1.4.1.20: phenylalanine dehydrogenase
This is an abbreviated version!
For detailed information about phenylalanine dehydrogenase, go to the full flat file.

Reaction
Synonyms
dehydrogenase, phenylalanine, L-PheDH, L-phenylalanine dehydrogenase, L-phenylalanine:NAD+ oxidoreductase, deaminating, PDH, PHD, PheDH, phenylalanine dehydrogenase, recombinant PheDH, recombinant phenylalanine dehydrogenase
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Application
Application on EC 1.4.1.20 - phenylalanine dehydrogenase
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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
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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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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
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use of fed-batch cultivation for achieving high cell densities for the pilot-scale production of the recombinant phenylalanine dehydrogenase
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
synthesis
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formation of L-Phe from phenylpyruvate in presence of formate-dehydrogenase from Candida boidinii
synthesis
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synthesis of allysine (S)-2-amino-5-(1,3-dioxolan-2-yl)-pentanoic acid