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Literature summary for 2.3.3.8 extracted from

  • Bazilevsky, G.A.; Affronti, H.C.; Wei, X.; Campbell, S.L.; Wellen, K.E.; Marmorstein, R.
    ATP-citrate lyase multimerization is required for coenzyme-A substrate binding and catalysis (2019), J. Biol. Chem., 294, 7259-7268 .
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + citrate + CoA Homo sapiens the enzyme is a major source of nucleocytosolic acetyl-CoA, a fundamental building block of carbon metabolism in eukaryotes ADP + phosphate + acetyl-CoA + oxaloacetate
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?

Organism

Organism UniProt Comment Textmining
Homo sapiens P53396
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + citrate + CoA
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Homo sapiens ADP + phosphate + acetyl-CoA + oxaloacetate
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?
ATP + citrate + CoA the enzyme is a major source of nucleocytosolic acetyl-CoA, a fundamental building block of carbon metabolism in eukaryotes Homo sapiens ADP + phosphate + acetyl-CoA + oxaloacetate
-
?

Subunits

Subunits Comment Organism
tetramer ACLY C-terminal citrate synthase homology domain maintains ACLY tetramerization, a conserved and essential quaternary structure. ATP-citrate lyase multimerization is required for coenzyme-A substrate binding and catalysis Homo sapiens

Synonyms

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

General Information

General Information Comment Organism
metabolism the enzyme is a major source of nucleocytosolic acetyl-CoA, a fundamental building block of carbon metabolism in eukaryotes Homo sapiens