scispace - formally typeset
J

Jay D. Keasling

Researcher at University of California, Berkeley

Publications -  700
Citations -  58305

Jay D. Keasling is an academic researcher from University of California, Berkeley. The author has contributed to research in topics: Metabolic engineering & Gene. The author has an hindex of 98, co-authored 667 publications receiving 51469 citations. Previous affiliations of Jay D. Keasling include Joint BioEnergy Institute & University of California, San Francisco.

Papers
More filters
Journal ArticleDOI

Production of the antimalarial drug precursor artemisinic acid in engineered yeast

TL;DR: The engineering of Saccharomyces cerevisiae to produce high titres (up to 100 mg l-1) of artemisinic acid using an engineered mevalonate pathway, amorphadiene synthase, and a novel cytochrome P450 monooxygenase from A. annua that performs a three-step oxidation of amorpha-4,11-diene to art Artemisinic acid.
Journal ArticleDOI

Engineering a mevalonate pathway in Escherichia coli for production of terpenoids

TL;DR: The strains developed in this study can serve as platform hosts for the production of any terpenoid compound for which a terpene synthase gene is available, and are the universal precursors to all isoprenoids.
Journal ArticleDOI

Microbial production of fatty-acid-derived fuels and chemicals from plant biomass

TL;DR: The engineering of Escherichia coli is demonstrated to produce structurally tailored fatty esters (biodiesel), fatty alcohols, and waxes directly from simple sugars, a step towards producing these compounds directly from hemicellulose, a major component of plant-derived biomass.
Journal ArticleDOI

Synthetic protein scaffolds provide modular control over metabolic flux

TL;DR: In this article, synthetic protein scaffolds bearing interaction domains from metazoan signaling proteins were used to spatially recruit metabolic enzymes in a designable manner, and the modularity of these domains enabled them to optimize the stoichiometry of three mevalonate biosynthetic enzymes recruited to a synthetic complex.