Structural insights into thermostabilization of leucine dehydrogenase from its atomic structure by cryo-electron microscopy

[Display omitted] Leucine dehydrogenase (LDH, EC 1.4.1.9) is a NAD+-dependent oxidoreductase that catalyzes the deamination of branched-chain l-amino acids (BCAAs). LDH of Geobacillus stearothermophilus (GstLDH) is a highly thermostable enzyme that has been applied for the quantification or producti...

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Veröffentlicht in:	Journal of structural biology 2019-01, Vol.205 (1), p.11-21
Hauptverfasser:	Yamaguchi, Hiroki, Kamegawa, Akiko, Nakata, Kunio, Kashiwagi, Tatsuki, Mizukoshi, Toshimi, Fujiyoshi, Yoshinori, Tani, Kazutoshi
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Binding Sites Conformational change Cryo-EM Cryoelectron Microscopy - methods De novo modeling Geobacillus stearothermophilus - enzymology Leucine Dehydrogenase - chemistry Molecular Structure Mutagenesis, Site-Directed NAD - chemistry NAD+ recognition Protein Stability Single particle analysis
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