Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion

Biochemistry

Volumn 45, Issue 19, 2006, Pages 6170-6178

  Gantt, Stephanie L ^a   Gattis, Samuel G ^b   Fierke, Carol A ^a,b  

^a UNIVERSITY OF MICHIGAN   (United States)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; HYDROLYSIS; IONS; METAL ANALYSIS; STOICHIOMETRY; TUMORS;

BIOLOGICAL FUNCTION AND REGULATIONS; CATALYTIC METALS; HISTONE DEACETYLASES; REGULATING TRANSCRIPTIONS;

ENZYME INHIBITION;

COBALT; HISTONE DEACETYLASE; HISTONE DEACETYLASE 8; HISTONE DEACETYLASE INHIBITOR; IRON; METAL ION; NICKEL; OXYGEN; UNCLASSIFIED DRUG; VORINOSTAT; ZINC ION;

ARTICLE; CATALYSIS; CELL LYSATE; DIALYSIS; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME PURIFICATION; HUMAN; HYDROLYSIS; MICHAELIS CONSTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; STOICHIOMETRY; TRANSCRIPTION REGULATION;

BASE SEQUENCE; BINDING SITES; CATALYSIS; DNA PRIMERS; HISTONE DEACETYLASES; HUMANS; IRON; MODELS, MOLECULAR; PLASMIDS; RECOMBINANT PROTEINS; REPRESSOR PROTEINS; ZINC;

EID: 33646548638     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060212u     Document Type: Article

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