A salt-bridge controlled by ligand binding modulates the hydrolysis reaction in a GH5 endoglucanase

Protein Engineering, Design and Selection

Volumn 25, Issue 5, 2012, Pages 223-233

  Badieyan, Somayesadat ^a   Bevan, David R ^b   Zhang, Chenming ^a  

^a State University   (United States)

^b VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

Author keywords

Cel5B; endoglucanases; ligand binding; molecular dynamics; protonation state

Indexed keywords

ACTIVE SITE; ANOMERIC CARBON; ASPARTATES; BIOMASS CONVERSION; CARBOXYLATE GROUPS; CEL5B; CELLOBIOSE; CLEAVAGE PRODUCTS; CLOSTRIDIUM THERMOCELLUM; CONFORMATIONAL CHANGE; ENDOGLUCANASES; GLYCOSIDE HYDROLASES; HYDROLYSIS REACTION; IN-SILICO; IN-VITRO; ION PAIRS; LIGAND BINDING; MICROENVIRONMENTS; NUCLEOPHILIC ATTACK; PROTON DONORS; PROTONATED; PROTONATION STATE; RENEWABLE ENERGIES; STEERED MOLECULAR DYNAMICS; WILD TYPES;

BIOCONVERSION; CARBOXYLATION; CONFORMATIONS; ENZYMES; MOLECULAR DYNAMICS; PLANTS (BOTANY); PROTONATION; PROTONS; REACTION KINETICS; SEPARATION; SUBSTRATES;

LIGANDS;

CEL5B PROTEIN; GLUCAN SYNTHASE; GLUTAMIC ACID; GLYCOSIDASE; PROTON; UNCLASSIFIED DRUG;

ARTICLE; CLOSTRIDIUM THERMOCELLUM; COMPUTER MODEL; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; HYDROLYSIS; HYDROPHILICITY; IN VITRO STUDY; LIGAND BINDING; MOLECULAR DYNAMICS; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTON TRANSPORT; STATIC ELECTRICITY;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CELLULASE; CELLULOSE; GLUTAMIC ACID; HISTIDINE; HYDROLYSIS; LIGANDS; MOLECULAR DYNAMICS SIMULATION; PROTEIN CONFORMATION; PROTONS; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY; TETROSES;

CLOSTRIDIUM THERMOCELLUM;

EID: 84860451743     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzs010     Document Type: Article

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