Substrate channelling as an approach to cascade reactions
- 22 March 2016
- journal article
- review article
- Published by Springer Science and Business Media LLC in Nature Chemistry
- Vol. 8 (4), 299-309
- https://doi.org/10.1038/nchem.2459
Abstract
In enzyme-catalysed metabolic pathways, substrate channelling often directs the movement of intermediates from one active site to the next. Intramolecular tunnels, electrostatic interactions and chemical swing arms pass intermediates from one enzyme to the next, enhancing pathway catalysis. Introducing mechanisms of bounded diffusion in chemical cascades can increase selectivity, transient rates and overall yield.This publication has 115 references indexed in Scilit:
- Fine Tuning of Spatial Arrangement of Enzymes in a PCNA-Mediated Multienzyme Complex Using a Rigid Poly-L-Proline LinkerPLOS ONE, 2013
- Engineering nanoscale protein compartments for synthetic organellesCurrent Opinion in Biotechnology, 2013
- Regulation of an Enzyme Cascade Reaction by a DNA MachineSmall, 2013
- Enzymatic transformation of nonfood biomass to starchProceedings of the National Academy of Sciences of the United States of America, 2013
- Butyrate production in engineered Escherichia coli with synthetic scaffoldsBiotechnology & Bioengineering, 2013
- Interenzyme Substrate Diffusion for an Enzyme Cascade Organized on Spatially Addressable DNA NanostructuresJournal of the American Chemical Society, 2012
- DNA-guided assembly of biosynthetic pathways promotes improved catalytic efficiencyNucleic Acids Research, 2011
- Channeling by Proximity: The Catalytic Advantages of Active Site Colocalization Using Brownian DynamicsThe Journal of Physical Chemistry Letters, 2010
- DNA-directed assembly of artificial multienzyme complexesBiochemical and Biophysical Research Communications, 2008
- Electrostatic Channeling in the Bifunctional Enzyme Dihydrofolate Reductase-thymidylate SynthaseJournal of Molecular Biology, 1996