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catharanthus roseus/tyrosine

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Evidence of protein-tyrosine kinase activity in Catharanthus roseus roots transformed by Agrobacterium rhizogenes.

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Homogenate fractions (soluble and particulate) from transformed roots of Catharanthus roseus (L.) G. Don showed several phosphorylated proteins when incubated with gamma-[32P]ATP. The phosphorylation in the proteins of 55, 40, 25, 18 and 10 kDa in the particulate fraction and 63 kDa in the soluble

A pathogen-responsive gene of parsley encodes tyrosine decarboxylase.

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A group of recently isolated parsley (Petroselinum crispum) cDNAs representing genes that are transcriptionally activated upon fungal infection or elicitor treatment have been demonstrated to encode tyrosine decarboxylase (TyrDC). The deduced TyrDC protein sequence shares extensive similarity with

Wounding activates a 47 kDa MAP kinase in Catharanthus roseus (L.) G. Don.

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Catharanthus roseus (L.) G. Don. is an important medicinal plant (Fam. Apocynaceae) known for its alkaloids that are accumulated in response to various biotic and abiotic stresses including wounding. Mitogen activated protein (MAP) kinases are important components of cellular signaling system
The purification of tryptophan decarboxylase from Catharanthus roseus (TDC, E.C.:4.1.1.27), to apparent homogeneity, is described. The enzyme represents a soluble protein with a molecular weight of 115 000±3 000, consisting of 2 identical subunits of 54 000±1 000. The pI was estimated to be 5.9 and
Mitogen activated protein (MAP) kinase-like activity was determined in extracts obtained from transformed Catharanthus roseus hairy roots by the ability to phosphorylate myelin basic protein (MBP). Both in solution and in gel kinase assays showed variation in activity, depending on root

Antidiabetic and antioxidant properties of alkaloids from Catharanthus roseus (L.) G. Don.

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Catharanthus roseus (L.) G. Don is a herbal plant traditionally used by local populations in India, South Africa, China and Malaysia to treat diabetes. The present study reports the in vitro antioxidant and antidiabetic activities of the major alkaloids isolated from Catharanthus roseus (L.) G. Don

Investigation of a substrate-specifying residue within Papaver somniferum and Catharanthus roseus aromatic amino acid decarboxylases.

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Plant aromatic amino acid decarboxylases (AAADs) catalyze the decarboxylation of aromatic amino acids with either benzene or indole rings. Because the substrate selectivity of AAADs is intimately related to their physiological functions, primary sequence data and their differentiation could provide

Metabolic alteration of Catharanthus roseus cell suspension cultures overexpressing geraniol synthase in the plastids or cytosol.

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Previous studies showed that geraniol could be an upstream limiting factor in the monoterpenoid pathway towards the production of terpenoid indole alkaloid (TIA) in Catharanthus roseus cells and hairy root cultures. This shortage in precursor availability could be due to (1) limited

Biochemical evaluation of the decarboxylation and decarboxylation-deamination activities of plant aromatic amino acid decarboxylases.

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Plant aromatic amino acid decarboxylase (AAAD) enzymes are capable of catalyzing either decarboxylation or decarboxylation-deamination on various combinations of aromatic amino acid substrates. These two different activities result in the production of arylalkylamines and the formation of aromatic

Producing Gram-Scale Unnatural Rosavin Analogues from Glucose by Engineered Escherichia coli.

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Cinnamyl alcohol glycosides (CAGs) are key active ingredients of the precious medicinal plant Rhodiola rosea L., which has diverse pharmacological activities. The quality of R. rosea extracts is standardized to the contents of rosavin, a cinnamyl alcohol disaccharide, along with
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