Structures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K + ions

Biochemistry

Volumn 45, Issue 24, 2006, Pages 7544-7552

  Milić, Dalibor ^a   Matković Čalogović, Dubravka ^a   Demidkina, Tatyana V ^b   Kulikova, Vitalia V ^b   Sinitzina, Nina I ^b   Antson, Alfred A ^c  

^a UNIVERSITY OF ZAGREB   (Croatia)

^b ENGELHARDT INSTITUTE OF MOLECULAR BIOLOGY   (Russian Federation)

^c UNIVERSITY OF YORK   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; CATALYSIS; CONFORMATIONS; MOLECULAR STRUCTURE; MUTAGENESIS; PH EFFECTS;

ENZYMATIC REACTIONS; HYDROLYTIC CLEAVAGE; LYASES; PROTEIN INTERACTIONS;

ENZYMES;

AMMONIA; AMMONIUM PYRUVATE; APOENZYME; ARGININE; BACTERIAL ENZYME; BETA ELIMINATING LYASE; GLUTAMIC ACID; HOLOENZYME; KETO(IMINO)QUINONOID; LYASE; PHENOL; PHENYLALANINE; POTASSIUM ION; PYRIDOXAL 5 PHOSPHATE; PYRUVIC ACID DERIVATIVE; QUINONE DERIVATIVE; TYROSINE; TYROSINE PHENOL LYASE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CITROBACTER FREUNDII; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROLYSIS; MOLECULAR DYNAMICS; MUTATIONAL ANALYSIS; PH; PRIORITY JOURNAL; PROTEIN INTERACTION; TRANSITION INTERMEDIATE;

APOENZYMES; ARGININE; BINDING SITES; CATALYSIS; CITROBACTER FREUNDII; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; GLUTAMINE; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; PHENYLALANINE; POTASSIUM; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PYRIDOXAL PHOSPHATE; SUBSTRATE SPECIFICITY; TYROSINE; TYROSINE PHENOL-LYASE;

CITROBACTER FREUNDII;

EID: 33745125692     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0601858     Document Type: Article

References (55)

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