Literature summary for 1.4.1.9 extracted from

Yamaguchi, H.; Kamegawa, A.; Nakata, K.; Kashiwagi, T.; Mizukoshi, T.; Fujiyoshi, Y.; Tani, K.
Structural insights into thermostabilization of leucine dehydrogenase from its atomic structure by cryo-electron microscopy (2019), J. Struct. Biol., 205, 11-21 .

Search for more literature for 1.4.1.9

Crystallization (Commentary)

Crystallization (Comment)	Organism
cryo-electron microscopy structures of apo and NAD+-bound LDH at 3.0 and 3.2 A resolution, respectively. A partial conformational change is triggered by the interaction between Ser147 and the nicotinamide moiety of NAD+. NAD+ binding also enhances the strength of oligomerization interfaces formed by the core domains	Geobacillus stearothermophilus

Protein Variants

Protein Variants	Comment	Organism
A94E	proportion of residual activity of A94E is 19% of that of wild type after incubation at 70 °C for 10 min	Geobacillus stearothermophilus
Y127N	proportion of residual activity of Y127N is 27% of that of wild type after incubation at 70 °C for 10 min	Geobacillus stearothermophilus

Organism

Organism	UniProt	Comment	Textmining
Geobacillus stearothermophilus	P13154	-	-

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
70	-	-	Geobacillus stearothermophilus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	non-conserved residues Ala94 Tyr127, and the C-terminal region, are crucial for oligomeric thermostability	Geobacillus stearothermophilus
80	-	the residual activity of NAD+-bound form is approximately three times higher than that of the apo form after incubation at 80°C	Geobacillus stearothermophilus

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Release 2023.1 (January 2023)