A lysine-tyrosine pair carries out acid-base chemistry in the metal ion-dependent pyridine dinucleotide-linked β-hydroxyacid oxidative decarboxylases

Biochemistry

Volumn 48, Issue 16, 2009, Pages 3565-3577

  Aktas, Deniz F ^a   Cook, Paul F ^a  

^a UNIVERSITY OF OKLAHOMA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACID-BASE CHEMISTRY; ACTIVE SITE; ACTIVE SITE RESIDUES; ACTIVE SITE STRUCTURE; ARGININE RESIDUE; CARBOXYLATE LIGANDS; DECARBOXYLASES; DINUCLEOTIDE; DIVALENT METAL ION; GENERAL BASE; ISOCITRATE DEHYDROGENASE; ISOPROPYLMALATE DEHYDROGENASE; KINETIC DATA; MALIC ENZYMES; METAL ION BINDING; MIRROR IMAGES; POSITIVE CHARGE DENSITY; PYRIDINE NUCLEOTIDES; SEQUENCE ALIGNMENTS; SEQUENCE IDENTITY; THREE-DIMENSIONAL STRUCTURE;

ACIDS; AMINO ACIDS; BINDING ENERGY; BINDING SITES; CARBOXYLATION; CATALYSTS; COENZYMES; METAL IONS; METALS; NUCLEOTIDES; PYRIDINE; SUBSTRATES;

ENZYMES;

ALPHA CARBOXYLATE; ARGININE; BETA HYDROXYACID; CARBOXYLIC ACID DERIVATIVE; CARBOXYLYASE; DINUCLEOTIDE; HOMOISOCITRATE DEHYDROGENASE; HYDROXYACID; ISOCITRATE DEHYDROGENASE; ISOPROPYLMALATE DEHYDROGENASE; LYSINE; METAL ION; OXIDOREDUCTASE; PYRIDINE DINUCLEOTIDE; TARTRATE DEHYDROGENASE; TYROSINE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; METAL; NUCLEOTIDE; PYRIDINE DERIVATIVE;

ACID BASE BALANCE; CATALYSIS; DENSITY; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBSTRATE; GEOMETRY; METAL BINDING; OXIDATION; PRIORITY JOURNAL; REVIEW; THREE DIMENSIONAL IMAGING; AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; OXIDATION REDUCTION REACTION; PROTEIN QUATERNARY STRUCTURE; SEQUENCE ALIGNMENT;

ACID-BASE EQUILIBRIUM; AMINO ACID SEQUENCE; ANIMALS; BACTERIAL PROTEINS; CARBOXY-LYASES; CATALYTIC DOMAIN; HUMANS; LYSINE; METALS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; NUCLEOTIDES; OXIDATION-REDUCTION; PROTEIN STRUCTURE, QUATERNARY; PYRIDINES; SEQUENCE ALIGNMENT; TYROSINE;

EID: 65449134009     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8022976     Document Type: Review

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