Triose Phosphate Isomerase: Difference between revisions

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 <applet load='2ypi' size='350' frame='true' align='right' scene=Triose_Phosphate_Isomerase/Three_catalytic_residues/6/>
-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/13'>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_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''',
 <!--<scene name='Triose_Phosphate_Isomerase/Lys12_shaded/1'>Lys12</scene>,-->
 with the resulting interaction stabilizing the substrate. According to the "classic" mechanism,