Sandbox 172: Difference between revisions
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[[Image:Glucosebinding.jpg|thumb|left|The conformational change in hexokinase caused by glucose binding.<ref>Martin D., Huang P., Pelicano H., Xu R. Glycolysis inhibition for anticancer treatment. Oncogene. 2006. '''25''': 4633-4646.</ref>]] | [[Image:Glucosebinding.jpg|thumb|left|The conformational change in hexokinase caused by glucose binding.<ref>Martin D., Huang P., Pelicano H., Xu R. Glycolysis inhibition for anticancer treatment. Oncogene. 2006. '''25''': 4633-4646.</ref>]] | ||
===Active Site=== | ===Active Site=== | ||
In the <scene name='Sandbox_172/Mynewscene/2'>active site</scene> of hexokinase type I, <scene name='Sandbox_172/Residue1/1'>Lys 621</scene> and Asp 657 show the hydrogen-bonding distance in which a reactive O6 hydroxyl is situated in between. Here Lys 621 functions to aid the transfer of the phosphate moiety which is negatively charged; Asp 657 serves as a catalytic base or to position the glucose O6 correctly for phosphoryl transfer to take place.<ref name="one" /> Though it may seem that Ser 603 may have functional significance, there has been no observed interaction of Ser 603 with glucose substrates. A torsional rotation of of the hydroxyl group brings about a much better distance for hydrogen bonding of the glucose O6. As a result of this observation, it can be assumed that Ser 603 may have some transient role during [http://en.wikipedia.org/wiki/phosphorylation phosphorylation].<ref name="one" /> | In the <scene name='Sandbox_172/Mynewscene/2'>active site</scene> of hexokinase type I, <scene name='Sandbox_172/Residue1/1'>Lys 621</scene> and <scene name='Sandbox_172/Residue1/2'>Asp 657</scene> show the hydrogen-bonding distance in which a reactive O6 hydroxyl is situated in between. Here Lys 621 functions to aid the transfer of the phosphate moiety which is negatively charged; Asp 657 serves as a catalytic base or to position the glucose O6 correctly for phosphoryl transfer to take place.<ref name="one" /> Though it may seem that | ||
<scene name='Sandbox_172/Residue1/3'>Ser 603</scene>may have functional significance, there has been no observed interaction of Ser 603 with glucose substrates. A torsional rotation of of the hydroxyl group brings about a much better distance for hydrogen bonding of the glucose O6. As a result of this observation, it can be assumed that Ser 603 may have some transient role during [http://en.wikipedia.org/wiki/phosphorylation phosphorylation].<ref name="one" /> | |||
===Regulatory Binding Site=== | ===Regulatory Binding Site=== | ||
As glucose-6-phosphate is being produced it binds to either one of the domains on hexokinase type I. On domain 1, the phosphate moiety is surrounded by Ser 88, Thr 232, and Ser 415. The presence of these three residues generate an anion binding site that is approximately 5.6 Å to the 6 hydroxyl of the glucose that is bound.<ref name="one" /> | As glucose-6-phosphate is being produced it binds to either one of the domains on hexokinase type I. On domain 1, the phosphate moiety is surrounded by Ser 88, Thr 232, and Ser 415. The presence of these three residues generate an anion binding site that is approximately 5.6 Å to the 6 hydroxyl of the glucose that is bound.<ref name="one" /> | ||
