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Deuterium isotope effects in mechanistic studies of biotransformations of l-tyrosine and p-hydroxyphenylpyruvic acid catalyzed by the enzyme l-phenylalanine dehydrogenase Cover

Deuterium isotope effects in mechanistic studies of biotransformations of l-tyrosine and p-hydroxyphenylpyruvic acid catalyzed by the enzyme l-phenylalanine dehydrogenase

Open Access
|May 2025

Figures & Tables

Fig. 1.

Enforced metabolic pathways of accumulated l-Phe and l-Tyr in a person suffering from PKU and type I tyrosinemia diseases.
Enforced metabolic pathways of accumulated l-Phe and l-Tyr in a person suffering from PKU and type I tyrosinemia diseases.

Fig. 2.

Alternative metabolic pathways of l-Tyr in a person suffering from type II tyrosinemia disease.
Alternative metabolic pathways of l-Tyr in a person suffering from type II tyrosinemia disease.

Fig. 3.

Reversible conversion of l-Phe and l-Tyr into corresponding oxoacids catalyzed by the enzyme PheDH.
Reversible conversion of l-Phe and l-Tyr into corresponding oxoacids catalyzed by the enzyme PheDH.

Solvent isotope effects (SIE) and kinetic isotope effects (KIE) in the oxidative deamination of l-Tyr and reductive amination of PPA catalyzed by enzyme PheDH

ReactantSIE

on Vmaxon Vmax/KM
l-Tyr1.43 ± 0.091.48 ± 0.12
PPA1.44 ± 0.081.58 ± 0.14

KIE
on Vmaxon Vmax/KM

l-Tyr/[2-2H]-l-Tyr2.26 ± 0.102.87 ± 0.11
PPA/[(3S)-2H]-PPA1.55 ± 0.061.53 ± 0.16
DOI: https://doi.org/10.2478/nuka-2025-0006 | Journal eISSN: 1508-5791 | Journal ISSN: 0029-5922
Language: English
Page range: 51 - 56
Submitted on: Jan 5, 2024
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Accepted on: Mar 4, 2025
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Published on: May 2, 2025
In partnership with: Paradigm Publishing Services
Publication frequency: 4 issues per year

© 2025 Katarzyna Pałka, Katarzyna Podsadni, Jolanta Szymańska-Majchrzak, Elżbieta Winnicka, published by Institute of Nuclear Chemistry and Technology
This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 License.