Young Researcher Paper Award 2023

Notice of retraction
Vol. 34, No. 8(3), S&M3042

Notice of retraction
Vol. 32, No. 8(2), S&M2292

Print: ISSN 0914-4935
Online: ISSN 2435-0869
Sensors and Materials
is an international peer-reviewed open access journal to provide a forum for researchers working in multidisciplinary fields of sensing technology.
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Improved Substrate Specificity of Phenylalanine Dehydrogenase for L-Phenylalanine Sensor

Moemi Tatsumi, Kazutoshi Takahashi, Hiroki Yamaguchi, Uno Tagami, Hiroshi Miyano, Toshimi Mizukoshi, and Masayuki Sugiki

(Received September 1. 2023; Accepted April 18.2024)

Keywords: L-phenylalanine, phenylalanine dehydrogenase, amino acid analysis, colorimetry, enzyme-based biosensors

L-Phenylalanine (L-Phe) is one of the essential amino acids and is important for the human body because it is used in the biosynthesis of neurotransmitters. Phenylalanine dehydrogenase (PheDH) has been studied as a material for the L-Phe sensor. In particular, the accurate and simple determination of L-Phe concentrations in human samples is needed for the diagnosis and treatment of patients with phenylketonuria. Thermostable PheDH from the bacterium Thermoactinomyces intermedius is suitable as a sensor material; however, it is reactive to not only L-Phe but also L-tyrosine (L-Tyr). Thus, we attempted to improve its substrate specificity for the accurate measurement of L-Phe. In this study, we developed the PheDH mutant with improved substrate specificity by amino acid substitution. The PheDH mutant, in which the 290th asparagine residue was substituted with aspartic acid (N290D), is considered to form a new interaction in the substrate binding site and has a markedly reduced reactivity with L-Tyr compared with the wild-type PheDH; the relative activities (L-Tyr/L-Phe) of the wild-type PheDH and the PheDH N290D mutant were 64.0% and 1.5%, respectively. An enzymatic assay using this mutant was established to quantify the L-Phe concentration in human plasma. The relative errors were −10.3% to 7.4% when compared with the quantitative value determined by high-performance liquid chromatography/electrospray ionization mass spectrometry. Furthermore, the immobilized mutant showed a concentration-dependent reactivity with L-Phe and no reactivity with L-Tyr, which indicate its potential use as a sensor material.

Corresponding author: Moemi Tatsumi

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