Phosphorylation of recombinant human ATP:citrate lyase by cAMP-dependent protein kinase abolishes homotropic allosteric regulation of the enzyme by citrate and increases the enzyme activity. Allosteric activation of atp:citrate lyase by phosphorylated sugars

Biochemistry

Volumn 39, Issue 5, 2000, Pages 1169-1179

  Potapova, Irina A ^a   El Maghrabi, M Raafat ^a   Doronin, Sergey V ^a   Benjamin, William B ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CITRIC ACID; LYASE; PROTEIN KINASE;

ARTICLE; ENZYME ACTIVITY; ENZYME ISOLATION; ENZYME KINETICS; ENZYME PHOSPHORYLATION; ENZYME REGULATION; HUMAN; NONHUMAN; PRIORITY JOURNAL;

ALLOSTERIC REGULATION; ANIMALS; ATP CITRATE (PRO-S)-LYASE; CATALYSIS; CITRIC ACID; CYCLIC AMP-DEPENDENT PROTEIN KINASES; ENZYME ACTIVATION; HUMANS; KINETICS; PHOSPHORYLATION; PLASMIDS; RATS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; SUGAR PHOSPHATES;

MAMMALIA;

EID: 0034620591     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi992159y     Document Type: Article

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