期刊
METABOLIC ENGINEERING
卷 14, 期 3, 页码 242-251出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ymben.2011.09.003
关键词
Synthetic scaffolds; Metabolite microdomains; Compartmentalization; Protein shells; Shell pores
资金
- Energy Biosciences Institute
- National Science Foundation [CBET-0756801]
- Directorate For Engineering [0756801] Funding Source: National Science Foundation
- Div Of Chem, Bioeng, Env, & Transp Sys [0756801] Funding Source: National Science Foundation
As synthetic pathways built from exogenous enzymes become more complicated, the probability of encountering undesired interactions with host organisms increases, thereby lowering product titer. An emerging strategy to combat this problem is to spatially organize pathway enzymes into multi-protein complexes, where high local concentrations of enzymes and metabolites may enhance flux and limit problematic interactions with the cellular milieu. Co-localizing enzymes using synthetic scaffolds has improved titers for multiple pathways. While lacking physical diffusion barriers, scaffolded systems could concentrate intermediates locally through a mechanism analogous to naturally occurring microdomains. A more direct strategy for compartmentalizing pathway components would be to encapsulate them within protein shells. Several classes of shells have been loaded with exogenous proteins and expressed successfully in industrial hosts. A critical challenge for achieving ideal pathway compartmentalization with protein shells will likely be evolving pores to selectively limit intermediate diffusion. Eventually, these tools should enhance our ability to rationally design metabolic pathways. (C) 2011 Elsevier Inc. All rights reserved.
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