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Title: Developmental changes in aspartate-family amino acid biosynthesis in pea chloroplasts

Conference · · Plant Physiology, Supplement; (USA)
OSTI ID:5851269

Isolated chloroplasts are known to synthesize the asp-derived amino acids (ile, hse, lys and thr) from ({sup 14}C)asp (Mills et al, 1980, Plant Physiol. 65, 1166). Now, we have studied the influence of tissue age on essential amino acid biosynthesis in pea (Pisum sativum) plastids. Chloroplasts from the younger (third and fourth) leaves of 12 day old plants, were 2-3 times more active in synthesizing lys and thr from ({sup 14}C)asp than those from older (first or second) leaves. We also examined two key pathway enzymes (aspartate kinase and homoserine dehydrogenase); with each enzyme,a activity in younger leaves was about 2 times that in plastids from older tissue. Both lys- and thr-sensitive forms of aspartate kinase are known in plants; in agreement with earlier work, we found that lys-sensitive activity was about 4 times higher in the younger tissues, while the thr-sensitive activity changed little during development (Davies and Miflin, 1977, Plant Sci. Lett. 9, 323). Recently the role of aspartate kinase and homoserine dehydrogenase in controlling asp-family amino acid synthesis has been questioned (Giovanelli et al, 1989, Plant Physiol. 90, 1584); we hope that measurements of amino acid levels in chloroplasts as well as further enzyme studies will help us to better understand the regulation of asp-family amino acid synthesis.

OSTI ID:
5851269
Report Number(s):
CONF-9007196-; CODEN: PPYSA
Journal Information:
Plant Physiology, Supplement; (USA), Vol. 93:1; Conference: Annual meeting of the American Society of Plant Physiologists, Indianapolis, IN (USA), 29 Jul - 2 Aug 1990; ISSN 0079-2241
Country of Publication:
United States
Language:
English