The Cyanobactin Heterocyclase Enzyme: A Processive Adenylase That Operates with a Defined Order of Reaction1. Issue 52 (8th November 2013)

• Record Type: Journal Article
• Authors: Koehnke, Jesko; Bent, Andrew F.; Zollman, David; Smith, Kieran; Houssen, Wael E.; Zhu, Xiaofeng; Mann, Greg; Lebl, Tomas; Scharff, Richard; Shirran, Sally; Botting, Catherine H.; Jaspars, Marcel; Schwarz‐Linek, Ulrich; Naismith, James H.
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 52(2013)
• Page Start: 13991
• Page End: 13996
• Publication Date: 2013-11-08
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201306302
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Counting backwards</bold>: 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.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg4t3hxf4d" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>