Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.2.1.22 (cystathionine beta-synthase)
 965 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The advances in molecular genetics and biotechnology in the field of medicinal plant research are discussed with focusing on the works using transgenic plants. Differentiated organ cultures and transgenic teratomas, incited by the infection with mutants of Agrobacterium Ti and Ri plasmids, were established in quinolizidine-alkaloid producing plants and Solanaceae plants. These cultured cells were used for the production and bioconversion of specific alkaloids produced in these plants. The methods of integration of foreign genes into medicinal plants were developed using an Ri binary vector. The mode of gene expression driven by TR1'-2' promoters was elucidated in transgenic medicinal plants, e.g., Nicotiana tabacum, Glycyrrhiza uralensis, Digitalis purpurea and Atropa belladonna. The genes for herbicide resistance, mammalian cytochrome P450 and bacterial beta-hydroxydecanoylthioester dehydrase were transferred and expressed in plants either to confer herbicide-resistant trait or to change the pattern of metabolites. The cDNA clones encoding cysteine synthase responsible for sulfur assimilation and biosynthesis of non-protein amino acids were isolated and characterized from Spinacea oleracea and Citrullus vulgaris. The functional lysine residue was identified by site-directed mutagenesis experiments. An over-expression system in Escherichia coli was constructed for the bacterial production of the plant specific non-protein amino acids. We made transgenic N. tabacum integrated with sense- and antisense-constructs of cysteine synthase cDNA driven by cauliflower mosaic virus 35S promoter for the purpose of genetic manipulation of biosynthetic flow of cysteine in plants. The future prospects of medicinal plant research are also discussed in the context of modern plant molecular biology.
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PMID:[Molecular genetics and biotechnology in medicinal plants: studies by transgenic plants]. 813 55

Cytochrome P450 was the first hemoprotein found to have a thiolate anion as the axial ligand of the heme. Several other heme-thiolate proteins, including nitric oxide synthase, were later found in animals, plants, and microorganisms. Both cytochrome P450 and nitric oxide synthase, two major members of the heme-thiolate protein family, catalyze monooxygenase reactions, but the physiological functions of other heme-thiolate proteins are apparently highly diverse. Chloroperoxidase of a mold, Caldaryomyces fumago, catalyzes a haloperoxidase reaction. CooA of a bacterium, Rhodospirillum rubrum, and heme-regulated eIF2alpha kinase of animals function as the sensors for carbon monoxide and nitric oxide, respectively, to elicit biological responses to these gases. The role of heme in the enzymatic activity of cystathionine beta-synthase is still unknown. It is likely that more heme-thiolate proteins with diversified functions will be found in various organisms in the future.
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PMID:Heme-thiolate proteins. 1619 3