Temperature differences for trans-glycosylation and hydrolysis reaction reveal an acceptor binding site in the catalytic mechanism of Trypanosoma cruzi trans-sialidase

Glycobiology

Volumn 7, Issue 8, 1997, Pages 1237-1246

  Ribeirão, Marcelo ^a   Pereira Chioccola, Vera Lucia ^b   Eichinger, Daniel ^c   Rodrigues, Mauricio M ^a   Schenkman, Sergio ^a,d  

^a FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

^b INSTITUTO DANTE PAZZANESE DE CARDIOLOGIA   (Brazil)

^c NEW YORK UNIVERSITY   (United States)

^d Disciplina de Biologia Celular   (Brazil)

Author keywords

Kinetics; Reaction mechanism; Sialidase; Temperature; Trypanosoma cruzi

Indexed keywords

SIALIDASE;

ARTICLE; BINDING AFFINITY; BINDING SITE; CHAGAS DISEASE; ENZYME BINDING; ENZYME KINETICS; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN GLYCOSYLATION; TEMPERATURE DEPENDENCE; TRYPANOSOMA CRUZI;

ANIMALS; BINDING SITES; CATALYSIS; ESCHERICHIA COLI; FLUORESCENT DYES; GALACTOSE; GLYCOPROTEINS; GLYCOSYLATION; HYDROLYSIS; HYMECROMONE; LACTOSE; N-ACETYLNEURAMINIC ACID; NEURAMINIDASE; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; TEMPERATURE; TRYPANOSOMA CRUZI;

EID: 0031440882     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/7.8.1237     Document Type: Article

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