4.3.1.24: phenylalanine ammonia-lyase
This is an abbreviated version!
For detailed information about phenylalanine ammonia-lyase, go to the full flat file.
Word Map on EC 4.3.1.24
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4.3.1.24
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phenol
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phenylpropanoids
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polyphenols
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flavonoid
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seedling
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chalcone
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elicitors
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lignin
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cinnamic
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cultivar
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4.3.1.5
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anthocyanins
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jasmonate
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chitinase
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postharvest
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4-hydroxylase
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trans-cinnamic
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defense-related
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p-coumaric
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phytoalexins
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pathogenesis-related
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lignification
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chlorogenic
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phytophthora
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petroselinum
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parsley
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4-coumarate
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phenylketonuria
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crispum
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fresh-cut
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elicitor-induced
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wall-bound
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dihydroflavonol
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elicitor-treated
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4-coumarate:coa
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polyphenoloxidase
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glutinis
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4-reductase
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rhodotorula
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rhodosporidium
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synthesis
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3-o-glucosyltransferase
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d-phenylalanine
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pharmacology
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dehydroalanine
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medicine
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hydroxycinnamoyl
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monolignols
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analysis
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food industry
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drug development
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agriculture
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syringyl
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biotechnology
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lindemuthianum
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glycinea
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matricaria
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cinnamoyl-coa
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nutrition
- 4.3.1.24
- phenol
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phenylpropanoids
- polyphenols
- flavonoid
- seedling
- chalcone
- elicitors
- lignin
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cinnamic
- cultivar
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4.3.1.5
- anthocyanins
- jasmonate
- chitinase
-
postharvest
-
4-hydroxylase
-
trans-cinnamic
-
defense-related
-
p-coumaric
-
phytoalexins
-
pathogenesis-related
-
lignification
-
chlorogenic
- phytophthora
- petroselinum
- parsley
- 4-coumarate
- phenylketonuria
- crispum
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fresh-cut
-
elicitor-induced
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wall-bound
- dihydroflavonol
-
elicitor-treated
-
4-coumarate:coa
- polyphenoloxidase
- glutinis
-
4-reductase
- rhodotorula
- rhodosporidium
- synthesis
- 3-o-glucosyltransferase
- d-phenylalanine
- pharmacology
- dehydroalanine
- medicine
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hydroxycinnamoyl
- monolignols
- analysis
- food industry
- drug development
- agriculture
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syringyl
- biotechnology
- lindemuthianum
- glycinea
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matricaria
- cinnamoyl-coa
- nutrition
Reaction
Synonyms
