Induction of de-novo synthesis of tryptophan decarboxylase in cell suspensions of Catharanthus roseus
- 1 December 1985
- journal article
- research article
- Published by Springer Nature in Planta
- Vol. 166 (4) , 500-504
- https://doi.org/10.1007/bf00391274
Abstract
Tryptophan decarboxylase (EC 4.2.1.27) is synthesized de-novo by Catharanthus roseus cells shortly after the cells have been transferred into culture medium in which monoterpenoid indole alkaloids are formed. The enzyme production, monitored by in-vivo labelling with [35S]methionine and immunoprecipitation, precedes the apparent maximal enzyme activity by 10–12 h. From the time course of the descending enzyme activity after induction, a half-life of 21 h for tryptophan decarboxylase in C. roseus cell suspensions is calculated. A comparison of the polyadenylated-RNA preparations from C. roseus cells indicates that mRNA activity for tryptophan decarboxylase is only detected in cells grown in the production medium. The importance of tryptophan decarboxylase induction with respect to the accumulation of th corresponding alkaloids is discussed.Keywords
This publication has 23 references indexed in Scilit:
- Phosphate Mediated Regulation of Cinnamoyl Putrescine Biosynthesis in Cell Suspension Cultures ofNicotiana tabacumPlanta Medica, 1981
- Enzymatic Synthesis of Ajmalicine and Related Indole AlkaloidsJournal of Natural Products, 1980
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Enzymes of General Phenylpropanoid Metabolism and of Flavonoid Glycoside Biosynthesis in ParsleyPlant Physiology, 1979
- Purification and properties of strictosidine synthetase (an enzyme condensing tryptamine and secologanin) from Catharanthus roseus cultured cellsBiochemistry, 1979
- Isovincoside (strictosidine), the key intermediate in the enzymatic formation of indole alkaloidsFEBS Letters, 1977
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Antigen — Antibody Reactions In GelsActa Pathologica Microbiologica Scandinavica, 1949