Regulation of phenylalanine ammonia-lyase synthesis by cinnamic acid.  Its implication for the light mediated regulation of the enzyme.
1. There is an increase in the extractable acitivity of phenylalanine ammonia-lyase following excision of hypocotyl segments of dark-grown gherkin seedlings  This increase is prevented by the reaction product, cinnamin acid.  2. Density-labelling experiments show that cinnamic acid affects the rate of enzyme synthesis.  By contrast the regulation of phenylalanine ammonia-lyase activity by light has previously been shown to involve activation of existing inactive enzyme.  3. It is proposed that regulation of synthesis by reaction products represents a mechanism for controlling the size of the pool of phenylalanine ammonia-lyase, and that the activity of this pool is regulated by light.
D000135:Acid Phosphatase / Q000378:metabolism; D000642:Ammonia-Lyases / Q000378:metabolism*; D002499:Centrifugation, Density Gradient; D002934:Cinnamates / Q000494:pharmacology*; D008027:Light; D010650:Phenylalanine Ammonia-Lyase / Q000378:metabolism*; D010944:Plants / Q000201:enzymology; D012639:Seeds / Q000187:drug effects / Q000528:radiation effects; D013997:Time Factors
D002934:Cinnamates; D000135:Acid Phosphatase; D000642:Ammonia-Lyases; D010650:Phenylalanine Ammonia-Lyase