We discuss here the construction of cell free biocatalytic pathways as added free enzymes or multi-enzyme modules that may contain heterologous catalysts. As a result, a cell-free biocatalysis allows the manipulation of substrate ratios, provision of regenerated cofactors and adjustment of high energy flux ratios that are difficult or impossible to control in whole cell synthesis. However, many whole cell production processes are beset by toxicity problems, metabolite competition, the production of side products, sub-optimal enzyme ratios and varying temperature optima. Industry has depended on chemical catalysts because of the known constraints experienced frequently with biological catalysts but when high stereochemistry, mild synthesis conditions and environmentally friendly processes are significant, application of enzymes is preferred, especially in the case of drug synthesis where enantioselectivity is important. The ability to assemble multiple enzymes into synthetic pathways is a new development aided by the synthetic biology approach of constructing and assembling suitable enzymes into pathways that may or may not occur in Nature to provide a high-impact platform for bio-manufacturing of chemicals, biofuels and pharmaceuticals. Such processes have been developed largely through the process of discovery. Genetically engineered host bacteria have an extensive history for the production of specific proteins including the synthesis of single enzymes for the modification of compounds produced for industrial purposes by biological or chemical processes. 3Biomolecular Discovery Research Centre, Macquarie University, Sydney, NSW, Australia.2Department of Molecular Medicine & Pathology, The University of Auckland, Auckland, New Zealand.1Department of Molecular Sciences, Macquarie University, Sydney, NSW, Australia.Bergquist 1,2 Sana Siddiqui 1 Anwar Sunna 1,3*
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