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].
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Rafferty, JB. et al.,J. Mol. Biol.(1994) 237:240-242.
Rafferty, JB et al.,Structure(1995) 3:927-938.
Slabas, AR. et al.,Biochim. Biophys. Acta(1986) 877:271-280.
Kater, MM et al.,Plant Mol. Biol.(1991) 17:895-909.
Cleland, WW. Biochim. Biophys. Acta(1963) 67: 188 - 192.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1997 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
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
Download citation
DOI: https://doi.org/10.1007/978-94-017-2662-7_26
Publisher Name: Springer, Dordrecht
Print ISBN: 978-90-481-4784-7
Online ISBN: 978-94-017-2662-7
eBook Packages: Springer Book Archive