Gavin John Williams

Targeted enzyme modifications enable regioselective biosynthesis of fluorinated polyketides

CHEM CATALYSIS, 2(10), 2440–2443.

Computationally-guided exchange of substrate selectivity motifs in a modular polyketide synthase acyltransferase

NATURE COMMUNICATIONS, 12(1).

Development of Genetically Encoded Biosensors for Reporting the Methyltransferase-Dependent Biosynthesis of Semisynthetic Macrolide Antibiotics

ACS SYNTHETIC BIOLOGY, 10(10), 2520–2531.

Protein engineering for natural product biosynthesis and synthetic biology applications

[Review of ]. PROTEIN ENGINEERING DESIGN & SELECTION, 34.

Transcription factor-based biosensors: a molecular-guided approach for natural product engineering

[Review of ]. CURRENT OPINION IN BIOTECHNOLOGY, 69, 172–181.

An artificial pathway for polyketide biosynthesis

Nature Catalysis, 3(7), 536–538.

Cheminformatics Analysis and Modeling with MacrolactoneDB

Scientific Reports, 10(1).

Computationally-guided exchange of substrate selectivity motifs in a modular polyketide synthase acyltransferase

Kalkreuter, E., Bingham, K. S., Keeler, A. M., Lowell, A. N., Schmidt, J. J., Sherman, D. H., & Williams, G. J. (2020, April 25). (Vol. 4). Vol. 4.

SIME: synthetic insight-based macrolide enumerator to generate the V1B library of 1 billion macrolides

Journal of Cheminformatics, 12(1).

Synthetic biology enabling access to designer polyketides

Current Opinion in Chemical Biology, 58, 45–53.

Synthetic biology, combinatorial biosynthesis, and chemo-enzymatic synthesis of isoprenoids (September, 10.1007/s10295-020-02306-3, 2020)

Malico, A. A., Calzini, M. A., Gayen, A. K., & Williams, G. J. (2020, December). JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY, Vol. 47, pp. 1181–1181.

Synthetic biology, combinatorial biosynthesis, and chemo‑enzymatic synthesis of isoprenoids

Journal of Industrial Microbiology & Biotechnology, 47(9-10), 675–702.

An Artificial Pathway for Isoprenoid Biosynthesis Decoupled from Native Hemiterpene Metabolism

ACS Synthetic Biology, 8(2), 232–238.

Cover Feature: Probing the Substrate Promiscuity of Isopentenyl Phosphate Kinase as a Platform for Hemiterpene Analogue Production (ChemBioChem 17/2019)

ChemBioChem, 8.

Development of a Genetically Encoded Biosensor for Detection of Polyketide Synthase Extender Units in Escherichia coli

ACS Synthetic Biology, 8(6), 1391–1400.

Engineering the Substrate Specificity of a Modular Polyketide Synthase for Installation of Consecutive Non-Natural Extender Units

Journal of the American Chemical Society, 141(5), 1961–1969.

Probing the Substrate Promiscuity of Isopentenyl Phosphate Kinase as a Platform for Hemiterpene Analogue Production

ChemBioChem, 20(17), 2217–2221.

Probing the Substrate Promiscuity of Isopentenyl Phosphate Kinase as a Platform for Hemiterpene Analogue Production

Lund, S., Courtney, T., & Williams, G. (2019, February 26). (Vol. 2). Vol. 2.

Cheminformatics-based enumeration and analysis of large libraries of macrolide scaffolds

Journal of Cheminformatics, 10(1).

Development of Transcription Factor-Based Designer Macrolide Biosensors for Metabolic Engineering and Synthetic Biology

ACS Synthetic Biology, 7(1), 227–239.

Engineering enzymatic assembly lines for the production of new antimicrobials

Current Opinion in Microbiology, 45, 140–148.

Extender Unit Promiscuity and Orthogonal Protein Interactions of an Aminomalonyl-ACP Utilizing Trans-Acyltransferase from Zwittermicin Biosynthesis

ACS Chemical Biology, 13(12), 3361–3373.

Direct analysis of terpenes from biological buffer systems using SESI and IR-MALDESI

Analytical and Bioanalytical Chemistry, 410(3), 953–962.

