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How Human ACP synthase works:

Can it lead to development of novel antibiotics?

A recent discovery was made which led to a proposal of a detailed mechanism describing the binding of this enzyme to substrates. Recent determination of the crystal structure of the enzyme can lead to ways of designing inhibitors that specifically target bacterial phosphopantetheinyl transferase (PPT) while not affecting the structurally similar human PPT. Discovery of such antibiotics could also help to reduce the cases of obesity and diabetes. (Bunkoczi et al., 2007).

This report examines the connections between those diseases, and how they are related to the structure and catalytic mechanism of human ACP synthase.

Home| Introduction | Background | Results | Conclusion | Reference