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Journal of the American Chemical Society

Volumn 123, Issue 48, 2001, Pages 11960-11969

Diphtheria toxin catalyzed hydrolysis of NAD+: Molecular dynamics study of enzyme-bound substrate, transition state, and inhibitor

(2) Kahn, K a Bruice, T C a

a UNIVERSITY OF CALIFORNIA (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL STRESS;

ACTIVATION ENERGY; CRYSTAL STRUCTURE; ENZYME INHIBITION; HYDROGEN BONDS; HYDROLYSIS; ISOMERIZATION; MOLECULAR DYNAMICS; PROTEINS; SUBSTRATES;

BIOCATALYSTS;

AMIDE; CARBONYL DERIVATIVE; CARBOXYLIC ACID DERIVATIVE; DIPHTHERIA TOXIN; ENZYME; ENZYME INHIBITOR; GLUTAMIC ACID; HYDROXYL GROUP; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE; RIBOSE;

ARTICLE; CALCULATION; CATALYSIS; CHEMICAL BOND; CHEMICAL REACTION KINETICS; CONFORMATIONAL TRANSITION; ENERGY; ENZYME ACTIVE SITE; ENZYME INHIBITOR COMPLEX; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; MOLECULAR DYNAMICS; MOLECULAR STABILITY; QUANTUM CHEMISTRY; REACTION ANALYSIS; TIME; TRANS ISOMER;

CATALYSIS; DIPHTHERIA TOXIN; HYDROLYSIS; KINETICS; MODELS, CHEMICAL; MODELS, MOLECULAR; NAD; NAD+ NUCLEOSIDASE; OLIGORIBONUCLEOTIDES; PROTEIN CONFORMATION; QUANTUM THEORY; THERMODYNAMICS;

EID: 0035814372 PISSN: 00027863 EISSN: None Source Type: Journal
DOI: 10.1021/ja0113807 Document Type: Article

Times cited : (10)

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