Sandbox Reserved 796

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-		+	== References ==
-	As an enzyme, the aldolase must not only encourage and favor the hydrolysis of fructose 1,6-bisphosphate, but also bind the substrate so as to hold it in the active site. The main-chain nitrogens of Ser271 and Gly272 hold the 1-phosphate group while the Lys41, Arg42 and Arg303 residues hold the 6-phosphate group. The five proposed binding residues are in close proximity to the catalytic Lys229, implicating them as participants in the binding process.[4] The C-terminus, which sits just outside of the barrel and catalytic site, of the enzyme also appears to contribute to the catalytic process of the aldolase. Mutations or suppression of the final tyrosine residue (Tyr363) causes a notable drop in the activity of the enzyme. Two cysteine residues have also been implicated in the catalytic process. Though they do not appear to be necessary for catalysis, modification of them does result in a decrease in catalytic activity. The two Cys residues are far from the active site, but do impact the movement of the C-terminus of the enzyme, which further implicates the terminus as participatory in the catalysis.	+

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Revision as of 19:30, 12 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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spinqualitylabelsall models Fructose-1,6-bisphosphate aldolase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Contents 1 Introduction and General Structure 2 Hydrogen and Disulfide Bond 3 Hydrophobic and Hydrophilic Residues 4 Solvent 5 The ligands and ligand contacts 6 Catalytic Residues 7 References

Introduction and General Structure

is an enzyme in glycolysis. 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 of the enzyme while the beta sheets are embedded in the inside of the enzyme.

Hydrogen and Disulfide Bond

are in black and there is no observable disulfide bond in 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.

Hydrophobic and Hydrophilic Residues

The are in orange while the are in teal. 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 enzyme, which indicated that the residues that made up the surface of the enzyme is hydrophilic. 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

is in purple. There are three other ligands in the other subunits (B, C, and D).

Catalytic Residues

are Asn33(A)-Glu187(A)-Lys229(A)(in red)

References