Mutational Analysis of Conserved Residues in the GCN5 Family of Histone Acetyltransferases

Journal of Biological Chemistry

Volumn 276, Issue 33, 2001, Pages 31321-31331

  Langer, Michael R ^c   Tanner, Kirk G ^a   Denu, John M ^b  

^a VERTEX PHARMACEUTICALS   (United States)

^b OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^c NONE

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CATALYSIS; ISOMERIZATION; ISOTOPES; MUTAGENESIS; PH EFFECTS; REACTION KINETICS;

CONFORMERS; MUTANTS;

ENZYMES;

ACETYL COENZYME A; ACYLTRANSFERASE; ASPARTIC ACID; GLUTAMIC ACID; HISTIDINE; HISTONE ACETYLTRANSFERASE; HISTONE ACETYLTRANSFERASE GCN5; HISTONE H3; LYSINE; PROTEIN; UNCLASSIFIED DRUG; DNA BINDING PROTEIN; FUNGAL PROTEIN; GCN5 PROTEIN, S CEREVISIAE; PROTEIN KINASE; SACCHAROMYCES CEREVISIAE PROTEIN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONFORMATIONAL TRANSITION; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; FUNGUS MUTANT; HYDROGEN BOND; ISOMERISM; MUTATIONAL ANALYSIS; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; SITE DIRECTED MUTAGENESIS; STEADY STATE; YEAST; BINDING SITE; CHEMISTRY; DIALYSIS; ENZYME SPECIFICITY; KINETICS; METABOLISM; PHOSPHORYLATION; STRUCTURE ACTIVITY RELATION;

FUNGI;

ACETYLTRANSFERASES; BINDING SITES; CATALYSIS; DIALYSIS; DNA-BINDING PROTEINS; FUNGAL PROTEINS; HISTONE ACETYLTRANSFERASES; KINETICS; MUTAGENESIS, SITE-DIRECTED; PHOSPHORYLATION; PROTEIN KINASES; SACCHAROMYCES CEREVISIAE PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 0035903089     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M103839200     Document Type: Article

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