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Literature summary for 3.2.1.18 extracted from

  • Watts, A.G.; Oppezzo, P.; Withers, S.G.; Alzari, P.M.; Buschiazzo, A.
    Structural and kinetic analysis of two covalent sialosyl-enzyme intermediates on Trypanosoma rangeli sialidase (2006), J. Biol. Chem., 281, 4149-4155.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Trypanosoma rangeli

Organism

Organism UniProt Comment Textmining
Trypanosoma rangeli O44049
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Reaction

Reaction Comment Organism Reaction ID
colominic acid + H2O = sialic acid + lactose catalytic chemistry involves the formation of a covalent intermediate with an active site tyrosine nucleophile Trypanosoma rangeli