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l phenylalanine/kartul
Link salvestatakse lõikelauale
Leht 1 alates 26 tulemused
[Role of L-phenylalanine ammonia lyase in the induced resistance and susceptibility of potato plants].
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Biogenic elicitors (chitosan and its complex with salicylic acid) and an immunosuppressor (laminarin) were shown to increase the activity of L-phenylalanine ammonia lyase (EC 4.3.1.5) and protein synthesis in potato tubers. Laminarin did not decrease L-phenylalanine ammonia lyase activity. It is
Density labelling studies of the photocontrol of L-phenylalanine ammonia-lyase in discs of potato (Solanum tuberosum) tuber parenchyme.
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The photocontrol of L-phenylalanine ammonia-lyase (EC 4.3.1.5) activity in discs of potato (Solanum tuberosum) tuber parenchyme has been investigated by density labelling with 2H from 2H2O. Labelling of enzyme was measured by analysis of the equilibrium distribution of enzyme activity in CsCl
Formation of p-coumaric acid and o-coumaric acid from L-phenylalanine by microsomal membrane fractions from potato: Evidence of membrane-bound enzyme complexes.
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The enzymes described here are the membrane-bound L-phenylalanine ammonia-lyase and cinnamate hydroxylase. Microsomes prepared from tubers of Solanum tuberosum L. are capable of converting L-phenylalanine into both o- and p-coumaric acid. Three microsomal fractions obtained by density gradient
L-phenylalanine ammonia-lyase (maize, potato, and Rhodotorula glutinis). Studies of the prosthetic group with nitromethane.
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Highly purified enzyme (EC 4.1.3.5) from Rhodotorula glutinis was shown by sodium dodecyl sulfate gel electrophoresis to have subunits which if not identical are closely similar in molecular weight. Like the enzyme from maize and potato [Havir, E. A., and Hanson, K. R. (1973), Biochemistry 12, 1583]
L-Phenylalanine ammonia-lyase (maize, potato, and Rhodotorula glutinis) Explaining the kinetic effects of substrate modification by linear free-energy relationships.
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L-phenylalanine ammonia-lyase (maize and potato). Evidence that the enzyme is composed of four subunits.
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L-phenylalanine ammonia-lyase. II. Mechanism and kinetic properties of the enzyme from potato tubers.
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L-Phenylalanine ammonia-lyase. I. Purification and molecular size of the enzyme from potato tubers.
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Estimation of metabolic fluxes, expression levels and metabolite dynamics of a secondary metabolic pathway in potato using label pulse-feeding experiments combined with kinetic network modelling and simulation.
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In this paper we present a method that allows dynamic flux analysis without a priori kinetic knowledge. This method was developed and validated using the pulse-feeding experimental data obtained in our previous study (Matsuda et al., 2005), in which incorporation of exogenously applied
l-Phenylalanine Ammonia-Lyase (Maize): Evidence for a Common Catalytic Site for l-Phenylalanine and l-Tyrosine.
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l-Phenylalanine ammonia-lyase (E.C. 4.3.1.5) from maize is active with l-tyrosine and l-phenylalanine and exhibits atypical Michaelis-Menten kinetics with both substrates. With phenylalanine as a substrate, the pH optimum is 8.7 and with tyrosine, 7.7. The estimated Km at high substrate
1-Amino-2-phenylethylphosphonic acid: an inhibitor of L-phenylalanine ammonia-lyase in vitro.
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L(-)-, and D(+)-enantiomers of 1-amino-2-phenylethylphosphonic acid (PheP), a phosphonic analogue of phenylalanine, inhibit the activity of L-phenylalanine ammonia-lyase (EC 4.3.1.5) of potato tuber tissue in vitro. The apparent type of inhibition depends on concentration of PheP; as the
Purification and properties of phenylalanine ammonia-lyase in cut-injured sweet potato.
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L-Phenylalanine ammonia-lyase (PAL) activity was developed in response to cut injury in sweet potato root tissue. The enzyme was purified from tissue incubated for 1 day after slicing by ammonium sulfate fractionation, column chromatographies on L-phenylalanyl Sepharose 4B, phosphocellulose.
Nitrogen recycling during phenylpropanoid metabolism in sweet potato tubers.
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In the first step of the phenylpropanoid metabolic pathway, L-phenylalanine (L-Phe) is deaminated to form E-cinnamate, in a conversion catalyzed by phenylalanine ammonia-lyase (PAL; EC 4.3.1.5). The metabolic fate of the ammonium ion (NH4+) produced in this reaction was investigated in sweet potato
Regulation of Bud Rest in Tubers of Potato, Solanum tuberosum L: VI. Biochemical Changes Induced in Excised Potato Buds by Gibberellic Acid.
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The rest period of the potato tuber was studied in relation to certain biochemical changes that are induced by gibberellic acid (GA(3)). The concentration of reducing sugars in excised plugs with buds treated with 10(-4)m GA(3) decreased in the first 4 hours after treatment and then rapidly
Beta-1,3-glucooligosaccharide induced activation of four enzymes responsible for N-p-coumaroyloctopamine biosynthesis in potato (Solanum tuberosum cv.) tuber tissue.
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Potato tuber disks, when treated with laminarin, a beta-1,3-glucooligosaccharide from Laminaria digitata, accumulate a hydroxycinnamoyl amide compound, N-p-coumaroyloctopamine (p-CO). The biosynthesis of p-CO was investigated by feeding experiments, in order to show that the precursors of
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