Center for Bioinformatics
Oxidoreductases | Transferases | Hydrolases | Lyases | Isomerases | Ligases

Basic Information

Enzyme Number

2.3.3.8

Official Name

ATP citrate synthase

Name from literature

citrate lyase

Pathway from literature

de novo synthesis of fatty acids and triglycerides

Pathway from KEGG

Energy Metabolism; Reductive carboxylate cycle (CO2 fixation); map00720

Carbohydrate Metabolism; Citrate cycle (TCA cycle); map00020

Organisms

Mouse (10090)

Genome localization

11 D[104112 ],

Comments

The enzyme can be dissociated into components, two of which are identical with EC 4.1.3.34 (citryl-CoA lyase) and EC 6.2.1.18 (citrate---CoA ligase).

Rate-limiting Description

"This phenotype is caused by a mild but significant reduction in total energy expenditure paralleled by increased expression of ATP citrate lyase, a rate-limiting step in de novo synthesis of fatty acids and triglycerides." (17404227)

Regulatory Information

Upstream transcription factor

20787

Regulatory type

Detail

phosphorylation;

Q91V92:from_uniprot:1090_Phosphoserine

phosphorylation;

Q91V92:from_uniprot:131_Phosphotyrosine

phosphorylation;

Q91V92:from_uniprot:455_Phosphoserine; by PKA

phosphorylation;

Q91V92:from_uniprot:672_Phosphotyrosine

transcriptional factor;SREBP1a(20787)

"The roles of sterol regulatory element-binding proteins in the transactivation of the rat ATP citrate-lyase promoter." (10801800#11750882)

Gene ontology

Gene ontology

GO:0000287 (F) magnesium ion binding [Q91V92 ];
GO:0008610 (P) lipid biosynthetic process [Q91V92 ];
GO:0004775 (F) succinate-CoA ligase (ADP-forming) activity [Q91V92 ];
GO:0005737 (C) cytoplasm [Q91V92 ];
GO:0005524 (F) ATP binding [Q91V92 ];
GO:0044262 (P) cellular carbohydrate metabolic process [Q91V92 ];
GO:0003878 (F) ATP citrate synthase activity [Q91V92 ];
GO:0005515 (F) protein binding [Q91V92 ];
GO:0006085 (P) acetyl-CoA biosynthetic process [Q91V92 ];

Subcellular localization

Localization

cytoplasm [Q91V92 ];

Links

SwissProt

Q91V92

Entrez Gene

104112



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  Last Modified: 2009-03-24  
  Design by Zhao Min