Class of enzymes
Human ATP citrate lyase |
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Crystal structure of human ATP citrate lyase in complex with citrate, coenzyme A and Mg.ADP. [1] |
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Symbol | ACLY |
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Alt. symbols | ACL |
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NCBI gene | 47 |
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HGNC | 115 |
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OMIM | 108728 |
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PDB | 3MWE, 3PFF, 5TDE, 5TDF, 5TDM, 5TDZ, 5TE1, 5TEQ, 5TES, 5TET, 6HXH, 6HXK, 6HXL, 6HXM, 6O0H, 6QFB 3MWD, 3MWE, 3PFF, 5TDE, 5TDF, 5TDM, 5TDZ, 5TE1, 5TEQ, 5TES, 5TET, 6HXH, 6HXK, 6HXL, 6HXM, 6O0H, 6QFB |
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RefSeq | NM_001096 |
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UniProt | P53396 |
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EC number | 2.3.3.8 |
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Locus | Chr. 17 q21.2 |
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ATP citrate synthase (also ATP citrate lyase (ACLY)) is an enzyme that in animals catalyzes an important step in fatty acid biosynthesis.[2] By converting citrate to acetyl-CoA, the enzyme links carbohydrate metabolism, which yields citrate as an intermediate, with fatty acid biosynthesis, which consumes acetyl-CoA.[3] In plants, ATP citrate lyase generates cytosolic acetyl-CoA precursors of thousands of specialized metabolites, including waxes, sterols, and polyketides.[4]
- ^ Verschueren KH, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, et al. (April 2019). "Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle" (PDF). Nature. 568 (7753): 571–575. Bibcode:2019Natur.568..571V. doi:10.1038/s41586-019-1095-5. PMID 30944476. S2CID 92999924.
- ^ Elshourbagy NA, Near JC, Kmetz PJ, Wells TN, Groot PH, Saxty BA, et al. (March 1992). "Cloning and expression of a human ATP-citrate lyase cDNA". European Journal of Biochemistry. 204 (2): 491–9. doi:10.1111/j.1432-1033.1992.tb16659.x. PMID 1371749.
- ^ Cite error: The named reference
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was invoked but never defined (see the help page).
- ^ Fatland BL, Ke J, Anderson MD, Mentzen WI, Cui LW, Allred CC, et al. (October 2002). "Molecular characterization of a heteromeric ATP-citrate lyase that generates cytosolic acetyl-coenzyme A in Arabidopsis". Plant Physiology. 130 (2): 740–56. doi:10.1104/pp.008110. PMC 166603. PMID 12376641.