Developmental variation in aspartate-family amino acid biosynthesis by isolated chloroplasts

Date

1990

Authors

Mills, Ronald

Journal Title

Journal ISSN

Volume Title

Publisher

Kluwer Academic Publishers

Abstract

In the last decade, it has become clear that the chloroplast is the main site, if not the sole site, for the biosynthesis of the nutritionally essential aspartate-derived amino acids (Fig. 1) in plant leaves [1,2]. For example, isolated intact chloroplasts carry out the light-driven synthesis of lysine, threonine, and isoleucine from labeled aspartic acid and malic acid [3]. This can be considered a photosynthetic process since ATP and NADPH produced in light are thought to be used directly (Fig. 1) to drive the synthetic reactions [3].

Description

Keywords

Amino Acid Synthesis, Amino Acid Production, Intact Chloroplast, Developmental Variation, Aspartate Kinase

Citation

Mills, W. R., S. F. Capo, S. A. Bergh, and C. B. Lassiter. 1990. Developmental variation in aspartate-family amino acid biosynthesis by isolated chloroplasts. In: M. Baltscheffsky, ed., Current Research in Photosynthesis. Vol. IV, pp. 271-274, Kluwer Academic Publishers, Netherlands.