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

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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… Click to show full 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.

Keywords: dehydrogenase; tryptophan dehydrogenase; creation thermostable; thermostable tryptophan; protein engineering; dehydrogenase protein

Journal Title: Analytical biochemistry
Year Published: 2019

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