Kinetic and mechanistic analysis of Trypanosoma cruzi trans-sialidase reveals a classical ping-pong mechanism with acid/base catalysis

Biochemistry

Volumn 47, Issue 11, 2008, Pages 3507-3512

  Damager, Iben ^a   Buchini, Sabrina ^a   Amaya, Maria F ^b   Buschiazzo, Alejandro ^b   Alzari, Pedro ^b   Frasch, Alberto C ^c   Watts, Andrew ^a   Withers, Stephen G ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^b INSTITUT PASTEUR   (France)

^c UNIVERSIDAD NACIONAL DE SAN MARTÍN   (Argentina)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; ENZYMES; MASS SPECTROMETRY; PEPTIDES;

SIALIC ACID; SIALYL AZIDE; TRYPANOSOMA CRUZI;

MICROORGANISMS;

4 NITROPHENOL; ACID; AZIDE; BASE; GALACTOSE; SIALIC ACID DERIVATIVE; SIALIDASE;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; CATALYST; CONCENTRATION RESPONSE; COVALENT BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; SIALYLATION; TRYPANOSOMA CRUZI;

ALANINE; ANIMALS; ASPARTIC ACID; AZIDES; CATALYSIS; GLYCOPROTEINS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; N-ACETYLNEURAMINIC ACID; NEURAMINIDASE; NITROPHENOLS; SUBSTRATE SPECIFICITY; TRYPANOSOMA CRUZI; TYROSINE;

TRYPANOSOMA CRUZI;

EID: 40849118185     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7024832     Document Type: Article

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