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Elicitor-Induced L-Tyrosine Decarboxylase from Plant Cell Suspension Cultures: II. Partial Characterization :  
Institute ofBiotechnology, ETH Hönggerberg, CH-8093 Zurich, Switzerland.ORCID iD: 0000-0001-8899-5046
1988 (English)In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 88, p. 52-55Article in journal (Refereed) Published
Abstract [en]

Properties of purified L-tyrosine decarboxylase (EC 4.1.1.25) fromelicitor-induced cell suspension cultures of Eschscholtzia californicaCham. and Thalictrum rugosum Ait. are described. L-Tyrosine decarboxylaseis a dimeric enzyme with a molecular weight of 112,600 ± 600daltons. The isoelectric point was estimated to be at pH 5.2 and pH 5.4for the enzyme from E. californica and T. rugosum, respectively. Thepurified enzymes were stabilized in the presence of pyridoxal-5-phosphate.Optimum pH for the enzyme from both plants was found to be8.4. 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-decarboxylasefor 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 inhibitedby the phenylalanine analogue L-a-aminooxy-#-phenylpropionate andlargely unaffected by D,L-a-monofluoromethyl-3,4-dihydroxyphenylalanineand a-difluoromethyltyrosine. 

Place, publisher, year, edition, pages
1988. Vol. 88, p. 52-55
National Category
Biochemistry and Molecular Biology
Research subject
Natural Science, Biochemistry
Identifiers
URN: urn:nbn:se:lnu:diva-603OAI: oai:DiVA.org:lnu-603DiVA, id: diva2:307333
Available from: 2010-04-01 Created: 2010-04-01 Last updated: 2017-12-12Bibliographically approved

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Brodelius, Peter

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