Triose Phosphate Isomerase: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Gregg Snider, Stephen Everse, Eran Hodis, David Canner, Eric Martz, Michal Harel, Alexander Berchansky, Jane S. Richardson, Angel Herraez

@@ Line 12: / Line 12: @@
 [[Image:classical2.png|center|thumb|500px| '''Classic Mechanism proposed by Knowles and co-workers''']]
-<StructureSection load='2ypi' size='500' side='right' scene='Triose_Phosphate_Isomerase/Three_catalytic_residues/6/' >
+<StructureSection load='2ypi' size='500' side='right' scene='Triose_Phosphate_Isomerase/Three_catalytic_residues1/1/' >
-TPI carries out the isomerization reaction through an acid-base-mediated mechanism involving '''three catalytic residues''' (<scene name='Triose_Phosphate_Isomerase/Three_catalytic_residues/6'>restore initial scene</scene>), each of which <scene name='Triose_Phosphate_Isomerase/Three_catalytic_residues/14'>contacts the substrate</scene>.  First, the DHAP or GAP substrate is initially attracted to the enzyme active site through '''electrostatic interactions''' between the negatively charged phosphate group of the substrate and the positively charged '''Lys12''',
+TPI carries out the isomerization reaction through an acid-base-mediated mechanism involving '''three catalytic residues''' (<scene name='Triose_Phosphate_Isomerase/Three_catalytic_residues1/1'>restore initial scene</scene>), each of which <scene name='Triose_Phosphate_Isomerase/Three_catalytic_residues/14'>contacts the substrate</scene>.  First, the DHAP or GAP substrate is initially attracted to the enzyme active site through '''electrostatic interactions''' between the negatively charged phosphate group of the substrate and the positively charged '''Lys12''',
 <!--<scene name='Triose_Phosphate_Isomerase/Lys12_shaded/1'>Lys12</scene>,-->
 with the resulting interaction stabilizing the substrate. According to the "classic" mechanism,