Literature summary extracted from

Noorbatcha, I.A.; Sultan, A.M.; Salleh, H.M.; Amid, A.
Understanding thermostability factors of Aspergillus niger PhyA phytase: a molecular dynamics study (2013), Protein J., 32, 309-316.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
3.1.3.8	molecular dynamics simulation and comparison between wild-type and thermostable mutant A35E/P42S/Q168R/T248R show that among secondary structure elements, loops have the most impact on the thermal stability of Aspergillus niger phytase. In addition, the location rather than the number of hydrogen bonds has an important contribution to thermostability. Salt bridges may have stabilizing or destabilizing effect on the enzyme and influence its thermostability accordingly	Aspergillus niger

Protein Variants

EC Number	Protein Variants	Comment	Organism
3.1.3.8	A35E/P42S/Q168R/T248R	thermostable mutant. Molecular dynamics simulation and comparison with wild-type show that among secondary structure elements, loops have the most impact on the thermal stability of Aspergillus niger phytase. In addition, the location rather than the number of hydrogen bonds has an important contribution to thermostability. Salt bridges may have stabilizing or destabilizing effect on the enzyme and influence its thermostability accordingly	Aspergillus niger

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.1.3.8	Aspergillus niger	P34752	-	-

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Release 2023.1 (January 2023)