Triose Phosphate Isomerase: Difference between revisions
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[[Image:classical2.png|center|thumb|500px| '''Classic Mechanism proposed by Knowles and co-workers''']] | [[Image:classical2.png|center|thumb|500px| '''Classic Mechanism proposed by Knowles and co-workers''']] | ||
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''', | <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/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>,--> | <!--<scene name='Triose_Phosphate_Isomerase/Lys12_shaded/1'>Lys12</scene>,--> | ||
with the resulting interaction stabilizing the substrate. According to the "classic" mechanism, | with the resulting interaction stabilizing the substrate. According to the "classic" mechanism, | ||
