1.4.1.20: phenylalanine dehydrogenase
This is an abbreviated version!
For detailed information about phenylalanine dehydrogenase, go to the full flat file.
Word Map on EC 1.4.1.20
Reaction
Synonyms
dehydrogenase, phenylalanine, L-PheDH, L-phenylalanine dehydrogenase, L-phenylalanine:NAD+ oxidoreductase, deaminating, PDH, PHD, PheDH, phenylalanine dehydrogenase, recombinant PheDH, recombinant phenylalanine dehydrogenase
ECTree
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Application on EC 1.4.1.20 - phenylalanine dehydrogenase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
biotechnology
diagnostics
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the immobilized enzyme is useful for establishing an analytical spectrophotometric determination method of L-Phe in the diagnostics of phenyketonuria, an inborn error of amino acid metabolism in which the conversion of L-phenylalanine to L-tyrosine is impaired and can cause profound mental retardation if not detected and treated soon after birth. Early quantitative measurement of the plasma L-Phe is essential for the diagnosis of phenylketonuria and the control of dietary therapy of the patients. The conversion efficiency of the reactor with immobillized enzyme is 100% in the range of 0.005-0.6 mM Phe at 9 mM NAD+ with a total flow rate of 0.1 mL/min. The reactor is used for the analyses of 30 samples each for 3 h per day. The half-life period of the reactor is 15 days, method evaluation, overview
medicine
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plays an important role in detection and screening of phenylketonuria diseases
synthesis
analysis
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high yield synthesis of L-amino acids in presence of formate dehydrogenase: L-Phe from phenylpyruvate, L-Tyr from 4-hydroxyphenylpyruvate, L-Trp from indole-3-pyruvate, L-Met from 2-oxo-4-methylthiobutanoate, L-Val from 2-oxoisopentanoate, L-Leu from 2-oxoisohexanoate
analysis
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the chimeric enzyme has a specific activity of 6% of that of the parental phenylalanine dehydrogenase
analysis
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monitoring of phenylketonuria, colorimetric method for the determination of plasma phenylalanine using L-phenylalanine dehydrogenase
analysis
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enzymatic cycling assays for the determination of L-Phe and phenylpyruvate. Assay 1 couples glutamine transferase K with L-phenylalanine dehydrogenase. Assay 2 combines phenylanine dehydrogenase, L-amino acid oxidase, and catalase
analysis
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enzymatic cycling assays for the determination of L-Phe and phenylpyruvate. Assay 1 couples glutamine transferase K with L-phenylalanine dehydrogenase. Assay 2 combines phenylanine dehydrogenase, L-amino acid oxidase, and catalase
analysis
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production of optical and electrochemical sensors for phenylalanine whose molecular architecture can be controlled with precision using mixed stearic acid/phenylalanine dehydrogenase Langmuir films and their immobilization onto solid supports as Langmuir-Blodgett films. PheDH from the aqueous subphase enters the surfactant matrix up to an exclusion surface pressure of 25.3 mN/m, leading to stable and highly condensed mixed Langmuir monolayers. The enzyme fluidizes the stearic acid monolayers, reducing their maximum dipoles when condensed to their maximum, and disorganizes the alkyl chains of the fatty acid
analysis
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monitoring of phenylketonuria, colorimetric method for the determination of plasma phenylalanine using L-phenylalanine dehydrogenase
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biotechnology
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application of the immobilised mutant enzyme N145A that is remarkably robust, even in the presence of high concentrations of polar or non-polar organic solvents such as acetone, methanol, n-hexane, toluene and methylene chloride in the synthesis of p-NO2-phenylalanine from the poorly water-soluble p-NO2-phenylpyruvic acid. 100% stereoselectivity
biotechnology
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use of fed-batch cultivation for achieving high cell densities for the pilot-scale production of the recombinant phenylalanine dehydrogenase
synthesis
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synthesis of allysine (S)-2-amino-5-(1,3-dioxolan-2-yl)-pentanoic acid
synthesis
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formation of L-Phe from phenylpyruvate in presence of formate-dehydrogenase from Candida boidinii
synthesis
expression of mutant R272M/E331Q/E196N in Escherichia coli via a fed-batch fermentation strategy. After 24 h of cultivation, the specific activity of crude extracts is 0.49 U/mg. The specific activity, recovery, yield and purification fold of PheDH are 3.21 U/mg, 104.19%, 84.53% and 6.55%, respectively
