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Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes
- Lindsay M. Repka, J. R. Chekan, S. Nair, W. A. van der Donk
- Biology, ChemistryChemical reviews
- 30 January 2017
This review focuses on studies published over the past decade that have provided much insight into the mechanisms of the enzymes that carry out the post-translational modifications of lanthipeptides.
Xylan utilization in human gut commensal bacteria is orchestrated by unique modular organization of polysaccharide-degrading enzymes
- Meiling Zhang, J. R. Chekan, I. Cann
- BiologyProceedings of the National Academy of Sciences
- 18 August 2014
Significance Fermentation of dietary fiber in the lower gut of humans is a critical process for the function and integrity of both the bacterial community and host cells. Here we demonstrate that two…
Biosynthesis of the neurotoxin domoic acid in a bloom-forming diatom
Using growth conditions known to induce DA production in Pseudo-nitzschia multiseries, transcriptome sequencing was implemented in order to identify DA biosynthesis genes that colocalize in a genomic four-gene cluster, establishing a model forDA biosynthesis.
Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis
- Kyle L. Dunbar, J. R. Chekan, C. Cox, Brandon J. Burkhart, S. Nair, D. Mitchell
- Biology, ChemistryNature chemical biology
- 19 July 2014
This study reports the X-ray crystal structure of an uncharacterized YcaO from Escherichia coli that harbors an unprecedented fold and ATP-binding motif that is conserved among TOMM YcaOs and demonstrates that the C protein regulates substrate binding and catalysis and that the proline-rich C-terminus of the D protein is involved in C protein recognition andCatalysis.
Scalable Biosynthesis of the Seaweed Neurochemical, Kainic Acid.
- J. R. Chekan, Shaun M. K. McKinnie, Malia L Moore, Shane G. Poplawski, T. Michael, B. Moore
- BiologyAngewandte Chemie
- 10 May 2019
This study establishes the feasibility of mining seaweed genomes for their biotechnological prowess and applies a key biosynthetic α-ketoglutarate-dependent dioxygenase enzyme in a biotransformation methodology to efficiently construct kainic acid on the gram scale.
Structural and Biochemical Basis for Mannan Utilization by Caldanaerobius polysaccharolyticus Strain ATCC BAA-17*
Transcriptome sequencing is used to gain insights into mannan degradation by the thermophilic anaerobic bacterium Caldanaerobius polysaccharolyticus and provides a framework for engineering mannan utilization capabilities for microbial fermentation.
Characterization of the macrocyclase involved in the biosynthesis of RiPP cyclic peptides in plants
- J. R. Chekan, P. Estrada, P. Covello, S. Nair
- Biology, ChemistryProceedings of the National Academy of Sciences
- 5 June 2017
It is described how a single enzyme can catalyze the cyclization of a range of ribosomally synthesized linear peptides into the corresponding cyclic products of varying ring sizes to provide a means for producing large libraries of cyclic peptides without any sequence bias.
A common late-stage intermediate in catalysis by 2-hydroxyethyl-phosphonate dioxygenase and methylphosphonate synthase.
- S. Peck, J. R. Chekan, Emily C. Ulrich, S. Nair, W. A. van der Donk
- Chemistry, BiologyJournal of the American Chemical Society
- 26 February 2015
The generation of a bifunctional mutant of HEPD (E176H) that exhibits the activity of both HEPD and MPnS is reported, consistent with an isotope-sensitive branching mechanism involving a common intermediate.
Molecular Basis for Resistance Against Phosphonate Antibiotics and Herbicides.
The current state of knowledge of the structural and biochemical characterization of resistance mechanisms against phosphonic acid antibiotics and herbicides, including fosfomycin, glyphosate, fosmidomycin and FR900098 is reviewed.
Structure of the Lasso Peptide Isopeptidase Identifies a Topology for Processing Threaded Substrates.
- J. R. Chekan, J. Koos, Chuhan Zong, M. O. Maksimov, A. J. Link, S. Nair
- BiologyJournal of the American Chemical Society
- 7 December 2016
Structural-based mutational analysis reveals how this enzyme recognizes the lasso peptide substrate by shape complementarity rather than through sequence specificity, and validate this mining approach by heterologous expression of two clusters encoded within the genome of Asticcaucalis benevestitus, and demonstrate that both clusters produceLasso peptides.