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==Glucokinase== | ==Glucokinase== | ||
The enzyme glucokinase facilitates phosphorylation of glucose to glucose-6-phosphate. In humans and most other vertebrates glucokinase is used in the liver, the pancreas, the gut and brain. It plays an important role in regulating carbohydrate metabolism, triggering shifts in the cell in response to glucose level: glucokinase is a sort of a glucose sensor. It only phosphorylates glucose if its concetnration is high enough. The structure of glucokinase reveals an allosteric site through which small molecules may modulate the kinetic properties of the enzyme; a property that is the basis for the enzyme use in type 2 diabetes treatment. | |||
===Structure==={{STRUCTURE_1v4s| PDB=1v4s | SCENE= }} | ===Structure==={{STRUCTURE_1v4s| PDB=1v4s | SCENE= }} | ||
The glucokinase has 18 <scene name='Sandbox22/Alpha_helices/1'>alpha helices</scene> (unless we counted wrong), 13 <scene name='Sandbox22/Beta_sheets/5'>beta sheets</scene> (this one is for sure), and 3 <scene name='Sandbox22/Ligands/1'>ligands</scene>: a sodium ion, | The glucokinase has 18 <scene name='Sandbox22/Alpha_helices/1'>alpha helices</scene> (unless we counted wrong), 13 <scene name='Sandbox22/Beta_sheets/5'>beta sheets</scene> (this one is for sure), and 3 <scene name='Sandbox22/Ligands/1'>ligands</scene>: a <scene name='Sandbox22/Sodium_ion/1'>sodium ion</scene>, <scene name='Sandbox22/Glc/1'>T2 amino-4-fluoro-5-[(1-methyl-1h-amidazol-2-yl)sulfanyl]-n-(1,3-thiazol-2-yl)benzamide</scene> | ||
amide or MRK in short, and last a sugar (alpha-d-glucose) or simply GLC. | |||
Purple denotes all the <scene name='Sandbox22/Polar/2'>polar</scene> sections of the protein: the hydrophillic areas that dominate the outer surface which comes in contact with aqueous environments. In this view we can see very neatly how the beta sheets alternate in polarity in a 'zigzag manner, and how the alpha helices are roughly 2-3 polar (while the inner protein is obviously hydrophobic). The | |||
<scene name='Sandbox22/Spacefill/2'>spacefill representation</scene>, in particular, shows how the surface is dominantly hydrophillic. | |||
===Reference=== | ===Reference=== | ||
http://www.proteopedia.org/wiki/index.php/1v4s | http://www.proteopedia.org/wiki/index.php/1v4s | ||
http://en.wikipedia.org/wiki/Glucokinase | |||
--Tinuke (Abike etc. etc. etc.) Adeyemi and Niva Ran | --Tinuke (Abike etc. etc. etc.) Adeyemi and Niva Ran | ||
Latest revision as of 14:16, 23 May 2009
This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks!
Glucokinase
The enzyme glucokinase facilitates phosphorylation of glucose to glucose-6-phosphate. In humans and most other vertebrates glucokinase is used in the liver, the pancreas, the gut and brain. It plays an important role in regulating carbohydrate metabolism, triggering shifts in the cell in response to glucose level: glucokinase is a sort of a glucose sensor. It only phosphorylates glucose if its concetnration is high enough. The structure of glucokinase reveals an allosteric site through which small molecules may modulate the kinetic properties of the enzyme; a property that is the basis for the enzyme use in type 2 diabetes treatment.
Structure
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| 1v4s, resolution 2.30Å (default scene) | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | GLC, MRK, NA | ||||||||||||
| Activity: | Hexokinase, with EC number 2.7.1.1 | ||||||||||||
| Related: | 1v4t | ||||||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
The glucokinase has 18 alpha helices (unless we counted wrong), 13 beta sheets (this one is for sure), and 3 ligands: a sodium ion, T2 amino-4-fluoro-5-[(1-methyl-1h-amidazol-2-yl)sulfanyl]-n-(1,3-thiazol-2-yl)benzamide amide or MRK in short, and last a sugar (alpha-d-glucose) or simply GLC.
Purple denotes all the polar sections of the protein: the hydrophillic areas that dominate the outer surface which comes in contact with aqueous environments. In this view we can see very neatly how the beta sheets alternate in polarity in a 'zigzag manner, and how the alpha helices are roughly 2-3 polar (while the inner protein is obviously hydrophobic). The spacefill representation, in particular, shows how the surface is dominantly hydrophillic.
Reference
https://www.proteopedia.org/wiki/index.php/1v4s https://en.wikipedia.org/wiki/Glucokinase
--Tinuke (Abike etc. etc. etc.) Adeyemi and Niva Ran
