Literature summary for 3.2.1.78 extracted from

Li, J.; Bewley, J.D.; Hua, Z.; Zheng, W.; Wang, A.
Model and molecular dynamic simulations of active and inactive endo-beta-1,4-mannanase in tomato fruit (2008), Protein J., 27, 363-370.

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular dynamic simulation of wild-type and mutant lacking the C-terminal amino acid residues 394-399, SerLysLeuSer. The inactive form has a lower stability than the active one. The loss of amino acids from the C-terminal end of the protein indirectly affects the conformation of the catalytic Glu318 residue and stability of active site because of interactions between residues at the C-terminus and the rest of protein	Solanum lycopersicum

Crystallization (Comment)

Organism

molecular dynamic simulation of wild-type and mutant lacking the C-terminal amino acid residues 394-399, SerLysLeuSer. The inactive form has a lower stability than the active one. The loss of amino acids from the C-terminal end of the protein indirectly affects the conformation of the catalytic Glu318 residue and stability of active site because of interactions between residues at the C-terminus and the rest of protein

Solanum lycopersicum

Protein Variants

Protein Variants	Comment	Organism
additional information	the cultivar Walter displays an inactive enzyme due to the absence of the C-terminal four amino acid residues 394-399, SerLysLeuSer. The inactive form has a lower stability than the active one. The loss of amino acids from the C-terminal end of the protein indirectly affects the conformation of the catalytic Glu318 residue and stability of active site because of interactions between residues at the C-terminus and the rest of protein	Solanum lycopersicum

Organism

Organism	UniProt	Comment	Textmining
Solanum lycopersicum	Q8L5J1	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
fruit	-	Solanum lycopersicum	-

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Release 2023.1 (January 2023)