Probing electrostatic interactions along the reaction pathway of a glycoside hydrolase: Histidine characterization by NMR spectroscopy

Biochemistry

Volumn 46, Issue 25, 2007, Pages 7383-7395

  Schubert, Mario ^a,c   Poon, David K Y ^a   Wicki, Jacqueline ^a   Tarling, Chris A ^a   Kwan, Emily M ^a   Nielsen, Jens E ^b   Withers, Stephen G ^a   McIntosh, Lawrence P ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^b UNIVERSITY COLLEGE DUBLIN   (Ireland)

^c ETH ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

COULOMB INTERACTIONS; HYDROGEN; IONIZATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH EFFECTS; TITRATION;

GLYCOSIDE HYDROLASE; HYDROGEN EXCHANGE; XYLOBIO-IMIDAZOLE;

ENZYME INHIBITION;

ALANINE; APOPROTEIN; BACTERIAL ENZYME; GLYCOSIDASE; HISTIDINE; HYDROGEN; NITROGEN; PROTON;

ARTICLE; CELLULOMONAS; CELLULOMONAS FIMI; CHEMICAL BOND; ELECTRICITY; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME MECHANISM; MOLECULAR PROBE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTON NUCLEAR MAGNETIC RESONANCE;

ALANINE; AMINO ACID SUBSTITUTION; BINDING SITES; CATALYTIC DOMAIN; CELLULOMONAS; ELECTROSTATICS; ENDO-1,4-BETA XYLANASES; GLYCOSIDE HYDROLASES; HISTIDINE; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTONS; STRUCTURE-ACTIVITY RELATIONSHIP;

CELLULOMONAS FIMI;

EID: 34250823484     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700249m     Document Type: Article

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