AtPAL 1, AtPAL 2, AtPAL 3, AtPAL 4, AtPAL-1, AtPAL-2, AtPAL-3, AtPAL-4, AtPAL2, AvPAL, DcPAL1, EC 4.3.1.5, EncP, L-phenylalanine ammonia-lyase, L-phenylalanine-ammonia lyase, LrPAL3, LsPAL1, More, PAL, PAL-CLEA, PAL1, PAL2, PAL3, PAL3a, PAL3b, PAL4, PAL5, PAL6, PALrs1, PcPAL1, Phe ammonia-lyase, phenylalanine ammonia lyase, phenylalanine ammonia-lyase, phenylalanine ammonia-lyase 1, phenylalanine ammonia-lyase 2, phenylalanine ammonia-lyase 3, phenylalanine ammonia-lyase 4, RgPAL, RxPAL, Sb04g026520, SsPAL1, TcPAL, ZmPAL2
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Application
Application on EC 4.3.1.24 - phenylalanine ammonia-lyase
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agriculture
analysis
biotechnology
drug development
food industry
medicine
nutrition
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the enzyme can be used for the development of dietary foods and biotechnological products for patients with phenylketonuria
pharmacology
synthesis
level of enzyme mRNA increases 5 days after the establishment of in vitro callus unions. Enzyme transcription shows a higher level in graft union of incompatible partners and does not result in formation of lignin
agriculture
level of enzyme mRNA increases 5 days after the establishment of in vitro callus unions. Enzyme transcription shows a higher level in graft union of incompatible partners and does not result in formation of lignin
agriculture
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treatment of plants with Pseudmonas sp. increases shoot length and significantly increases the activity of both peroxidase and phenylalanine ammonia-lyase. Treatment may help plants against pathogen invasion by modulating plant peroxidase and phenylalanine ammonia-lyase activities
agriculture
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treatment of plants with Pseudmonas sp. increases shoot length and significantly increases the activity of both peroxidase and phenylalanine ammonia-lyase. Treatment may help plants against pathogen invasion by modulating plant peroxidase and phenylalanine ammonia-lyase activities
agriculture
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treatment of plants with Pseudomonas fluorescens and Pseudomonas aeruginosa induces enzyme synthesis associated with increased synthesis of phenolic compounds such as tannic, gallic, caffeic, chlorogenic and cinnamic acids. Treatment with Sclerotinia slerotiorum does not induce enzyme synthesis
agriculture
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during culture of Morinda citrifolia adventitious roots in different strength, i.e. 0.25, 0.50, 0.75, 1.0, 1.5 and 2.0 of Murashige and Skoog medium supplemented with 5 mg/l indole butyric acid and 30 g/l sucrose, phenylalanine ammonia lyase activity shows a positive correlation in relation to salt strength that leads to an increase in phenol biosynthesis in expense of anthraquinone formation. With the increasing salt strength, root growth and anthraquinone accumulation decrease significantly
agriculture
expression of isoform PAL6 is fruit-specific, and increases during fruit ripening in both cultivars along with anthocyanin accumulation. PAL enzyme activity increases at similar rates in both cultivars at early ripening stages, but at the end of ripening PAL activity diminishes in cultivar Toyonoka while it rises markedly in cultivar Camarosa. PAL activity is higher in internal fruit tissue, showing no correlation with anthocyanin level of the same section in both cultivars. The higher FaPAL6 expression and activity detected in Camarosa may be associated to the enhanced anthocyanin accumulation found in this cultivar
agriculture
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PAL activity is significantly higher in the tissues infected by Glomerella cingulata than in corresponding control and reaches its peak 24 hours after inoculation in the resistant varieties. Defense enzymes PAL, tyrosine ammonia-lyase and polyphenol oxidase prevent the infection by Glomerella cingulata in the resistant tea varieties, in a sequential manner. PAL is induced first, followed by tyrosine ammonia-lyase and than polyphenol oxidase, during biotic stress induced by Glomerella cingulata in tea plants
agriculture
transgenic roots of Coleus blumei, harbouring the Arabidopsis thaliana PAL1 gene, under the control of the CaMV 35S promoter, show disparate phenylalanine ammonia-lyase activities ranging from 67 to 350%, compared to wild-type roots. Growth rates significantly differ, with the lowest in transgenic roots exerting augmented phenylalanine ammonia-lyase activity. Transgenic roots with high phenylalanine ammonia-lyase activity have lower growth rates, lower amounts of total phenolics, rosmarinic acid, i.e. the major phenolic compound in Coleus blumei and chlorogenic acid, but increased amounts of caffeic acid. There is no increase in total phenolics and rosmarinic acid content after feeding transgenic roots with casein enzymatic hydrolysate and L-tyrosine
agriculture
rain shelter treatment may affect phenylalanine lignin monomer synthesis and subsequent cork accumulation by altering the expression or enzyme activities of phenylalanine ammonia lyase (PAL), catechol-O-methyltransferase (COMT), cinnamoyl-CoA reductase (CCR), cinnamyl alcohol dehydrogenase (CAD), peroxidase (POD), and omega-hydroxypalmitate O-feruloyl transferase (HHT1), thus decreasing exocarp russet accumulation in semi-russet pear
