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

Daisuke Matsui; Yasuhisa Asano

doi:10.1016/j.ab.2019.05.010

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

Anal Biochem. 2019 Aug 15:579:57-63. doi: 10.1016/j.ab.2019.05.010. Epub 2019 May 14.

Authors

Daisuke Matsui¹, Yasuhisa Asano²

Affiliations

¹ 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.
² 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: asano@pu-toyama.ac.jp.

PMID: 31100220
DOI: 10.1016/j.ab.2019.05.010

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.

Publication types

Review

MeSH terms

Amino Acid Oxidoreductases / chemistry*
Amino Acid Oxidoreductases / genetics
Bacterial Proteins / chemistry*
Directed Molecular Evolution / methods
Humans
Nostoc / enzymology*
Protein Engineering / methods
Tryptophan / blood*

Substances

Bacterial Proteins
Tryptophan
Amino Acid Oxidoreductases