Charge stabilization and entropy reduction of central lysine residues in fructose-bisphosphate aldolase

Biochemistry

Volumn 48, Issue 21, 2009, Pages 4528-4537

  St Jean, Miguel ^a   Blonski, Casimir ^b   Sygusch, Jurgen ^a  

^a UNIVERSITÉ DE MONTRÉAL   (Canada)

^b UPS)   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ALDOLASE; BISPHOSPHATE; C-C BONDS; C-TERMINAL REGIONS; CARBON-CARBON BOND FORMATION; CATALYTIC ACTIVITY; CHARGE STABILIZATION; CONFORMATIONAL CHANGE; DIHYDROXYACETONE PHOSPHATE; ENAMINE; ENTROPY REDUCTION; ENZYMATIC ACTIVITIES; GLYCOLYTIC ENZYME; INTERCONVERSION; KINETIC BARRIER; LYSINE RESIDUES; PROTONATED; SCHIFF-BASE; SIDE CHAINS;

AMINES; AMINO ACIDS; BINDING SITES; CATALYTIC OXIDATION; CRYSTALS; FRUCTOSE; ORGANIC ACIDS; OXIDATION; STABILIZATION; STRUCTURAL ANALYSIS;

PROTON TRANSFER;

ASPARAGINE; DIHYDROXYACETONE PHOSPHATE; ENAMINE; FRUCTOSE BISPHOSPHATE ALDOLASE; GLYCERALDEHYDE 3 PHOSPHATE; LYSINE; PHOSPHATE; SCHIFF BASE; TYROSINE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; COVALENT BOND; ENTHALPY; ENTROPY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ENZYME STABILITY; NONHUMAN; OXIDATION; PKA; PRIORITY JOURNAL; PROTON TRANSPORT; STRUCTURE ANALYSIS;

ANIMALS; BIOCATALYSIS; CATALYTIC DOMAIN; CONSERVED SEQUENCE; ENTROPY; FRUCTOSE-BISPHOSPHATE ALDOLASE; KINETICS; LYSINE; MODELS, MOLECULAR; PHOSPHATES; POINT MUTATION; PROTEIN CONFORMATION; PROTONS; RABBITS;

EID: 66349123522     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8021558     Document Type: Article

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