agriculture
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PAL activity is significantly higher in the tissues infected by Glomerella cingulata than in corresponding control and reaches its peak 24 hours after inoculation in the resistant varieties. Defense enzymes PAL, tyrosine ammonia-lyase and polyphenol oxidase prevent the infection by Glomerella cingulata in the resistant tea varieties, in a sequential manner. PAL is induced first, followed by tyrosine ammonia-lyase and than polyphenol oxidase, during biotic stress induced by Glomerella cingulata in tea plants
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analysis
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immobilization of phenylalanine ammonia-lyase into gelatin on polyester films to determine phenylalanine in urine for the prediagnosis of phenylketonuria. Immobilized enzyme retaines 100% apparent activity after 30 days and as much as 75% of activity is retained after 2 months. The method is sufficiently sensitive to determine the phenylalanine concentration in phenylketonuric infants' urine
analysis
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an HPLC method for the determination of phenylalanine ammonia-lyase, flavanone 3-hydroxylase and flavonol synthase enzyme activity is proposed. This method is based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis. Optimisation of the method consideres kinetic studies to establish the incubation time to perform the assay. The method is an approach to measure the activities of the three enzymes simultaneously increasing the rapidity, selectivity and sensitivity over other methods
analysis
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an HPLC method for the determination of phenylalanine ammonia-lyase, flavanone 3-hydroxylase and flavonol synthase enzyme activity is proposed. This method is based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis. Optimisation of the method consideres kinetic studies to establish the incubation time to perform the assay. The method is an approach to measure the activities of the three enzymes simultaneously increasing the rapidity, selectivity and sensitivity over other methods
analysis
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an HPLC method for the determination of phenylalanine ammonia-lyase, flavanone 3-hydroxylase and flavonol synthase enzyme activity is proposed. This method is based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis. Optimisation of the method consideres kinetic studies to establish the incubation time to perform the assay. The method is an approach to measure the activities of the three enzymes simultaneously increasing the rapidity, selectivity and sensitivity over other methods
analysis
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an HPLC method for the determination of phenylalanine ammonia-lyase, flavanone 3-hydroxylase and flavonol synthase enzyme activity is proposed. This method is based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis. Optimisation of the method consideres kinetic studies to establish the incubation time to perform the assay. The method is an approach to measure the activities of the three enzymes simultaneously increasing the rapidity, selectivity and sensitivity over other methods
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compared to the free enzyme, the PAL-CLEA exhibit increased stability of the enzyme against various deactivating conditions such as pH, temperature, denaturants, and organic solvents and show higher storage stability than its soluble counterpart. Additionally, PAL-CLEAs can be recycled at least for 12 consecutive batch reactions without dramatic activity loss, increases the commercial potential of PAL for synthesis of L-phenylalanine
biotechnology
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the enzyme can be used for the development of dietary foods and biotechnological products for patients with phenylketonuria
AtPAL2 is a very good catalyst for the formation of 3-fluoro-L-phenylalanine, 4-fluoro-L-phenylalanine and 2-chloro-L-phenylalanine. Such noncanonical amino acids are valuable building blocks for the formation of various drug molecules
drug development
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the enzyme can reduce the level of L-Phe in the blood and is a prospective drug for the treatment of phenylketonuria
drug development
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the enzyme can reduce the level of L-Phe in the blood and is a prospective drug for the treatment of phenylketonuria
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the enzyme can be used for the development of dietary foods and biotechnological products for patients with phenylketonuria
food industry
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the enzyme from Cyathobasis fruticulosa is a potential candidate for serial production of dietary food and biotechnological products
use of enzyme for substitution treatment of human phenylketonuria. Identification of B and T cell epitopes on the enzyme protein and covering of the immunogenic regions
medicine
