Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2

Proceedings of the National Academy of Sciences of the United States of America

Volumn 103, Issue 27, 2006, Pages 10224-10229

  Schwer, Bjoern ^a   Bunkenborg, Jakob ^b   Verdin, Regis O ^a   Andersen, Jens S ^b   Verdin, Eric ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF SOUTHERN DENMARK   (Denmark)

Author keywords

sir2; SIRT3; SIRT5; Sirtuin

Indexed keywords

ACETYL COENZYME A SYNTHETASE; ACETYL COENZYME A SYNTHETASE 2; BACTERIAL ENZYME; LYSINE; MITOCHONDRIAL ENZYME; SIRT3 PROTEIN; SIRTUIN; UNCLASSIFIED DRUG;

ACETYLATION; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DEACETYLATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME METABOLISM; ENZYME MODIFICATION; ENZYME REGULATION; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; FUNCTIONAL PROTEOMICS; GENETIC CONSERVATION; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; METABOLIC REGULATION; MITOCHONDRION; NONHUMAN; NUCLEOTIDE SEQUENCE; ORTHOLOGY; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION;

ACETATE-COA LIGASE; ACETYLATION; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CELL LINE; CERCOPITHECUS AETHIOPS; CONSERVED SEQUENCE; HUMANS; LYSINE; MITOCHONDRIA; MITOCHONDRIAL PROTEINS; MOLECULAR SEQUENCE DATA; SEQUENCE ALIGNMENT; SIRTUINS;

BACTERIA (MICROORGANISMS); MAMMALIA;

EID: 33745889628     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0603968103     Document Type: Article

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