Structure and functions of the GNAT superfamily of acetyltransferases

Archives of Biochemistry and Biophysics

Volumn 433, Issue 1, 2005, Pages 212-226

  Vetting, Matthew W ^a   S De Carvalho, Luiz Pedro ^a   Yu, Michael ^a   Hegde, Subray S ^a   Magnet, Sophie ^a   Roderick, Steven L ^a   Blanchard, John S ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

Acetyltransferase; Antibiotic resistance; Chemical mechanism; GNAT; Histone acetyltransferase; Protein modification; Steady state kinetics; Structure and function of enzymes; Three dimensional structure

Indexed keywords

ACYL COENZYME A; ACYLTRANSFERASE; AMINO ACYL TRANSFERASE; AMINOGLYCOSIDE N ACETYLTRANSFERASE; FUNGAL ENZYME; GCN5 RELATED N ACETYLTRANSFERASE; GLUCOSAMINE PHOSPHATE ACETYLTRANSFERASE; HISTONE ACETYLTRANSFERASE; ISOENZYME; MYCOTHIOL SYNTHASE; PROTEIN N MYRISTOYLTRANSFERASE; SEROTONIN N ACETYLTRANSFERASE; UNCLASSIFIED DRUG;

ACYLATION; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBUNIT; FUNGAL STRAIN; ISOENZYME ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; SHORT SURVEY; STRUCTURE ACTIVITY RELATION; YEAST GCN5;

ACETYLTRANSFERASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; FUNGAL PROTEINS; KINETICS; MELATONIN; MODELS, MOLECULAR; MODELS, STRUCTURAL; MOLECULAR CONFORMATION; MOLECULAR STRUCTURE; PROTEIN STRUCTURE, SECONDARY; SUBSTRATE SPECIFICITY;

EID: 9744255506     PISSN: 00039861     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.abb.2004.09.003     Document Type: Short Survey

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