Sandbox 172: Difference between revisions

Line 15:

[[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===

In the <scene name='Sandbox_172/Mynewscene/2'>active site</scene> of hexokinase type I, <scene name='Sandbox_172/Residue1/1'>Lys 621</scene>-denoted in red, and <scene name='Sandbox_172/Residue1/2'>Asp 657</scene>-denoted in blue, 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

In the <scene name='Sandbox_172/Mynewscene/2'>active site</scene> of hexokinase type I, <scene name='Sandbox_172/Residue1/4'>Lys 621</scene>-denoted in red, and <scene name='Sandbox_172/Residue1/2'>Asp 657</scene>-denoted in blue, 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>-denoted in black, 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===

Sandbox 172: Difference between revisions

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@@ Line 15: / Line 15: @@
 [[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===
-In the <scene name='Sandbox_172/Mynewscene/2'>active site</scene> of hexokinase type I, <scene name='Sandbox_172/Residue1/1'>Lys 621</scene>-denoted in red, and <scene name='Sandbox_172/Residue1/2'>Asp 657</scene>-denoted in blue, 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
+In the <scene name='Sandbox_172/Mynewscene/2'>active site</scene> of hexokinase type I, <scene name='Sandbox_172/Residue1/4'>Lys 621</scene>-denoted in red, and <scene name='Sandbox_172/Residue1/2'>Asp 657</scene>-denoted in blue, 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>-denoted in black, 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===