Group Red – Demacia Gabe, Chris, Tom

- Enzymes with more than one polypeptide chain can change between an active shape and an inactive shape - When the body needs to slow down a reaction, it bonds an allosteric inhibitor to a site on the enzyme that locks it into its inactive shape

 An allosteric inhibitor is the substance that binds to an enzyme to make its active sites inactive

An allosteric inhibitor is a molecule that binds to enzymes and helps decrease their activity. Since these inhibitors molecules block an enzyme’s activity it can kill a pathogen or correct a metabolic imbalance in the body. Many drugs are enzyme inhibitors.

Allosteric inhibition of the protein tyrosine phosphatase-1B (PTP1B) prevents formation of the active conformation of the enzyme by blocking mobility of the catalytic loop, according to research published in the August issue of Nature Structural and Molecular Biology. PTP1B is an attractive target for the therapeutic intervention of metabolic syndromes such as type 2 diabetes and obesity — states that show hallmark resistance to the hormones insulin and leptin — because it is a negative regulator of the relevant hormone receptors. The catalytic site of PTP1B has so far proven intractable to small-molecule drugs, making allosteric inhibition an appealing strategy.

 Feedback Inhibition of Biochemical Pathways Q8&feature=related  Enzyme Regulation (long video 20min) 4A