while His 95 is H-bonded to the carbonyl oxygen and acts as the acid by protonating carbonyl oxygen.</scene>  TIM’s Glu 165 acts as the base and grabs GAP’s C2 proton, while His 95 is H-bonded to the carbonyl oxygen and acts as the acid by protonating carbonyl oxygen.  The enediol intermediate is negatively charged, but is somewhat stabilized by Lys 12’s positively charged side chain.  To convert the enediol intermediate to DHAP, C1 is protonated by Glu 165, with His 95 removing a proton from C2’s OH group.  As a result, the catalytic groups are back at their original states, and catalysis is completed.
+<scene name='Christian_Krenk_Sandbox/Active_site/1'> Glu 165 acts as the base and grabs GAP’s C2 proton, while His 95 is H-bonded to the carbonyl oxygen and acts as the acid by protonating carbonyl oxygen.</scene>  TIM’s Glu 165 acts as the base and grabs GAP’s C2 proton, while His 95 is H-bonded to the carbonyl oxygen and acts as the acid by protonating carbonyl oxygen.  The enediol intermediate is negatively charged, but is somewhat stabilized by Lys 12’s positively charged side chain.  To convert the enediol intermediate to DHAP, C1 is protonated by Glu 165, with His 95 removing a proton from C2’s OH group.  As a result, the catalytic groups are back at their original states, and catalysis is completed.
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