Abstract
Aconitase (EC 4.2.1.3) is an enzyme that catalyzes the reaction of reversible conversion between citrate and isocitrate. In cotyledons of oil-storage plants such as pumpkin, aconitase was thought to exist not only in mitochondria as a member of the tricarboxylic acid cycle but also in glyoxysomes as a member of glyoxylate cycle. The glyoxylate cycle is an important pathway for producing sucrose from reserved lipid at early stage of seedling growth under the cooperation of other metabolic pathways such as ß-oxidation.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Similar content being viewed by others
References
De Bellis L, Tsugeki R, Alpi A. Nishimura M. Purification and characterization of aconitase isoforms from etiolated pumpkin cotyledons. Physiol Plant 1993;88:485–492.
De Bellis L, Hayashi M, Biagi PP, Hara-Nishimura I, Alpi A. Nishimura M. Immunological analysis of aconitase in pumpkin cotyledons: the absence of aconitase in glyoxysomes. Physiol Plant 1994;90:757–762.
Courtois-Verniquet F. Douce R. Lack of aconitase in glyoxysomes and peroxisomes. Biochem J 1993; 294:103–107.
De Bellis L, Hayashi M, Nishimura M. Alpi A. Subcellular and developmental changes in distribution of aconitase isoforms in pumpkin cotyledons. Planta in press.
Author information
Authors and Affiliations
Editor information
Rights and permissions
Copyright information
© 1995 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Hayashi, M., Bellis, L.D., Nishimura, M. (1995). Molecular Characterization of Aconitase in Etiolated Pumpkin Cotyledons. In: Kader, JC., Mazliak, P. (eds) Plant Lipid Metabolism. Springer, Dordrecht. https://doi.org/10.1007/978-94-015-8394-7_133
Download citation
DOI: https://doi.org/10.1007/978-94-015-8394-7_133
Publisher Name: Springer, Dordrecht
Print ISBN: 978-90-481-4498-3
Online ISBN: 978-94-015-8394-7
eBook Packages: Springer Book Archive