Works (6)

Updated: July 5th, 2023 15:46

2017 journal article

Polyketide Bioderivatization Using the Promiscuous Acyltransferase KirCII

ACS Synthetic Biology, 6(3), 421–427.

By: E. Musiol-Kroll*, F. Zubeil*, T. Schafhauser*, T. Härtner*, A. Kulik*, J. McArthur n, I. Koryakina n, W. Wohlleben* ...

author keywords: antibiotic; kirromycin; polyketide synthase; trans-acyltransferase; engineering click chemistry
MeSH headings : Acyltransferases / metabolism; Anti-Bacterial Agents / metabolism; Bacteria / metabolism; Bacterial Proteins / metabolism; Polyketide Synthases / metabolism; Polyketides / metabolism; Pyridones / metabolism
TL;DR: This work exploits the promiscuity of KirCII to generate new kirromycins with allyl- and propargyl-side chains in vivo, and the latter were utilized as educts for further modification by "click" chemistry. (via Semantic Scholar)
Sources: Web Of Science, ORCID, NC State University Libraries, Crossref
Added: August 6, 2018

2014 journal article

Evaluating nonpolar surface area and liquid chromatography/mass spectrometry response: an application for site occupancy measurements for enzyme intermediates in polyketide biosynthesis

Rapid Communications in Mass Spectrometry, 28(23), 2511–2522.

By: S. Randall n, I. Koryakina n, G. Williams n & D. Muddiman n

MeSH headings : Acyltransferases / metabolism; Chromatography, Liquid / methods; Filtration; Hydrophobic and Hydrophilic Interactions; Mass Spectrometry / methods; Oligopeptides / chemistry; Oligopeptides / metabolism; Peptide Fragments / chemistry; Peptide Fragments / metabolism; Polyketides / chemistry; Polyketides / metabolism
TL;DR: The MS signal as a function of nonpolar surface area (NPSA) is explored in order to better understand this bias in electrospray response and to determine relative LC/MS response for peptides. (via Semantic Scholar)
Sources: Web Of Science, NC State University Libraries, Crossref
Added: August 6, 2018

2013 journal article

Promiscuity of a modular polyketide synthase towards natural and non-natural extender units

Organic & Biomolecular Chemistry, 11(27), 4449.

By: I. Koryakina n, J. McArthur n, M. Draelos n & G. Williams n

MeSH headings : Acyl Coenzyme A / chemistry; Acyl Coenzyme A / metabolism; Bacterial Proteins / chemistry; Bacterial Proteins / metabolism; Coenzyme A Ligases / chemistry; Coenzyme A Ligases / metabolism; Polyketide Synthases / chemistry; Polyketide Synthases / metabolism; Protein Structure, Tertiary; Rhizobium / chemistry; Rhizobium / enzymology; Rhizobium / metabolism; Substrate Specificity
TL;DR: A panel of chemo-enzymatically synthesized acyl-CoA's was used to probe the promiscuity of a polyketide synthase, revealing that the KS is remarkably tolerant to a diverse array of extender units, while the AT likely discriminates betweenextender units that are native to the producing organism. (via Semantic Scholar)
UN Sustainable Development Goal Categories
10. Reduced Inequalities (OpenAlex)
Sources: Web Of Science, ORCID, NC State University Libraries, Crossref
Added: August 6, 2018

2012 journal article

Poly Specific trans-Acyltransferase Machinery Revealed via Engineered Acyl-CoA Synthetases

ACS Chemical Biology, 8(1), 200–208.

By: I. Koryakina*, J. McArthur*, S. Randall, M. Draelos*, E. Musiol*, D. Muddiman*, T. Weber*, G. Williams*

MeSH headings : Acyltransferases / chemistry; Acyltransferases / genetics; Bacterial Proteins / chemistry; Bacterial Proteins / genetics; Chromatography, Liquid; Coenzyme A Ligases / chemistry; Coenzyme A Ligases / genetics; Crystallography, X-Ray; Genetic Variation; Models, Molecular; Substrate Specificity
TL;DR: Results reveal that polyketide biosynthetic machinery might be more tolerant to non-natural substrates than previously established, and that mutant synthetases are valuable tools for probing the specificity of biosynthetics machinery. (via Semantic Scholar)
UN Sustainable Development Goal Categories
Sources: Web Of Science, ORCID, NC State University Libraries, Crossref
Added: August 6, 2018

2011 journal article

A High-Throughput Screen for Directed Evolution of the Natural Product Sulfotransferase LipB

Journal of Biomolecular Screening, 16(8), 845–851.

By: I. Koryakina n, J. Neville n, K. Nonaka, S. Van Lanen* & G. Williams n

author keywords: chemistry; medicinal; organic; synthetic; and combinatorial; enzyme assays or enzyme kinetics; anti-infective drugs; natural products screening
MeSH headings : Acyltransferases / chemistry; Acyltransferases / genetics; Acyltransferases / metabolism; Aminoglycosides / metabolism; Biocatalysis; Biological Products / chemistry; Biological Products / metabolism; Biotransformation; Cloning, Molecular; Colorimetry; Escherichia coli / chemistry; Escherichia coli / enzymology; Escherichia coli / genetics; Escherichia coli Proteins / chemistry; Escherichia coli Proteins / genetics; Escherichia coli Proteins / metabolism; Gene Library; High-Throughput Screening Assays; Nitrobenzenes / analysis; Nitrobenzenes / metabolism; Plasmids; Recombinant Proteins / chemistry; Recombinant Proteins / genetics; Recombinant Proteins / metabolism; Small Molecule Libraries / analysis; Small Molecule Libraries / chemistry; Substrate Specificity
TL;DR: A colorimetric, high-throughput assay suitable for optimizing the activity of the recently discovered sulfotransferase LipB, by directed evolution is described and plans to use the screen to identify LipB variants with altered acceptor specificity and promiscuity for use in sulfation of natural products and other small-molecule therapeutics. (via Semantic Scholar)
Sources: Web Of Science, NC State University Libraries, Crossref
Added: August 6, 2018

2011 journal article

Mutant Malonyl-CoA Synthetases with Altered Specificity for Polyketide Synthase Extender Unit Generation

ChemBioChem, 12(15), 2289–2293.

By: I. Koryakina n & G. Williams n

author keywords: directed evolution; enzymes; polyketides; protein engineering; specificity
MeSH headings : Bacterial Proteins / genetics; Bacterial Proteins / metabolism; Cloning, Molecular; Coenzyme A Ligases / genetics; Coenzyme A Ligases / metabolism; Mutagenesis; Mutant Proteins / genetics; Mutant Proteins / metabolism; Polyketide Synthases / metabolism; Rhizobium / enzymology; Rhizobium / genetics; Substrate Specificity
TL;DR: This work has used structure-guided saturation mutagenesis followed by colorimetric screening to identify mutant malonyl-CoA synthetases with altered substrate specificity with a 240-fold shift in specificity. (via Semantic Scholar)
UN Sustainable Development Goal Categories
Sources: Web Of Science, ORCID, NC State University Libraries, Crossref
Added: August 6, 2018

Citation Index includes data from a number of different sources. If you have questions about the sources of data in the Citation Index or need a set of data which is free to re-distribute, please contact us.

Certain data included herein are derived from the Web of Science© and InCites© (2024) of Clarivate Analytics. All rights reserved. You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.