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Literature summary for 2.3.3.8 extracted from

  • Granchi, C.
    Discovery of allosteric inhibition of human ATP-citrate lyase (2019), Trends Pharmacol. Sci., 40, 364-366 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
full structure of human ACLY homotetramer in ternary complex with the inhibitor and ADP with an overall resolution of 3.67 A Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
methyl 3-chloro-5-(N-(4,6-difluoro-[1,1'-biphenyl]-3-yl)sulfamoyl)-4-hydroxybenzoate i.e. NDI-091143, allosteric inhibition Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + citrate + CoA Homo sapiens the enzyme links glycolysis to lipid metabolism ADP + phosphate + acetyl-CoA + oxaloacetate
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P53396
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + citrate + CoA
-
Homo sapiens ADP + phosphate + acetyl-CoA + oxaloacetate
-
?
ATP + citrate + CoA the enzyme links glycolysis to lipid metabolism Homo sapiens ADP + phosphate + acetyl-CoA + oxaloacetate
-
?

Subunits

Subunits Comment Organism
homotetramer
-
Homo sapiens

Synonyms

Synonyms Comment Organism
ACLY
-
Homo sapiens
ATP-citrate lyase
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Homo sapiens