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Wiley, Angewandte Chemie International Edition, 52(52), p. 13991-13996, 2013

DOI: 10.1002/anie.201306302

Wiley, Angewandte Chemie, 52(125), p. 14241-14246, 2013

DOI: 10.1002/ange.201306302

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The Cyanobactin Heterocyclase Enzyme: A Processive Adenylase That Operates with a Defined Order of Reaction**

Journal article published in 2013 by Jesko Koehnke, Andrew F. Bent, David Zollman, Kieran Smith, Wael E. Houssen ORCID, Xiaofeng Zhu, Greg Mann, Tomas Lebl, Richard Scharff, Sally Shirran, Catherine H. Botting, Marcel Jaspars, Ulrich Schwarz-Linek, James H. Naismith ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Counting backwards: The cyanobactin class of heterocyclases, exemplified by TruD, possess an almost unique combination of processivity, specificity, chemical versatility, and promiscuity. TruD is shown by biochemical assay to be an adenylase, and processes cysteines in a defined order. The entire substrate leader can be removed and TruD will process a single specific cysteine residue; however the role of leader is to permit processivity through a balance of recognition. ATP/AMP=adenosine tri/monophosphate; PPi=pyrophosphate.