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

dc.contributor.authorMills, Ronald
dc.date.accessioned2020-07-09T20:56:45Z
dc.date.available2020-07-09T20:56:45Z
dc.date.issued1990
dc.description.abstractIn 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].en_US
dc.identifier.citationMills, 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.en_US
dc.identifier.urihttps://hdl.handle.net/10657.1/2406
dc.language.isoen_USen_US
dc.publisherKluwer Academic Publishersen_US
dc.subjectAmino Acid Synthesis, Amino Acid Production, Intact Chloroplast, Developmental Variation, Aspartate Kinaseen_US
dc.titleDevelopmental variation in aspartate-family amino acid biosynthesis by isolated chloroplastsen_US
dc.typeArticleen_US

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