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Leucine Dehydrogenase: Structure and Thermostability

Authors :
Hiroki, Yamaguchi
Akiko, Kamegawa
Kunio, Nakata
Tatsuki, Kashiwagi
Yoshinori, Fujiyoshi
Kazutoshi, Tani
Toshimi, Mizukoshi
Source :
Sub-cellular biochemistry. 96
Publication Year :
2020

Abstract

Thermostability is a key factor in the industrial and clinical application of enzymes, and understanding mechanisms of thermostability is valuable for molecular biology and enzyme engineering. In this chapter, we focus on the thermostability of leucine dehydrogenase (LDH, EC 1.4.1.9), an amino acid-metabolizing enzyme that is an NAD

Details

ISSN :
03060225
Volume :
96
Database :
OpenAIRE
Journal :
Sub-cellular biochemistry
Accession number :
edsair.pmid..........6bbffe0a56bdd1be5885b212401cfbb2