Dopa decarboxylase in Cytisus scoparius

Tocher, R. D.; Tocher, C. S.

doi:10.1016/0031-9422(72)85014-3

Cited by 32 publications

(9 citation statements)

References 7 publications

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“…For example, TDC from Catharanthus roseus is highly specific for Trp (Noé et al, 1984) and DODC from Cytisus scoparius can only decarboxylate DOPA (Tocher and Tocher, 1972). Other plant species, such as Syringa vulgaris, Thalictrum rugosum, and Eschscholtzia californica, appear to have dual TyDC/DODC activities that accept both Tyr and DOPA as substrates, but not Trp or Phe (Marques and Brodelius, 1988).…”

Section: Discussionmentioning

confidence: 99%

Molecular Analysis of a New Member of the Opium Poppy Tyrosine/3,4-Dihydroxyphenylalanine Decarboxylase Gene Family

et al. 1996

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Section: Discussionmentioning

confidence: 99%

Molecular Analysis of a New Member of the Opium Poppy Tyrosine/3,4-Dihydroxyphenylalanine Decarboxylase Gene Family

et al. 1996

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“…However, only very limited information about these enzymes has been published (2,7,9,14,15 A sample (0.5 ml) ofpurified TDC was desalted by centrifugation through a 5 ml Sephadex G-25 column equilibrated in 25 mM bis-Tris-HCI (pH 6.7) and applied to the Mono P column, which had been equilibrated with the same buffer. Elution was performed with a decreasing pH gradient (30 ml) using a 10-fold diluted Polybuffer 74-HCI (pH 4.9).…”

Section: Introductionmentioning

confidence: 99%

Elicitor-Induced l-Tyrosine Decarboxylase from Plant Cell Suspension Cultures

Marques¹,

Brodelius²

1988

Plant Physiol.

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Properties of purified L-tyrosine decarboxylase (EC 4.1.1.25) from elicitor-induced cell suspension cultures of Eschscholtzia californica Cham. and Thalictrum rugosum Ait. are described. L-Tyrosine decarboxylase is a dimeric enzyme with a molecular weight of 112,600 ± 600 daltons. The isoelectric point was estimated to be at pH 5.2 and pH 5.4for the enzyme from E. californica and T. rugosum, respectively. The purified enzymes were stabilized in the presence of pyridoxal-5-phosphate. Optimum pH for the enzyme from both plants was found to be 8.4. Enzyme activity was dependent on exogeneously supplied pyridoxal-5-phosphate. The enzyme decarboxylated L-tyrosine and L-,a-3,4-dihydroxyphenylalanine but was inactive toward L-phenylalanine and Ltryptophan. Apparent Km values of Eschscholtzia-and Thalictrum-decarboxylase for L-tyrosine were 0.25 ± 0.03 and 0.27 ± 0.04 millimolar, respectively. Similar affinities were found for L-3,4-dihydroxyphenylalanine. Eschscholtzia L-tyrosine decarboxylase was strongly inhibited by the phenylalanine analogue L-a-aminooxy-#-phenylpropionate and largely unaffected by D,L-a-monofluoromethyl-3,4-dihydroxyphenylalanine and a-difluoromethyltyrosine.An enhanced biosynthesis of berberine in cell suspension cultures of Thalictrum rugosum Ait. was achieved by treating the cells with a yeast carbohydrate elicitor (6). This increased product formation followed an increase of TDC2 (EC 4.1.1.25) activity (8). These findings, coupled with results from feeding experiments with radioactive labeled tyrosine (8), indicate that TDC might control the branching point between primary and secondary metabolisms. Furthermore, the synthesis ofdopamine (one of the direct precursors of norlaudanosoline) from tyrosine during the initial steps of alkaloid biosynthesis is not clear. Two possible routes could be considered: first, hydroxylation of tyrosine to DOPA followed by a decarboxylation of DOPA to dopamine; second, decarboxylation of tyrosine to tyramine and subsequent hydroxylation of tyramine to dopamine.Data about the catalytic and molecular properties of plant DOPA and tyrosine decarboxylase would be valuable in establishing the function of these enzymes in alkaloid biosynthesis. However, only very limited information about these enzymes has been published (2,7,9,14,15 A sample (0.5 ml) ofpurified TDC was desalted by centrifugation through a 5 ml Sephadex G-25 column equilibrated in 25 mM bis-Tris-HCI (pH 6.7) and applied to the Mono P column, which had been equilibrated with the same buffer. Elution was performed with a decreasing pH gradient (30 ml) using a 10-fold diluted Polybuffer 74-HCI (pH 4.9). The pI values were also estimated by isoelectric focusing. IEF was carried out on tubes as described (5) using ampholine pH 4 to 6. 52 www.plantphysiol.org on May 11, 2018 -Published by Downloaded from

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“…96 The similar biosynthetic pathways of cathecholamines have been described both in plants and animals (Figure 3). 97 In plants, it is produced in the cytoplasm through the decarboxylation of glutamate. 98 Dopamine levels ranged from 80-560 mg/100 g in peel and 2.5-10 mg/100 g in pulp, even in ripened bananas.…”

Section: Catecholamine Signaling In Plantsmentioning

confidence: 99%

New insights on neurotransmitters signaling mechanisms in plants

Ramakrishna

Bhatla

2020

Plant Signaling & Behavior

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Neurotransmitters (NTs) such as acetylcholine, biogenic amines (dopamine, noradrenaline, adrenaline, histamine), indoleamines [(melatonin (MEL) & serotonin (SER)] have been found not only in mammalians, but also in diverse living organisms-microorganisms to plants. These NTs have emerged as potential signaling molecules in the last decade of investigations in various plant systems. NTs have been found to play important roles in plant life including-organogenesis, flowering, ion permeability, photosynthesis, circadian rhythm, reproduction, fruit ripening, photomorphogenesis, adaptation to environmental changes. This review will provide an overview of recent advancements on the physiological and molecular mechanism of NTs in plants. Moreover, molecular crosstalk of SER and MEL with various biomolecules is also discussed. The study of these NTs may serve as new understanding of the mechanisms of signal transmission and cell sensing in plants subjected to various environmental stimulus.

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Dopa decarboxylase in Cytisus scoparius

Cited by 32 publications

References 7 publications

Molecular Analysis of a New Member of the Opium Poppy Tyrosine/3,4-Dihydroxyphenylalanine Decarboxylase Gene Family

Molecular Analysis of a New Member of the Opium Poppy Tyrosine/3,4-Dihydroxyphenylalanine Decarboxylase Gene Family

Elicitor-Induced l-Tyrosine Decarboxylase from Plant Cell Suspension Cultures

New insights on neurotransmitters signaling mechanisms in plants

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