Abstract
The metabolic enzymes like any enzymes generally display globular architecture where secondary structure elements and interactions between them preserve the spatial organization of the protein. A typical enzyme features a well-defined active site, designed for selective binding of the reaction substrate and facilitating a chemical reaction converting the substrate into a product. While many chemical reactions could be facilitated using only the functional groups that are found in proteins, the large percentage or intracellular reactions require use of cofactors, varying from single metal ions to relatively large molecules like numerous coenzymes, nucleotides and their derivatives, dinucleotides or hemes. Quite often these large cofactors become important not only for the catalytic function of the enzyme but also for the structural stability of it, as those are buried deep in the enzyme.
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Acknowledgments
Funding was provided by the BioEnergy Science Center (BESC) and the Center for Bioenergy Innovation (CBI), from the U.S. Department of Energy Bioenergy Research Centers supported by the Office of Biological and Environmental Research in the DOE Office of Science. This work was authored in part by Alliance for Sustainable Energy, LLC, the Manager and Operator of the National Renewable Energy Laboratory for the U.S. Department of Energy (DOE) under Contract No. DE-AC36-08GO28308. The views expressed in the chapter do not necessarily represent the views of the DOE or the U.S. Government. The U.S. Government retains and the publisher, by accepting the chapter for publication, acknowledges that the U.S. Government retains a nonexclusive, paid-up, irrevocable, worldwide license to publish or reproduce the published form of this work, or allow others to do so, for U.S. Government purposes.
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Alahuhta, M., Himmel, M.E., Bomble, Y.J., Lunin, V.V. (2020). Crystallography of Metabolic Enzymes. In: Himmel, M., Bomble, Y. (eds) Metabolic Pathway Engineering. Methods in Molecular Biology, vol 2096. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0195-2_10
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DOI: https://doi.org/10.1007/978-1-0716-0195-2_10
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