A Sensitive gel-based method combining distinct cyclophellitol-based probes for the identification of acid/base residues in human retaining β-glucosidases

Journal of Biological Chemistry

Volumn 289, Issue 51, 2014, Pages 35351-35362

  Kallemeijn, Wouter W ^a   Witte, Martin D ^b,c   Voorn Brouwer, Tineke M ^a   Walvoort, Marthe T C ^b,d   Li, Kah Yee ^b   Codée, Jeroen D C ^b   Van Der Marel, Gijsbert A ^b   Boot, Rolf G ^a   Overkleeft, Herman S ^b   Aerts, Johannes M F G ^a  

^a UNIVERSITY OF AMSTERDAM   (Netherlands)

^b LEIDEN UNIVERSITY   (Netherlands)

^c UNIVERSITY OF GRONINGEN   (Netherlands)

^d MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; FLUORESCENCE; NUCLEOPHILES; PROBES;

ACTIVITY-BASED PROBE; BETA-GLUCOSIDASE; BETA-GLUCOSIDASES; CATALYTIC RESIDUE; IRREVERSIBLE INHIBITIONS; SELECTIVE LABELING; SENSITIVE METHOD; SITE DIRECTED MUTAGENESIS;

AMINO ACIDS;

AZIRIDINE; BETA GLUCOSIDASE; CYCLOPHELLITOL; EPOXIDE; GLUTAMINE; GLYCINE; AMINO ACID; AZIRIDINE DERIVATIVE; CYCLOHEXANOL DERIVATIVE; MOLECULAR PROBE; SODIUM AZIDE;

AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL LABELING; CHEMICAL STRUCTURE; COVALENT BOND; ENZYME ACTIVITY; HUMAN; HYDROLYSIS; MOLECULAR CLONING; NUCLEIC ACID PROBE; NUCLEOPHILICITY; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN ISOLATION; PROTEIN MODIFICATION; PROTON TRANSPORT; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS; STEREOCHEMISTRY; ANIMAL; CHEMISTRY; CHLOROCEBUS AETHIOPS; COS 1 CELL LINE; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; GENETICS; IMMUNOBLOTTING; METABOLISM; MISSENSE MUTATION; MOLECULAR PROBE; PROCEDURES; REPRODUCIBILITY;

AMINO ACID SUBSTITUTION; AMINO ACIDS; ANIMALS; AZIRIDINES; BETA-GLUCOSIDASE; CATALYTIC DOMAIN; CERCOPITHECUS AETHIOPS; COS CELLS; CYCLOHEXANOLS; EPOXY COMPOUNDS; HUMANS; HYDROLYSIS; IMMUNOBLOTTING; MOLECULAR PROBES; MUTAGENESIS, SITE-DIRECTED; MUTATION, MISSENSE; REPRODUCIBILITY OF RESULTS; SODIUM AZIDE; SUBSTRATE SPECIFICITY;

EID: 84919476580     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.593376     Document Type: Article

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