Sandbox Reserved 784

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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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pyruvate kinase

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Introduction

Pyruvate kinase (PDB 4IP7) is a transferase. It plays a key role in glycolysis by catalyzing the reaction of ADP and phosphoenolpyruvate to ATP and pyruvate. (1)

Current research into this molecule is being done on its role in the altered metabolism in cancer cells in the M2 form of the enzyme.(2) There is also research being done on inhibitors and activators on the enzyme in order to manipulate its activity. (3)

Structure

Pyruvate kinase is a , meaning it has four identical . This enzyme contains both and .

It has three . consists of an alpha-beta-alpha 3-layer sandwich. consists of a parallel alpha-beta barrel. consists of an anti-parallel beta-barrel.

in the backbone show the interactions within the elements of secondary structure.

of the side chains is shown. Hydrophobic side chains are grey while hydrophilic side chains are purple. You can see that the hydrophobic residues are mostly on the interior, buried within the protein, while hydrophilic are on the outside. is in contact with most of the chain except the largely hydrophobic 3 beta barrel (shown in green). When looking at the quaternary , water is present over most of the exterior except the cavity in the middle and the outer barrels in 3 (green).

The with such as Arg (+ charge), Lys (+ charge), Thr (polar), Gly (nonpolar), and Asp (- charge).

The 4IP7 form of pyruvate kinase does not contain catalytic residues according to PDBsum. However, , the activator-bound form, shows similar and does show its (in green).

References

1. Holyoak, T.; Zhang, B.; Deng, J.; Tang, Q.; Prasannan, C. B.; Fenton, A. W. Energetic Coupling between an Oxidizable Cysteine and the Phosphorylatable N-Terminus of Human Liver Pyruvate Kinase. 2013, 52, 466-476.

2. Yang, W.; Lu, Z. Regulation and function of pyruvate kinase M2 in cancer. Cancer Lett. 2013, 339, 153-158.

3. Faustova, I.; Järv, J. Interaction of Non-Phosphorylated Liver Pyruvate Kinase with Fructose 1,6-Bisphosphate and Peptides that Mimic the Phosphorylatable N-terminus of the Enzyme. Protein Pept. Lett. 2013, 20, 1200-1203.

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