The characterization of phenylalanine ammonia-lyase from several plant species

Jangaard, N. O.

doi:10.1016/0031-9422(74)85086-7

Cited by 43 publications

(23 citation statements)

References 17 publications

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“…As indicated by several earlier reports (Neish, 1961;Young et al, 1966;Havir et al, 1971;Jangaard, 1974), PAL, not only from maize but from monocot plants in general, has TAL activity. This implies that these plants can, in principle, produce p-coumaric acid from both Phe and Tyr (Fig.…”

Section: Potential Physiological Implicationsmentioning

confidence: 71%

“…Results from severa1 studies (Neish, 1961; Young et al, 1966;Havir et al, 1971;Jangaard, 1974) indicated that the enzyme from monocots utilizes Tyr (TAL activity) in addition to Phe, whereas the enzyme from dicots utilizes only Phe efficiently. The four homotetrameric parsley PAL (Havir et al, 1971), indicating that PAL from maize also has TAL activity.…”

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confidence: 99%

“…The occurrence of heteromers is likely but has as yet not been proven. On the other hand, apparent charge isoforms of a poplar PAL were recovered from insect cell cultures producing the protein from a baculovirus expression vector containing the respective cDNA (McKegney et al, 1996).Results from severa1 studies (Neish, 1961; Young et al, 1966;Havir et al, 1971;Jangaard, 1974) indicated that the enzyme from monocots utilizes Tyr (TAL activity) in addition to Phe, whereas the enzyme from dicots utilizes only Phe efficiently. The four homotetrameric parsley PAL (Havir et al, 1971), indicating that PAL from maize also has TAL activity.…”

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Maize Phenylalanine Ammonia-Lyase Has Tyrosine Ammonia-Lyase Activity

et al. 1997

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A full-length cDNA encoding phenylalanine ammonia-lyase (PAL) from Zea mays L. was isolated and the coding region was expressed in Escherichia coli as a C-terminal fusion to glutathione S-transferase. After purification by glutathione-Sepharose chromatography, the glutathione S-transferase moiety was cleaved off and the resulting PAL enzyme analyzed. In contrast to PAL from dicots, this maize PAL isozyme catalyzed the deamination of both i-phenylalanine (PAL activity) and i-tyrosine (tyrosine ammonialyase activity). These results provide unequivocal proof that PAL and tyrosine ammonia-lyase activities reside in the same polypeptide. In spite of large differences in the Michaelis constant and turnover number of the two activities, their catalytic efficiencies are very similar. Also, both activities have the same p H and temperature optima. These results imply that maize can produce p-coumaric acid from both phenylalanine and tyrosine.PAL (EC 4.3.1.5) catalyzes the elimination of ammonia from L-Phe to yield (E)-cinnamic acid ( Fig. 1) (Koukol and Com, 1961), the first step in the phenylpropanoid pathway (for reviews, see Hahlbrock and Scheel, 1989;Dixon and Paiva, 1995;Whetten and Sederoff, 1995;Campbell and Sederoff, 1996). PAL activity has been found in some fungi and in a11 higher plants analyzed but not in animals. Because of the central function of PAL at a branch point of metabolism, this enzyme is one of the best studied in plants; the same is true for its corresponding gene(s).In a11 plants analyzed, PAL has been shown to occur as a tetramer, and multiple forms have often been isolated (Bolwell et al., 1985). PAL multigene families, such as those in tomato (Lycopersicon esculentum; Lee et al., 1992), parsley (Petroselinum crispum; Appert et al., 1994), or Arabidopsis thaliana (Wanner et al., 1995), explain at least in part these different forms. The occurrence of heteromers is likely but has as yet not been proven. On the other hand, apparent charge isoforms of a poplar PAL were recovered from insect cell cultures producing the protein from a baculovirus expression vector containing the respective cDNA (McKegney et al., 1996).Results from severa1 studies (Neish, 1961; Young et al., 1966;Havir et al., 1971;Jangaard, 1974) indicated that the enzyme from monocots utilizes Tyr (TAL activity) in addition to Phe, whereas the enzyme from dicots utilizes only Phe efficiently. The four homotetrameric parsley PAL (Havir et al., 1971), indicating that PAL from maize also has TAL activity. However, the uncertainty remains that a protein with TAL activity copurifies with PAL activity. Referring to the heterologous expression of parsley PAL cDNAs (Schulz et al., 1989; Appert et al., 1994), Whetten and Sederoff (1995) stated: "The same experiment could be performed with maize cDNA to test for PAL and TAL activities in the same polypeptide." This is exactly the experiment we report here. Expression of a PAL-specific cDNA from maize in Escherichia coli provided the ultimate proof that PAL and TAL activities reside in ...

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Section: Potential Physiological Implicationsmentioning

confidence: 71%

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confidence: 99%

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Maize Phenylalanine Ammonia-Lyase Has Tyrosine Ammonia-Lyase Activity

et al. 1997

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“…PAL activity was assayed by the modified method of Jangaard (1974). The amount of cinnamic acid produced in the assay mixture was determined by measuring the absorbance at 275 nm using a JENWAY 6305 UV/Vis spectrophotometer.…”

Section: Establishment and Growth Of Tissue Culturesmentioning

confidence: 99%

Induction of Phenolic Compounds in Wheat (Triticum aestivum L.) Tissue Cultures by Streptomycin

Hassan

2007

Zeitschrift Für Naturforschung C

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The tissue cultures of wheat (Triticum aestivum L.) were induced from the mature embryos (explants) of the dry grains and grown on MS medium containing kinetin (0.1 mg/l) and 2,4 D (1.0 mg/l). The cultures were incubated for two weeks at (25 ð 2) ∞C under a light/dark regime (16 h light daily). The formed calli were subcultured at the beginning of the stationary growth phase (15 days) with fresh MS medium containing 0, 5, 10, 25, 50, 100, 150 mg/l streptomycin elicitor and maintained for two weeks for three subcultures. A significant increase in phenylalanine ammonia lyase (PAL) activity coincided with the increase of the total phenolic compounds after elicitation with streptomycin. Maximum induction was recorded during the first two weeks, then gradually declined during the rest of the experimental period, but the values attained were still markedly higher than that of the control. The endogenous cinnamic acid content was also increased significantly with the increase in PAL activity making about 2Ð18% of the total phenolic acids. The growth and accumulation of phenolic compounds were inversely related. However, accumulation of phenolic compounds became limited for growth of wheat tissue culture especially during the long term cultivation.

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“…O f all plants, only grasses usually show an activity of L-tyrosine am m onia-lyase (TAL) comparable with that of L-phenylalanine am m onialyase (PAL) [2][3][4][5]. Thus L-tyrosine may be an ad d i tional true precursor of phenolics in the Gramineae, but not in other plants.…”

Section: Introductionmentioning

confidence: 99%