Sandbox Reserved 803
From Proteopedia
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== Hexokinase (Glucokinase) == | == Hexokinase (Glucokinase) == | ||
| - | <scene name='56/563215/Color_coded_helices_and_sheets/1'>Hexokinase</scene>, also known as <scene name='56/563215/Color_coded_helices_and_sheets/1'>glucokinase</scene>, is an enzyme that facilitates the phosphorylation of glucose to glucose-6-phosphate in the first step of glycolysis. Glycolysis is the process by which cells break down a molecule of glucose to release energy which can then be used for various cellular processes. In the image to the right, the helices are shown in a brown, while the sheets are a green color. The other colored space filling model in the image is a glucose molecule, which is the ligand in this enzyme catalyzed reaction. | + | <scene name='56/563215/Color_coded_helices_and_sheets/1'>Hexokinase</scene>, also known as <scene name='56/563215/Color_coded_helices_and_sheets/1'>glucokinase</scene>, is an enzyme that facilitates the phosphorylation of glucose to glucose-6-phosphate in the first step of glycolysis. Glycolysis is the process by which cells break down a molecule of glucose to release energy which can then be used for various cellular processes. Hexokinase is unique in that it functions in both aerobic and anaerobic conditions for glycolysis. In the image to the right, the helices are shown in a brown, while the sheets are a green color. The other colored space filling model in the image is a glucose molecule, which is the ligand in this enzyme catalyzed reaction. |
Hexokinase has many <scene name='56/563215/Hydrogen_bonds/1'>hydrogen bonds</scene> which are used to hold different parts of the protein together. (unfortunately, the link often doesn't work so I am unable to describe how they affect the protein structure specifically.) Hydrogen bonding in the beta sheets can determine if the sheets are parallel or antiparallel. A parallel sheet will have hydrogen bonds that are not formed at right angles to the sheet, while in an antiparallel sheet, the bonds will be about perpendicular to the sheets. Disulfide bonds are not seen in hexokinase because the protein is an intercellular protein, and the intercellular environment is reducing, meaning that most disulfide bonds will be reduced inside the cell. | Hexokinase has many <scene name='56/563215/Hydrogen_bonds/1'>hydrogen bonds</scene> which are used to hold different parts of the protein together. (unfortunately, the link often doesn't work so I am unable to describe how they affect the protein structure specifically.) Hydrogen bonding in the beta sheets can determine if the sheets are parallel or antiparallel. A parallel sheet will have hydrogen bonds that are not formed at right angles to the sheet, while in an antiparallel sheet, the bonds will be about perpendicular to the sheets. Disulfide bonds are not seen in hexokinase because the protein is an intercellular protein, and the intercellular environment is reducing, meaning that most disulfide bonds will be reduced inside the cell. | ||
| - | <scene name='56/563215/Hydrophobic_residues/2'>Hydrophobic residues</scene>, colored lime green, are mostly found inside the protein, while the <scene name='56/563215/Hydrophilic_residues/ | + | <scene name='56/563215/Hydrophobic_residues/2'>Hydrophobic residues</scene>, colored lime green, are mostly found inside the protein, while the <scene name='56/563215/Hydrophilic_residues/2'>hydrophilic residues</scene> are mostly found on the outside of the protein. This is due to the interaction of the protein with the intercellular <scene name='56/563215/Water_and_ligand/1'>water</scene> molecules, which push hydrophobic residues into the center of the protein by the hydrophobic effect, while making hydrogen bonds with the polar residues on the outside. |
<scene name='56/563215/Hydrophobic_hydrophilic/1'>hydrophobic and hydrophilic residues</scene> | <scene name='56/563215/Hydrophobic_hydrophilic/1'>hydrophobic and hydrophilic residues</scene> | ||
Revision as of 00:53, 18 October 2013
| This Sandbox is Reserved from Oct 10, 2013, through May 20, 2014 for use in the course "CHEM 410 Biochemistry 1 and 2" taught by Hanna Tims at the Messiah College. This reservation includes Sandbox Reserved 780 through Sandbox Reserved 807. |
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Hexokinase (Glucokinase)
, also known as , is an enzyme that facilitates the phosphorylation of glucose to glucose-6-phosphate in the first step of glycolysis. Glycolysis is the process by which cells break down a molecule of glucose to release energy which can then be used for various cellular processes. Hexokinase is unique in that it functions in both aerobic and anaerobic conditions for glycolysis. In the image to the right, the helices are shown in a brown, while the sheets are a green color. The other colored space filling model in the image is a glucose molecule, which is the ligand in this enzyme catalyzed reaction.
Hexokinase has many which are used to hold different parts of the protein together. (unfortunately, the link often doesn't work so I am unable to describe how they affect the protein structure specifically.) Hydrogen bonding in the beta sheets can determine if the sheets are parallel or antiparallel. A parallel sheet will have hydrogen bonds that are not formed at right angles to the sheet, while in an antiparallel sheet, the bonds will be about perpendicular to the sheets. Disulfide bonds are not seen in hexokinase because the protein is an intercellular protein, and the intercellular environment is reducing, meaning that most disulfide bonds will be reduced inside the cell.
, colored lime green, are mostly found inside the protein, while the are mostly found on the outside of the protein. This is due to the interaction of the protein with the intercellular molecules, which push hydrophobic residues into the center of the protein by the hydrophobic effect, while making hydrogen bonds with the polar residues on the outside.
