On the catalytic mechanism of human ATP citrate lyase

Biochemistry

Volumn 51, Issue 25, 2012, Pages 5198-5211

  Fan, Fan ^a   Williams, Howard J ^b   Boyer, Joseph G ^a   Graham, Taylor L ^a   Zhao, Huizhen ^a   Lehr, Ruth ^a   Qi, Hongwei ^a   Schwartz, Benjamin ^a   Raushel, Frank M ^b   Meek, Thomas D ^a  

^a GLAXOSMITHKLINE   (United States)

^b TEXAS A AND M UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACTIVE SITE RESIDUES; ATP-ASE ACTIVITY; ATP-CITRATE LYASE; CATALYTIC MECHANISMS; CATALYTIC ROLE; COENZYME A; COMPUTATIONAL SIMULATION; DIETHYLPYROCARBONATE; IONIZABLE GROUPS; ISOTOPE EXCHANGE; MATHEMATICAL ANALYSIS; MAXIMAL RATES; PH-DEPENDENCE; PHOSPHORYL TRANSFER; RATE-LIMITING STEPS; STEADY-STATE MEASUREMENTS; WILD TYPES;

AMINO ACIDS; BIOCHEMISTRY; BIOSYNTHESIS; CATALYSIS; DESORPTION; FINANCE; ISOTOPES; PHOSPHORYLATION; QUANTUM CHEMISTRY;

REACTION RATES;

ACETYL COENZYME A; ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE CITRATE LYASE; ALANINE; CITRIC ACID; COENZYME A; DIETHYL PYROCARBONATE; HISTIDINE; OXALOACETIC ACID;

ARTICLE; BIOSYNTHESIS; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME PHOSPHORYLATION; MATHEMATICAL ANALYSIS; MUTAGENESIS; PRIORITY JOURNAL; STEADY STATE;

ACETYL COENZYME A; ATP CITRATE (PRO-S)-LYASE; BIOCATALYSIS; CATALYTIC DOMAIN; CONSERVED SEQUENCE; DEUTERIUM EXCHANGE MEASUREMENT; HISTIDINE; HUMANS; MUTATION; OXALOACETATE; PHOSPHORYLATION;

EID: 84862893463     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300611s     Document Type: Article

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