Tracking Down Acetyltransferases | Chemical & Engineering News
Volume 85 Issue 37 | p. 33 | Concentrates
Issue Date: September 10, 2007

Tracking Down Acetyltransferases

Department: Science & Technology
News Channels: Materials SCENE
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By employing a functional group never before used in protein labeling, a new chemical probe could enable closer scrutiny of an enormous and diverse enzyme family (Angew. Chem. Int. Ed., DOI: 10.1002/anie.200702485). A team led by Philip A. Cole at Johns Hopkins School of Medicine and Neil L. Kelleher of the University of Illinois, Urbana-Champaign, designed a probe for capturing acetyltransferases, which are enzymes that use the cofactor acetyl coenzyme A (CoA) to acylate their substrates. At the probe's heart is a thiocarbamate sulfoxide (shown, left), an electron-poor functional group that's attacked by the thiol group of acetyltransferases' nucleophilic cysteine residues (Nu). The reaction releases the CoA directing group and tags the enzyme with a biotin analog for detection and purification (right). The team anticipates that the probe will be useful in identifying unknown CoA-binding proteins involved in signaling or gene regulation and that thiocarbamate sulfoxides will be broadly applicable in protein labeling.

 
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