Electronic structure of the metal center in the Cd2+, Zn 2+, and Cu2+ substituted forms of KDO8P synthase: Implications for catalysis

Biochemistry

Volumn 48, Issue 16, 2009, Pages 3610-3630

  Kona, Fathima ^a   Tao, Peng ^a   Martin, Philip ^a   Xu, Xingjue ^a   Gatti, Domenico L ^a  

^a WAYNE STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; AQUIFEX AEOLICUS; BOUND STATE; CONTROL COEFFICIENTS; DIVALENT METAL ION; GASPHASE; GEOMETRY OPTIMIZATION; HIGH-RESOLUTION STRUCTURES; IN-VIVO; LINEAR CONFORMATION; METAL BOUNDS; METAL CENTERS; METAL LIGANDS; PHOSPHOENOLPYRUVATE; PRODUCT CONCENTRATION; PRODUCT RELEASE; QM/MM CALCULATIONS; RELEVANT REACTIONS; REORGANIZATION ENERGIES; STRUCTURAL STUDIES; SUBSTRATE-BOUND; SYNTHASE; WATER MOLECULE;

CADMIUM; CATALYSTS; CONDENSATION REACTIONS; CONFORMATIONS; CRYSTAL STRUCTURE; ELECTRONIC PROPERTIES; ELECTRONIC STRUCTURE; ENZYMES; METAL IONS; METALS; MOLECULAR MECHANICS; ZINC;

STRUCTURAL METALS;

3 DEOXY DEXTRO MANNO OCTULOSONATE 8 PHOSPHATE SYNTHASE; ARABINOSE 5 PHOSPHATE; CADMIUM; COPPER; HYDROXIDE; LIGAND; METAL ION; PHOSPHATE; PHOSPHOENOLPYRUVATE; SYNTHETASE; UNCLASSIFIED DRUG; ZINC; 2 DEHYDRO 3 DEOXYPHOSPHOOCTONATE ALDOLASE; 2-DEHYDRO-3-DEOXYPHOSPHOOCTONATE ALDOLASE; BACTERIAL PROTEIN; LYASE;

ARTICLE; CATALYSIS; CONFORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SUBSTRATE; GEOMETRY; POLYMERIZATION; PRIORITY JOURNAL; QUANTUM MECHANICS; SIMULATION; SUBSTITUTION REACTION; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HYDROGEN BOND; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

AQUIFEX AEOLICUS;

ALDEHYDE-LYASES; BACTERIAL PROTEINS; CADMIUM; CATALYSIS; CATALYTIC DOMAIN; COPPER; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; LIGANDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PROTEIN CONFORMATION; ZINC;

EID: 65449181188     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801955h     Document Type: Article

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