7 results match your criteria: "and Joint BioEnergy Institute[Affiliation]"
bioRxiv
December 2023
Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720 USA and Department of Chemical & Biomolecular Engineering, University of California, Berkeley, Berkeley, CA 94720 USA and Department of Molecular & Cell Biology, University of California, Berkeley, Berkeley, CA 94720 USA.
Amino acids (AAs) are modular and modifiable building blocks which nature uses to synthesize both macromolecules, such as proteins, and small molecule natural products, such as alkaloids and non-ribosomal peptides (NRPs). While the 20 main proteinogenic AAs display relatively limited side-chain diversity, a wide range of non-canonical amino acids (ncAAs) exist that are not used by the ribosome for protein synthesis but contain a broad array of structural features and functional groups not found in proteinogenic AAs. In this communication, we report the discovery of the biosynthetic pathway for a new ncAA, pazamine, which contains a cyclopropane ring formed in two steps.
View Article and Find Full Text PDFPhys Chem Chem Phys
February 2020
Advanced Biofuel and Bioproducts Process Development Unit (ABPDU), Lawrence Berkeley National Laboratory, Berkeley, CA, USA. and Biological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
Keggin-type polyoxometalate derived ionic liquids (POM-ILs) have recently been presented as effective solvent systems for biomass delignification. To investigate the mechanism of lignin dissolution in POM-ILs, the system involving POM-IL ([C4C1Im][PWO]) and guaiacyl glycerol-β-guaiacyl ether (GGE), which contains a β-O-4 bond (the most dominant bond moiety in lignin), was studied using quantum mechanical calculations and molecular dynamics simulations. These studies show that more stable POM-IL structures are formed when [C4C1Im] is anchored in the connecting four terminal oxygen region of the [PWO] surface.
View Article and Find Full Text PDFMetab Eng
January 2018
DOE Joint BioEnergy Institute, Emeryville, CA 94608, United States; Biological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, United States; Department of Chemical Engineering and Bioengineering, University of California at Berkeley and Physical Biosciences Division, Lawrence Berkeley National Laboratory, and Joint BioEnergy Institute, Emeryville, CA, United States. Electronic address:
Euphorbiaceae are an important source of medically important diterpenoids, such as the anticancer drug ingenol-3-angelate and the antiretroviral drug prostratin. However, extraction from the genetically intractable natural producers is often limited by the small quantities produced, while the organic synthesis of terpene-derived drugs is challenging and similarly low-yielding. While transplanting the biosynthetic pathway into a heterologous host has proven successful for some drugs, it has been largely unsuccessful for diterpenoids due to their elaborate biosynthetic pathways and lack of genetic resources and tools for gene discovery.
View Article and Find Full Text PDFCurr Biol
November 2016
Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, UK. Electronic address:
Stomatal opening and closure depends on changes in turgor pressure acting within guard cells to alter cell shape [1]. The extent of these shape changes is limited by the mechanical properties of the cells, which will be largely dependent on the structure of the cell walls. Although it has long been observed that guard cells are anisotropic due to differential thickening and the orientation of cellulose microfibrils [2], our understanding of the composition of the cell wall that allows them to undergo repeated swelling and deflation remains surprisingly poor.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
March 2015
Department of Biochemistry and the Institute for Protein Design, Biomolecular Structure and Design Program, Howard Hughes Medical Institute,
We describe a computationally designed enzyme, formolase (FLS), which catalyzes the carboligation of three one-carbon formaldehyde molecules into one three-carbon dihydroxyacetone molecule. The existence of FLS enables the design of a new carbon fixation pathway, the formolase pathway, consisting of a small number of thermodynamically favorable chemical transformations that convert formate into a three-carbon sugar in central metabolism. The formolase pathway is predicted to use carbon more efficiently and with less backward flux than any naturally occurring one-carbon assimilation pathway.
View Article and Find Full Text PDFElife
November 2014
Benjamin Schwessinger is in the Department of Plant Pathology, University of California, Davis, Davis, United States and Joint Bioenergy Institute, Emeryville, United States
Members of UAW 5810—the union for postdoctoral researchers at the University of California—describe how their union has led to improved terms and conditions for postdocs.
View Article and Find Full Text PDFFront Plant Sci
December 2013
Department of Cellular and Molecular Medicine, Copenhagen Center for Glycomics, University of Copenhagen Copenhagen, Denmark.