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

被引：3
|
作者：
Matsui, Daisuke [1 ,2 ,3 ]
Asano, Yasuhisa [1 ,2 ,3 ]
机构：
[1] Toyama Prefectural Univ, Biotechnol Res Ctr, 5180 Kurokawa, Imizu, Toyama 9390398, Japan
[2] Toyama Prefectural Univ, Dept Biotechnol, 5180 Kurokawa, Imizu, Toyama 9390398, Japan
[3] JST, ERATO, Asano Act Enzyme Mol Project, 5180 Kurokawa, Imizu, Toyama 9390398, Japan
来源：
ANALYTICAL BIOCHEMISTRY | 2019年 / 579卷
基金：
日本学术振兴会;
关键词：
PERFORMANCE LIQUID-CHROMATOGRAPHY; PLASMA AMINO-ACIDS; PROLINE DEHYDROGENASE; SELECTION SYSTEM; L-THREONINE; BIOSYNTHESIS; QUANTITATION; METABOLITES; KYNURENINE; STABILITY;
D O I：
10.1016/j.ab.2019.05.010
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：57 / 63
页数：7
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