Role of phenylalanine in the biosynthesis of flavonoids and cinnamic acids in strawberry leaf disks
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Cinnamic acid
Phenylalanine ammonia-lyase
Limiting
Cinnamic acid
Phenylalanine ammonia-lyase
Chlorogenic Acid
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Several carboxylic, phosphonic, phosphinic, boronic and nitro analogues of ( £ )-cinnamic acid were synthesized. These and other compounds related to (E)-cinnamic acid were evaluated as potential inhibitors of both phenylalanine ammonia-lyase and of anthocyanin biosynthesis in buckwheat. The most potent inhibition was found for 3-phenylprop-2-ynoic acid (21), however its K i is comparable to K M . The molecular modelling of the interaction of (E)-cinnamic acid (1) and 21 with PAL model suggests some similarities in the binding mode of both compounds.
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Phenylalanine ammonia-lyase
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Abstract The phosphonic analogue of ʟ-phenylalanine, (R)-(1-amino-2-phenylethyl)phosphonic acid (APEP), inhibits buckwheat phenylalanine ammonia-lyase (PAL) competitively with a K i value of 1.5 μM. The K i value for the (S)-enantiomer is 11.6 μM. The corresponding values for the enantiomers of the phosphonous analogue are 35 and 205 μm , respectively. APEP inhibits the light-induced synthesis of anthocyanin in hypocotyls of etiolated buckwheat seedlings and causes a specific increase in the endogenous phenylalanine concentration in buckwheat hypocotyls as well as other plant tissues. Kohlrabi seedlings develop normally in the presence of APEP, while their anthocyanin content is greatly reduced. These results indicate that APEP inhibits PAL in vivo.
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Phenylalanine ammonia-lyase
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The conversion of trans-cinnamic acid to phenylalanine using phenylalanine ammonia lyase (PAL) was examined. The optimum concentration of trans-cinnamic acid for the reaction was observed at 100 mM in cells and at 20 mM in cell free extracts, respectively. The production of L-phenylalanine was increased in both experiments as the concentration of ammonia was increased up to 10 M. The optimal pHs for the maximal conversion of trans-cinnamic acid to L-phenylalanine were 9.5 and 9.0 in experiments carried out with cells and with cell free extracts, respectively.
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Cinnamic acid
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L-phenylalanine is an important amino acid in commercial production of food industry and medicine nowaday. The biotransformations of trans-cinnamic acid to L-phenylalanine using phenylalanine ammonia- lyase(PAL) is in the front of research and development now.This article reviews the research progress in molecular biology of Phenylalanine ammonia-lyase (PAL) as an important enzyme for production of L-phenylalanine. Ref 43
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Abstract The ability of l ‐phenylalanine ammonia‐lyase (E.C. 4.3.1.5) to metabolize dl ‐ m ‐, dl ‐ o ‐ and dl ‐ p ‐fluorophenylalanine in Avena sativa has been examined. Although all three amino acid analogues served as substrates for this enzyme, there was a marked difference in the behavior of the meta isomer from that of the para and ortho species. The Michaelis constant for the meta analogue was similar to that obtained for the natural substrate, l ‐phenylalanine, but distinct from the kinetic data for the para and ortho isomers. In addition, in vivo analyses demonstrated that both l ‐phenylalanine and the meta‐fluoro‐derivative served to protect against chlorogenic acid loss, whereas previous studies have shown that the para and ortho species depressed levels of this phenolic derivative. Finally, treatment of coleoptile apices with either the meta isomer or l ‐phenylalanine reversed dl ‐ p ‐fluorophenylalanine stimulated growth and attendant reduction in chlorogenic acid content. These findings provide further clarification of the effects of fluorophenylalanines upon l ‐phenylalanine ammonia‐lyase mediated biosynthesis of low molecular weight phenols in Avena .
Phenylalanine ammonia-lyase
Avena
Phenylacetic acid
Chlorogenic Acid
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Phenylalanine ammonia-lyase
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In vivo and in vitro experiments were performed in order to study the regulatory role of trans- cinnamic acid and its hydroxylated derivatives (p-coumaric acid, caffeic acid) on the deamination of phenylalanine catalyzed by PAL (EC 4.3.1.5). Trans-cinnamic acid inhibits growth and reduces the content of soluble proteins of anthocyanin-containing carrot cells grown in suspension. There is strong evidence from the polysomal patterns and from the effect of trans-cinnamic acid on protein synthesis in vitro that protein synthesis is inhibited. The kinetic data of PAL clearly demonstrate that trans-cinnamic acid inhibits the enzyme by a noncompetitive mechanism. On the contrary, ʟ-α-aminooxy-β-phenylpropionic acid (ʟ-AOPP), a competitive inhibitor of PAL, does not affect protein metabolism.
Cinnamic acid
Phenylalanine ammonia-lyase
Daucus carota
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Phenylpropanoid pathway 생성물질은 식물의 self-defense에 관계하며 이러한 물질들은 UV뿐 아니라 wounding, pathogen과 같은 environmental stress에 의해 생성되는 것으로 알려져 있다. 벼에서 PAL mRNA 는 UV 조사 후 12시간에서 48시간까지는 증가하였으나 48시간부터 60시간까지는 점점 줄어드는 경향을 보였다. 한편 PAL의 활성은 UV 조사 후 24시간에서 가장 높았지만 상처에 의해서는 PAL의 활성이 벼에서는 증가하지 않았다. 그러나 고추에서는 UV조사와 상처를 준 후 24시간과 10시간에서 각각 높은 활성을 나타내었다. 벼와 고추 모두 cinnamic acid 4-hydroxylase의 활성은 상처를 준 후 12시간에서 증가하였지만 UV 조사는 C4H 활성에 영향을 주지 않았다. 이러한 결과로 볼 때 벼와 고추에서는 UV 조사와 상처가 모두 PAL, C4H 효소활성에 영향을 주는 것으로 나타났다.
Phenylalanine ammonia-lyase
Cinnamic acid
Phenylpropanoid
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