Creation of thermostable l-tryptophan dehydrogenase by protein engineering and its application for l-tryptophan quantification.

Daisuke Matsui, Yasuhisa Asano

Journal: Analytical biochemistry 2020;579():57-63

PMID: 31100220

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Abstract

l-Tryptophan dehydrogenase is a new NAD-dependent amino acid dehydrogenase discovered in Nostoc punctiforme. The enzyme is involved in scytonemin biosynthesis and is highly selective toward l-tryptophan. By a growth-dependent molecular evolution technique, a thermostable mutant enzyme was selected successfully. l-Tryptophan concentration in human plasma was successfully determined using the thermostable mutant of l-tryptophan dehydrogenase.

Address: Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama, 939-0398, Japan; Asano Active Enzyme Molecule Project, ERATO, JST, 5180 Kurokawa, Imizu, Toyama, 939-0398, Japan.; Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama, 939-0398, Japan; Asano Active Enzyme Molecule Project, ERATO, JST, 5180 Kurokawa, Imizu, Toyama, 939-0398, Japan. Electronic address: [email protected].

DOI: 10.1016/j.ab.2019.05.010

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MeSH Terms: Amino Acid Oxidoreductases, Bacterial Proteins, Directed Molecular Evolution, Humans, Nostoc, Protein Engineering, Tryptophan