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use of enzyme in therapy of human phenylketonuria. Preparation of microcapsules containing emulsified enzyme. Emulsification of enzyme solution with water-saturated ether causes no loss in activity but results in loss of protein content in the aqueous phase due to specific loss of impurities in the protein sample. Emulsification of enzyme solution with ether/ethanol mixture results in a 50% decrase in activity. Hydroxypropyl-gamma-cyclodextrin and hydroxypropyl-beta-cyclodextrin protect against emulsion mediated loss in activity
medicine
PAL activity is able to effect a reduction in phenylalanine levels and hence provide the basis of a unique therapy for human hyperphenylalaninemic patients
medicine
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the enzyme can be used as oral therapeutic, in an encapsulated form, in phenylketonuria/hyperphenylalaninemia
medicine
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enzyme substitution therapy for the treatment of phenylketonuria
medicine
enzyme substitution therapy for the treatment of phenylketonuria
medicine
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enzyme substitution therapy with the phenylalanine ammonia lyase is a new approach to the treatment of patients with phenylketonuria
medicine
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the enzyme can reduce the level of L-Phe in the blood and is a prospective drug for the treatment of phenylketonuria
medicine
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the shift of the pH-optimum from pH 8.5 for the wild-type enzyme to pH 7.5 with 30% higher specific activity than that of the wild-type enzyme, the prolonged half-life of the mutant enzyme at 70°C, the higher resistance to a low pH of 3.5 and protease make the mutant enzyme E75L a candidate for oral medicine of phenylketonuria
medicine
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the enzyme can reduce the level of L-Phe in the blood and is a prospective drug for the treatment of phenylketonuria
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medicine
Trichormus variabilis FACHB-82
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the shift of the pH-optimum from pH 8.5 for the wild-type enzyme to pH 7.5 with 30% higher specific activity than that of the wild-type enzyme, the prolonged half-life of the mutant enzyme at 70°C, the higher resistance to a low pH of 3.5 and protease make the mutant enzyme E75L a candidate for oral medicine of phenylketonuria
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the ability of PAL to catalyze the conversion of L-Phe into nontoxic compounds in the absence of additional cofactors leads to its use as a therapeutic agent for the treatment of phenylketonuria
pharmacology
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enzyme substitution therapy for the treatment of phenylketonuria
pharmacology
enzyme substitution therapy for the treatment of phenylketonuria
pharmacology
-
enzyme substitution therapy with the phenylalanine ammonia lyase is a new approach to the treatment of patients with phenylketonuria
pharmacology
-
the enzyme can reduce the level of L-Phe in the blood and is a prospective drug for the treatment of phenylketonuria
pharmacology
the enzyme is specifically advantageous for the production of the hypertension drug 2-chloro-L-phenylalanine
pharmacology
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the shift of the pH-optimum from pH 8.5 for the wild-type enzyme to pH 7.5 with 30% higher specific activity than that of the wild-type enzyme, the prolonged half-life of the mutant enzyme at 70°C, the higher resistance to a low pH of 3.5 and protease make the mutant enzyme E75L a candidate for oral medicine of phenylketonuria
pharmacology
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the enzyme can reduce the level of L-Phe in the blood and is a prospective drug for the treatment of phenylketonuria
-
pharmacology
Trichormus variabilis FACHB-82
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the shift of the pH-optimum from pH 8.5 for the wild-type enzyme to pH 7.5 with 30% higher specific activity than that of the wild-type enzyme, the prolonged half-life of the mutant enzyme at 70°C, the higher resistance to a low pH of 3.5 and protease make the mutant enzyme E75L a candidate for oral medicine of phenylketonuria
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production of L-phenylalanine, which is used in the manufacture of the artificial sweetener aspartame and in parenteral nutrition, it is also used as a building block for the synthesis of the macrolide antibiotic rutamycin B
synthesis
Rhodococcus rubra
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production of L-phenylalanine, which is used in the manufacture of the artificial sweetener aspartame and in parenteral nutrition, it is also used as a building block for the synthesis of the macrolide antibiotic rutamycin B
synthesis
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use of enzyme for production of enantiopure D- and L-heteroaryl-2-alanines, i.e. R- and S-2-amino-3-(heteroaryl)propanoic acids
synthesis
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phenylalanine ammonia-lyase's reverse reaction is exploited for the commercial production of optically pure L-phenylalanine from trans-cinnamic acid
synthesis
the enzyme is involved in and useful for production salidroside, an effective adaptogenic drug from the medicinal plant Rhodiola sachalinensis
synthesis
