Studies of l-Cysteine Biosynthetic Enzymes in Phaseolus vulgaris L
Author(s) -
Ivan K. Smith
Publication year - 1972
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.50.4.477
Subject(s) - phaseolus , serine , biochemistry , biosynthesis , chemistry , cysteine , enzyme , biology , botany
In higher plants the biosynthesis of l-cysteine from l-serine, acetylCoA, and sulfide requires serine transacetylase and O-acetylserine sulfhydrylase. The distribution of these enzymes in kidney bean (Phaseolus vulgaris L. cv. Red Kidney) seedlings was determined. Between one-third and two-thirds of the serine transacetylase activity was associated with mitochondria, whereas all of the O-acetyl-serine sulfhydrylase activity was present in the soluble fraction of cell homogenates. In a 14-day plant approximately two-thirds of the O-acetylserine sulfhydrylase activity and approximately one-half of the serine transacetylase activity was found in the leaves.Sulfur-deficient plants were grown to determine the effect of sulfur status on the levels of cysteine biosynthetic enzymes. Total extractable serine transacetylase activity was not affected by sulfur deficiency; in contrast, there was an increase in O-acetylserine sulfhydrylase activity under these conditions.
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