The enzyme does not act on 4-O-acetylated sialic acids. endo-alpha-Sialidase activity is listed as EC 3.2.1.129, endo-alpha-sialidase. See also EC 4.2.2.15 anhydrosialidase.
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SYSTEMATIC NAME
IUBMB Comments
acetylneuraminyl hydrolase
The enzyme does not act on 4-O-acetylated sialic acids. endo-alpha-Sialidase activity is listed as EC 3.2.1.129, endo-alpha-sialidase. See also EC 4.2.2.15 anhydrosialidase.
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparison of the catalytic cleft plasticity of free and ligand-bound forms of Trypanosoma rangeli sialidase and Trypanosoma cruzi trans-sialidase using molecular dynamics simulations. The Trypanosoma cruzi enzyme has a very flexible, widely open catalytic cleft, mostly due to resiude W312 loop motion, in apo form. In ligan-bound form, the flexibility and solvent exposure is significantly reduced. The Trypanosoma rangeli sialidase maintains a more open catalytic cleft in both apo and holo forms
three-dimensional structures of the covalent glycosyl-enzyme complexes formed by Trypanosoma rangeli sialidase with two different mechanism-based inactivators at 1.9 A and at 1.7 A resolution
engineered free sialidase Tr6 is stable at 25°C for at least 24 h. At 45°C the enzyme is stable for at least 100 min. 2% of the initial trans-sialidase activity is retained after 5 min of incubation at 65°C
Modulation of catalytic function by differential plasticity of an active site: case study of Trypanosoma cruzi trans-sialidase and Trypanosoma rangeli sialidase
Unraveling the differences of the hydrolytic activity of Trypanosoma cruzi trans-sialidase and Trypanosoma rangeli sialidase: a quantum mechanics-molecular mechanics modeling study