Sandbox Reserved 796
From Proteopedia
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== Introduction and General Structure == | == Introduction and General Structure == | ||
| - | <scene name='56/563208/Fructose_biphosphate_aldolase/1'>Fructose-1,6-bisphosphate aldolase </scene> is an enzyme in glycolysis, the metabolic pathway that converts glucose into pyruvate and produces cellular energy in form of ATP (adenosine triphosphate). Aldolase catalyzes an aldol cleavage reaction that hydrolyzes fructose 1,6-bisphosphate. | + | <scene name='56/563208/Fructose_biphosphate_aldolase/1'>Fructose-1,6-bisphosphate aldolase </scene> is an enzyme in glycolysis, the metabolic pathway that converts glucose into pyruvate and produces cellular energy in form of ATP (adenosine triphosphate). Aldolase catalyzes an aldol cleavage reaction that hydrolyzes fructose 1,6-bisphosphate into glycerone phosphate and glyceraldehyde 3-phosphate. |
Fructose-1,6-bisphosphate aldolase is a tetramer, <scene name='56/563208/Secondary_structure/1'>the secondary structure</scene> has alpha helices in pinkish purple and beta sheets in blue. The alpha helices are mostly found on the surface (outside) of the enzyme while the beta sheets are embedded in the inside of the enzyme; which might indicate that most of polar amino acids are located on the peripheral helices, while hydrophobic or paired-polar amino acids are found within the beta sheets. | Fructose-1,6-bisphosphate aldolase is a tetramer, <scene name='56/563208/Secondary_structure/1'>the secondary structure</scene> has alpha helices in pinkish purple and beta sheets in blue. The alpha helices are mostly found on the surface (outside) of the enzyme while the beta sheets are embedded in the inside of the enzyme; which might indicate that most of polar amino acids are located on the peripheral helices, while hydrophobic or paired-polar amino acids are found within the beta sheets. | ||
Revision as of 18:17, 16 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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Contents |
Introduction and General Structure
is an enzyme in glycolysis, the metabolic pathway that converts glucose into pyruvate and produces cellular energy in form of ATP (adenosine triphosphate). Aldolase catalyzes an aldol cleavage reaction that hydrolyzes fructose 1,6-bisphosphate into glycerone phosphate and glyceraldehyde 3-phosphate. Fructose-1,6-bisphosphate aldolase is a tetramer, has alpha helices in pinkish purple and beta sheets in blue. The alpha helices are mostly found on the surface (outside) of the enzyme while the beta sheets are embedded in the inside of the enzyme; which might indicate that most of polar amino acids are located on the peripheral helices, while hydrophobic or paired-polar amino acids are found within the beta sheets.
Hydrogen and Disulfide Bond
are in black and there is no observable disulfide bond in the enzyme. Hydrogen bonding holds the molecule together (especially in secondary structure) and stabilizes the enzyme. Based on the position of the hydrogen bonds, we concluded that the beta sheets are parallel to each other since the H-bonds are slanted between sheets.
Hydrophobic and Hydrophilic Residues
The are in orange while the are in teal. The hydrophobic residues are mostly observed in the interior of the enzyme,away from the aqueous solvent(possibly on the beta sheets). The hydrophilic residues are mostly located on the alpha helices (on the outside of this enzyme)which interact with the aqueous solvent. Based on this model, we can conclude that the enzyme is made out of a roughly equal amount of both hydrophobic and hydrophilic residues.
Solvent
(colored in cream) surrounded the surface of the enzyme, which indicated that the residues that made up the surface of the enzyme is hydrophilic (as observed above). With 50% transparency, no water molecules is observed to be inside the enzyme, which indicated that the inner surface of the enzyme must be hydrophobic.
The ligands and ligand contacts
(for chain A) is in purple. There are three other ligands in the other subunits (B, C, and D). No cofactors are present in this enzyme. The main chain nitrogens found within the Ser271 and Gly272 residues hold the 1-phosphate group in position, while the 6-phosphate group is held in position by Lys41, Arg42 and Arg303 residues.
Catalytic Residues
are Asn33(A)-Glu187(A)-Lys229(A)(in red). The lysine residue has the major role in the molecule's catalysis. The positive charge present on the side chain's nitrogen atom attacks a carbon found within the substrate to begin catalysis. Same residues are observed in other subunits (B, C and D).
References
1.
