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papaver somniferum/tyrosine
Krækjan er vistuð á klemmuspjaldið
Bls 1 frá 32 niðurstöður
Expression in Escherichia coli and partial characterization of two tyrosine/dopa decarboxylases from opium poppy.
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Two tyrosine/dopa decarboxylases (TYDC1 and TYDC2) from opium poppy (Papaver somniferum) were heterologously expressed in Escherichia coli and partially characterized. TYDC1 and TYDC2 are representative members of the two major isoform sub-classes of genes found in opium poppy which share less than
Decreased cell wall digestibility in canola transformed with chimeric tyrosine decarboxylase genes from opium poppy
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Tyrosine decarboxylase (TYDC) is a common plant enzyme involved in the biosynthesis of numerous secondary metabolites, including hydroxycinnamic acid amides. Although a definite function has not yet been determined, amides have been proposed to form a physical barrier against pathogens because they
Tyrosine aminotransferase contributes to benzylisoquinoline alkaloid biosynthesis in opium poppy.
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Tyrosine aminotransferase (TyrAT) catalyzes the transamination of L-Tyr and α-ketoglutarate, yielding 4-hydroxyphenylpyruvic acid and L-glutamate. The decarboxylation product of 4-hydroxyphenylpyruvic acid, 4-hydroxyphenylacetaldehyde, is a precursor to a large and diverse group of natural products
Structural Basis of the Substrate Specificity and Enzyme Catalysis of a Papaver somniferum Tyrosine Decarboxylase.
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Tyrosine decarboxylase (TyDC), a type II pyridoxal 5'-phosphate decarboxylase, catalyzes the decarboxylation of tyrosine. Due to a generally high sequence identity to other aromatic amino acid decarboxylases (AAADs), primary sequence information is not enough to understand substrate specificities
Crystal structures clarify cofactor binding of plant tyrosine decarboxylase.
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Plant tyrosine decarboxylase (TyrDC) is a group II pyridoxal 5'-phosphate (PLP)-dependent decarboxylase that mainly catalyzes the decarboxylation of tyrosine to tyramine. This is biologically important for diverting essential primary metabolites into secondary metabolic pathways. Intensive studies
Molecular analysis of a new member of the opium poppy tyrosine/3,4-dihydroxyphenylalanine decarboxylase gene family.
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An aromatic amino acid decarboxylase DNA fragment was generated from opium poppy (Papaver somniferum L.) genomic DNA by the PCR using primers designed from conserved amino acid sequences of other aromatic amino acid decarboxylase genes. Using this fragment as a probe, a genomic clone was isolated
Analysis of promoters from tyrosine/dihydroxyphenylalanine decarboxylase and berberine bridge enzyme genes involved in benzylisoquinoline alkaloid biosynthesis in opium poppy.
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Tyrosine/dihydroxyphenylalanine decarboxylase (TYDC) and the berberine bridge enzyme (BBE) represent the entry point and a key branch point, respectively, in the biosynthesis of benzylisoquinoline alkaloids in select species of the Papaveraceae and Fumariaceae. Genomic clones for tydc7 and bbe1 from
Expression patterns conferred by tyrosine/dihydroxyphenylalanine decarboxylase promoters from opium poppy are conserved in transgenic tobacco.
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Opium poppy (Papaver somniferum) contains a large family of tyrosine/dihydroxyphenylalanine decarboxylase (tydc) genes involved in the biosynthesis of benzylisoquinoline alkaloids and cell wall-bound hydroxycinnamic acid amides. Eight members from two distinct gene subfamilies have been isolated,
Differential and tissue-specific expression of a gene family for tyrosine/dopa decarboxylase in opium poppy.
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Two early and potential rate-limiting steps in the biosynthesis of isoquinoline alkaloids, such as morphine and codeine, in opium poppy (Papaver somniferum) involve decarboxylation of L-tyrosine and L-dihydroxyphenylalanine (L-dopa) to yield tyramine and dopamine, respectively. A DNA fragment was
BIOSYNTHESIS OF ALKALOIDS. ON THE TRANSFORMATION OF TYROSINE TO 3,4-DIHYDROXYPHENYLALANINE IN PAPAVER SOMNIFERUM L. PLANTS.
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Retraction: Structural Basis of the Substrate Specificity and Enzyme Catalysis of a Papaver somniferum Tyrosine Decarboxylase.
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[This retracts the article on p. 5 in vol. 4, PMID: 28232911.].
Proceedings: The oxidation of tyrosine a precursor of morphine by polyphenolase in the 1000g organelles of Papaver somniferum.
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[On the biosynthesis of thebaine from tyrosine in Papaver bracteatum].
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Formation of secondary products derived from tyrosine in Papaver suspension cultures.
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Implication of tyramine in the biosynthesis of morphinan alkaloids in Papaver.
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Doubly-labeled [(3)H, (14)C]tyrosines, [1-(13)C-]tyramine or [2-(14)C]tyramine, administered to the stems of intact Papaver somniferum L. plants, were found to be incorporated into the morphinan alkaloids of the plant with comparable efficiency. (3)H/(14)C ratios of alkaloids from plants fed the
Heillasta gagnagrunnur lækningajurtanna sem studdur er af vísindum
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