What is it about?

Bacterial Enzyme I (EI) is a central regulator of bacterial metabolism and a promising drug target. The C-terminal domain of EI exists as a mixture of active and inactive conformations. In this work we combine biochemical and biophysical techniques to show how functional regulation of EI is attained by diluting the active enzyme with inactive states.

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Why is it important?

Conformational disorder is emerging as an important feature of enzyme catalysis. In this work we use biophysical (NMR, crystallography, MD simulations) and biochemical (enzymology, protein engineering) techniques to show how bacterial Enzyme I is thermodynamically regulated by structural heterogeneity in the active site.


This is the first fruit of an ongoing collaboration with Prof. Vincenzo Venditti‘s group (Dept of Chemistry, Iowa State University). I enjoyed working with Dr. Venditti’s group on the crystallography portion of the work presented here and our discussions about how the crystallographic models relate to data from the other experiments.

Charles Stewart
Iowa State University

Read the Original

This page is a summary of: Hybrid Thermophilic/Mesophilic Enzymes Reveal a Role for Conformational Disorder in Regulation of Bacterial Enzyme I, Journal of Molecular Biology, July 2020, Elsevier,
DOI: 10.1016/j.jmb.2020.05.024.
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