Journal article

The domains carrying the opposing activities in adenylyltransferase are separated by a central regulatory domain.

Paula Clancy, Yibin Xu, Wally C van Heeswijk, Subhash G Vasudevan, David L Ollis

The FEBS Journal | Published : 2007

Abstract

Adenylyltransferase is a bifunctional enzyme that controls the enzymatic activity of dodecameric glutamine synthetase in Escherichia coli by reversible adenylylation and deadenylylation. Previous studies showed that the two similar but chemically distinct reactions are carried out by separate domains within adenylyltransferase. The N-terminal domain carries the deadenylylation activity, and the C-terminal domain carries the adenylylation activity [Jaggi R, van Heeswijk WC, Westerhoff HV, Ollis DL & Vasudevan SG (1997) EMBO J16, 5562-5571]. In this study, we further map the domain junctions of adenylyltransferase on the basis of solubility and enzymatic analysis of truncation constructs, and ..

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University of Melbourne Researchers