Catalytic mechanisms and reaction intermediates along the hydrolytic pathway of a plant β-D-glucan glucohydrolase

Structure

Volumn 9, Issue 11, 2001, Pages 1005-1016

  Hrmova, Maria ^a   Varghese, Joseph N ^b   De Gori, Ross ^b   Smith, Brian J ^b,c   Driguez, Hugues ^d   Fincher, Geoffrey B ^a  

^a UNIVERSITY OF ADELAIDE   (Australia)

^b CSIRO   (Australia)

^c WALTER AND ELIZA HALL INSTITUTE OF MEDICAL RESEARCH   (Australia)

^d CENTRE DE RECHERCHES SUR LES MACROMOLÉCULES VÉGÉTALES CERMAV CNRS   (France)

Author keywords

Catalytic acid base; Catalytic nucleophile; Enzyme kinetics; Family 3 glycoside hydrolases; Mechanism based inhibitors; S glycosyl substrate analog

Indexed keywords

GLUCAN; GLUCOSE; GLUCOSIDASE; HYDROLASE; ISOENZYME; OLIGOSACCHARIDE;

AMINO ACID ANALYSIS; ARTICLE; BARLEY; BINDING AFFINITY; CATALYSIS; CATALYST; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HIGHER PLANT; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; REDUCTION; X RAY CRYSTALLOGRAPHY;

CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; CYCLOHEXANOLS; FLUORODEOXYGLUCOSE F18; GLUCOSE; GLUCOSIDASES; HORDEUM; HYDROLYSIS; INOSITOL; MODELS, CHEMICAL; MODELS, MOLECULAR; PEPTIDE MAPPING; QUANTUM THEORY;

EMBRYOPHYTA; HORDEUM VULGARE SUBSP. VULGARE;

EID: 0035183914     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(01)00673-6     Document Type: Article

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