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

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 su...

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Published inAngewandte Chemie International Edition Vol. 52; no. 52; pp. 13991 - 13996
Main 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.
Format Journal Article
LanguageEnglish
Published Weinheim WILEY-VCH Verlag 23.12.2013
WILEY‐VCH Verlag
Wiley Subscription Services, Inc
Wiley-VCH Verlag GmbH & Co
EditionInternational ed. in English
Subjects
Adenylation
Adenylyl Cyclases - metabolism
Bacterial Proteins - genetics
Balancing
Biochemistry
Counting
Cyanobacteria - genetics
cyanobactins
Cysteine
Enzymes
heterocyclase
Recognition
Residues
ribosomal peptide pathways
Versatility
cyanobactins
heterocyclase
ribosomal peptide pathways
adenylation
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Summary: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.
Bibliography:BBSRC - No. BB/K015508/1
ArticleID:ANIE201306302
Funded Access
We thank the staff of beam line I03 at the Diamond Light Source for their support with data collection. This work was funded by the Leverhulme Trust (RPG-2012-504), BBSRC (BB/K015508/1) and the University of St Andrews infrastructure is supported by a Wellcome Trust Capital Award (086036). W.E.H. is a recipient of the Sulsa leaders award.
Leverhulme Trust - No. RPG-2012-504
Sulsa leaders award
istex:A304BD63093447F10E630C087FB8617A311D45FB
Wellcome Trust
ark:/67375/WNG-3L5Q79Z5-G
These authors contributed equally to this work.
We thank the staff of beam line I03 at the Diamond Light Source for their support with data collection. This work was funded by the Leverhulme Trust (RPG‐2012–504), BBSRC (BB/K015508/1) and the University of St Andrews infrastructure is supported by a Wellcome Trust Capital Award (086036). W.E.H. is a recipient of the Sulsa leaders award.
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We thank the staff of beam line I03 at the Diamond Light Source for their support with data collection. This work was funded by the Leverhulme Trust (RPG-2012–504), BBSRC (BB/K015508/1) and the University of St Andrews infrastructure is supported by a Wellcome Trust Capital Award (086036). W.E.H. is a recipient of the Sulsa leaders award.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201306302