Triose Phosphate Isomerase: Difference between revisions
Eric Martz (talk | contribs) |
Eric Martz (talk | contribs) |
||
| Line 18: | Line 18: | ||
[[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''']] | ||
<StructureSection load='2ypi' size=' | <StructureSection load='2ypi' size='450' side='right' scene='Triose_Phosphate_Isomerase/Three_catalytic_residues1/2'> | ||
TPI carries out the isomerization reaction through an acid-base-mediated mechanism involving '''three catalytic residues''' (<scene name='Triose_Phosphate_Isomerase/Three_catalytic_residues1/2'>restore initial scene</scene>), each of which <scene name='Triose_Phosphate_Isomerase/Three_catalytic_residues2/1'>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_residues1/2'>restore initial scene</scene>), each of which <scene name='Triose_Phosphate_Isomerase/Three_catalytic_residues2/1'>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>,--> | ||
| Line 48: | Line 48: | ||
</StructureSection> | </StructureSection> | ||
===Inhibitors of Triose Phosphate Isomerase=== | ===Inhibitors of Triose Phosphate Isomerase=== | ||