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the enzyme is useful for an economic way for biosynthesis of 15NL-phenylalanine, yield and purity of 15NL-phenylalanine reach 71% and 99.3%, respectively
synthesis
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heterologous expression of enzyme in Streptomyces lividans. After 4 days of cultivation using glucose as carbon source, the maximal level of cinnamic acid reaches 210 mg/l. When glycerol is used as carbon source az 30 g/l, the maximal level of produced cinnamic acid reaches 450 mg/l. Using raw starch, xylose or xylan as carbon source, the maximal level of cinnamic acid reaches 460, 300, and 130 mg/l, respectively
synthesis
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improvement of recombinant phenylalanine ammonia-lyase stability in Escherichia coli during the enzymatic methods of L-phenylalanine production. The optimum values for testing variables are 13.04 mM glycerol, 1.87 mM sucrose, 4.09 mM DTT, and 69 mM Mg2+. The maximum phenylalanine ammonia-lyase activity is retained as 67.73 units/g after three successive cycles of bioconversion. In comparison to initial phenylalanine ammonia-lyase activity, the loss of phenylalanine ammonia-lyase activity was only 22%. Phenylalanine ammonia-lyase activity is enhanced about 23% in comparison to the control
synthesis
AtPAL2 is a very good catalyst for the formation of 3-fluoro-L-phenylalanine, 4-fluoro-L-phenylalanine and 2-chloro-L-phenylalanine. Such noncanonical amino acids are valuable building blocks for the formation of various drug molecules
synthesis
reconstructed phenylpropanoid pathway in engineered Escherichia coli or Saccharomyces cerevisiae leads to the biosynthesis of a wide range of phenylpropanoid-derived compounds, including (2S)-pinocembrin, (2S)-naringenin, p-hydroxystyrene, p-coumarate, trans-cinnamic acid
synthesis
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reconstructed phenylpropanoid pathway in engineered Escherichia coli or Saccharomyces cerevisiae leads to the biosynthesis of a wide range of phenylpropanoid-derived compounds, including dicinnamoylmethane, 6-fluoro-dicinnamoylmethane, 6,6'-difluoro-dicinnamoylmethane or pinosylvin
synthesis
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reconstructed phenylpropanoid pathway in engineered Escherichia coli or Saccharomyces cerevisiae leads to the biosynthesis of a wide range of phenylpropanoid-derived compounds, including trans-cinnamic acid
synthesis
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reconstructed phenylpropanoid pathway in engineered Escherichia coli or Saccharomyces cerevisiae leads to the biosynthesis of a wide range of phenylpropanoid-derived compounds, including trans-cinnamic acid, (2RS)-pinocembrin, styrene, pinosylvin or (2S)-naringenin
synthesis
reconstructed phenylpropanoid pathway in engineered Escherichia coli or Saccharomyces cerevisiae leads to the biosynthesis of a wide range of phenylpropanoid-derived compounds, including trans-cinnamic acid, p-coumaric acid, (2RS)-pinocembrin, (2RS)-naringenin, trans-resveratrol, pinosylvin, genistein
synthesis
synthesis of analogues of L-phenylalanine, that are incorporated as pharmacophores in several peptidomimetic drug molecules and are therefore of particular interest to the fine chemical industry. Engineering of phenylalanine ammonia lyase from Rhodotorula graminis and identification of variants with very high levels of activity towards a panel of substituted cinnamic acids including; 4-bromo-, 3-bromo-, 4-fluoro-, 3-fluoro- and 3-nitro-cinnamic acid. Optimisation studies for use of one of these variants in the preparative synthesis of related variants of L-phenylalanine. Identification of variants used in a preparative scale biotransformation resulting in a 94% conversion to L-4-Br-phenylalanine (more than 99% enantiomeric excess)
synthesis
synthesis of substituted D-phenylalanines in high yield and excellent optical purity, starting from inexpensive cinnamic acids, is achieved with a one-pot approach by coupling phenylalanine ammonia lyase amination with a chemoenzymatic deracemization (based on stereoselective oxidation and nonselective reduction). A simple high-throughput solid-phase screening method is developed to identify phenylalanine ammonia lyases with higher rates of formation of non-natural D-phenylalanines. The best variants are exploited in the chemoenzymatic cascade, thus increasing the yield and enantiomeric excess value of the D-configured product
synthesis
the enzyme is specifically advantageous for the production of 2-chloro-L-phenylalanine, an important intermediate for the synthesis of angiotensin 1-converting enzyme inhibitors
synthesis
the recombinant ZmPAL2 is a good candidate for the production of trans-cinnamic acid. The recombinant ZmPAL2 can effectively catalyze L-phenylalanine to trans-cinnamic acid, and the trans-cinnamic acid concentration can reach up to 5 g/l
synthesis
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the enzyme is useful for an economic way for biosynthesis of 15NL-phenylalanine, yield and purity of 15NL-phenylalanine reach 71% and 99.3%, respectively
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synthesis
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phenylalanine ammonia-lyase's reverse reaction is exploited for the commercial production of optically pure L-phenylalanine from trans-cinnamic acid
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