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Volumn 346, Issue 6, 2011, Pages 863-866
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Chitinase-catalyzed hydrolysis of 4-nitrophenyl penta-N-acetyl-β- chitopentaoside as determined by real-time ESIMS: The 4-nitrophenyl moiety of the substrate interacts with the enzyme binding site
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Author keywords
4 Nitrophenyl penta N acetyl chitopentaoside; Chitinase; Oligosaccharide hydrolysis; Real time ESIMS; Tryptophan residue
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Indexed keywords
CHITINASE;
CHITINASES;
CLASS II;
ENZYMATIC REACTION;
ENZYME-BINDING SITES;
MUTATED ENZYMES;
REAL-TIME ESIMS;
SIDE CHAINS;
SUBSITES;
SUBSTRATE BINDS;
SUBSTRATE-BINDING;
TRYPTOPHAN RESIDUE;
TRYPTOPHAN RESIDUES;
WILD-TYPE ENZYMES;
AMINO ACIDS;
BINDING ENERGY;
BINDING SITES;
ENZYMES;
HYDROLASES;
HYDROLYSIS;
OLIGOSACCHARIDES;
SUBSTRATES;
4 NITROPHENYL PENTA N ACETYL BETA CHITOPENTAOSIDE;
ALANINE;
CHITINASE;
INDOLE;
PHENYL GROUP;
TRYPTOPHAN;
UNCLASSIFIED DRUG;
ARTICLE;
CATALYSIS;
CRYSTAL STRUCTURE;
ENZYME BINDING;
ENZYME MECHANISM;
HYDROLYSIS;
MUTATION;
PRIORITY JOURNAL;
SUBSTITUTION REACTION;
BINDING SITES;
CATALYSIS;
CHITINASE;
HYDROLYSIS;
MODELS, MOLECULAR;
NITROPHENOLS;
OLIGOSACCHARIDES;
PROTEIN BINDING;
SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;
SUBSTRATE SPECIFICITY;
TRYPTOPHAN;
HORDEUM;
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EID: 79953297036
PISSN: 00086215
EISSN: None
Source Type: Journal
DOI: 10.1016/j.carres.2011.01.012 Document Type: Article |
Times cited : (10)
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References (15)
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