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

Jesko Koehnke, Andrew F Bent, David Zollman, Kieran Smith, Wael E Houssen, Xiaofeng Zhu, Greg Mann, Tomas Lebl, Richard Scharff, Sally Shirran, Catherine H Botting, Marcel Jaspars, Ulrich Schwarz-Linek, James H Naismith

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57 Citations (Scopus)
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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.
Original languageEnglish
Pages (from-to)13991-13996
Number of pages6
JournalAngewandte Chemie International Edition
Volume52
Issue number52
Early online date8 Nov 2013
DOIs
Publication statusPublished - 23 Dec 2013

Keywords

  • adenylation
  • cyanobactins
  • heterocyclase
  • ribosomal peptide pathways

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    Koehnke, J., Bent, A. F., Zollman, D., Smith, K., Houssen, W. E., Zhu, X., Mann, G., Lebl, T., Scharff, R., Shirran, S., Botting, C. H., Jaspars, M., Schwarz-Linek, U., & Naismith, J. H. (2013). The Cyanobactin Heterocyclase Enzyme: A Processive Adenylase That Operates with a Defined Order of Reaction. Angewandte Chemie International Edition, 52(52), 13991-13996. https://doi.org/10.1002/anie.201306302