Abstract
Enoyl-ACP reductase(ER) catalyses the second reductive step during the cyclical reactions of fatty acid synthesis. Brassica napus NADH-dependent ER has been purified in milligram quantities from Escherichia coli harbouring an expression plasmid containing the plant cDNA. The availability of large quantities of protein has enabled successful crystallization[1] and elucidation of the complete structure of this enzyme[2]. In addition the supply of recombinant protein has allowed detailed kinetic investigations to be carried out. This was not possible with the small quantities of protein available from rape seed material[3].
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© 1997 Springer Science+Business Media Dordrecht
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Fawcett, T., Overend, C. (1997). Kinetic Analysis of the Mechanism of Enoyl-ACP Reductase. In: Williams, J.P., Khan, M.U., Lem, N.W. (eds) Physiology, Biochemistry and Molecular Biology of Plant Lipids. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-2662-7_26
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DOI: https://doi.org/10.1007/978-94-017-2662-7_26
Publisher Name: Springer, Dordrecht
Print ISBN: 978-90-481-4784-7
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