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Updated: Jan 24, 2026

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
Published on: October 9, 2021
Creation of thermostable l-tryptophan dehydrogenase by protein engineering and its application for l-tryptophan
Daisuke Matsui1, Yasuhisa Asano1
1Biotechnology 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.
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.
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