Inversion of Extender Unit Selectivity in the Erythromycin Polyketide Synthase by Acyltransferase Domain Engineering

ACS Chemical Biology, 12(1), 114–123.

Polyketide Bioderivatization Using the Promiscuous Acyltransferase KirCII

ACS Synthetic Biology, 6(3), 421–427.

Harnessing natural product assembly lines: structure, promiscuity, and engineering

Journal of Industrial Microbiology & Biotechnology, 43(2-3), 371–387.

Harnessing the promiscuity of natural product biosynthesis: A platform for engineering pathways with new specificities

Planta Medica, 81(11).

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.

Intracellular Light-Activation of Riboswitch Activity

ChemBioChem, 15(9), 1346–1351.

Mapping a Ketosynthase:Acyl Carrier Protein Binding Interface via Unnatural Amino Acid-Mediated Photo-Cross-Linking

Biochemistry, 53(48), 7494–7502.

Reprogramming Acyl Carrier Protein Interactions of an Acyl-CoA Promiscuous trans-Acyltransferase

Chemistry & Biology, 21(5), 636–646.

Synthetic Biology Approaches For Combinatorial Biosynthesis Of Polyketide Natural Products.

Abstracts of Papers for the American Chemical Society. Presented at the 247th National Spring Meeting of the American Chemical Society, Dallas, Texas, USA.

Engineering polyketide synthases and nonribosomal peptide synthetases

Current Opinion in Structural Biology, 23(4), 603–612.

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

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

Reprogramming the Biosynthesis of Natural Products by Directed Evolution

In A. Kantardjieff, P. Asuri, J. L. Coffman, & K. Jayapal (Eds.), Developments in Biotechnology and Bioprocessing (pp. 147–163).

Engineering Glycosyltransferases

In S. Lutz & U. T. Bornscheuer (Eds.), The Protein Engineering Handbook (Vol. 3, pp. 303–326). Weinheim: Wiley-HCH.

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

ACS Chemical Biology, 8(1), 200–208.

Reprogramming the biosynthesis of natural products by directed evolution.

Abstracts of Papers of the American Chemical Society. Presented at the 243rd National Spring Meeting of the American Chemical Society, San Diego, CA, USA.

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

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

A high-throughput screen for directed evolution of aminocoumarin amide synthetases

Analytical Biochemistry, 419(1), 61–66.

A photocrosslinking assay for reporting protein interactions in polyketide and fatty acid synthases

Molecular BioSystems, 7(11), 3152.

Inside Cover: Mutant Malonyl-CoA Synthetases with Altered Specificity for Polyketide Synthase Extender Unit Generation (ChemBioChem 15/2011)

ChemBioChem, 12(15), 2230–2230.

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

ChemBioChem, 12(15), 2289–2293.

Recombinant E. coli Prototype Strains for in Vivo Glycorandomization

ACS Chemical Biology, 6(1), 95–100.

Natural Product Glycosyltransferases: Properties and Applications

In Advances in Enzymology - and Related Areas of Molecular Biology (pp. 55–119).

A high-throughput fluorescence-based glycosyltransferase screen and its application in directed evolution

Nature Protocols, 3(3), 357–362.

Optimizing Glycosyltransferase Specificity via “Hot Spot” Saturation Mutagenesis Presents a Catalyst for Novobiocin Glycorandomization

Chemistry & Biology, 15(4), 393–401.

Probing the Aglycon Promiscuity of an Engineered Glycosyltransferase

Angewandte Chemie International Edition, 47(46), 8889–8892.

The impact of enzyme engineering upon natural product glycodiversification

Current Opinion in Chemical Biology, 12(5), 556–564.

Stereochemically Complementary Biocatalysts Created by Directed Evolution

Synfacts, 2007(2), 0208–0208.

Creation of a Pair of Stereochemically Complementary Biocatalysts

Journal of the American Chemical Society, 128(50), 16238–16247.

Structure-guided saturation mutagenesis of N-acetylneuraminic acid lyase for the synthesis of sialic acid mimetics

Protein Engineering, Design and Selection, 18(5), 239–246.

Directed evolution: Creating new enzymes

The Biochemist, 25(4), 13–15.

Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution

Proceedings of the National Academy of Sciences, 100(6), 3143–3148.