Abstract
Acetyl-CoA carboxylase (ACCase, EC 6.4.1.2) catalyzes an ATP-dependent conversion of acetyl-CoA to malonyl-CoA, which is a regulated step in de novo synthesis of fatty acids that takes place in chloroplasts. In soybean, the chloroplast ACCase is apparently a multiprotein, prokaryotic type of complex [1], that is thought to consist of 4 subunits: biotin carboxylase (BC), biotin carboxyl carrier protein (BCCP), and the alpha and beta transcarboxylase subunits (α- and β-CT). The study of chloroplast ACCase by traditional methods of protein chemistry have proven difficult, hence we started with the isolation of ACCase genes and have initiated attempts to synthesize the subunits in vitro so that the interactions among the components of this enzyme can be studied more completely.
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© 1997 Springer Science+Business Media Dordrecht
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Reverdatto, S.V., Beilinson, V., Nielsen, N.C. (1997). Soybean Chloroplast Acetyl-CoA Carboxylase. 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_9
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DOI: https://doi.org/10.1007/978-94-017-2662-7_9
Publisher Name: Springer, Dordrecht
Print ISBN: 978-90-481-4784-7
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