<?xml version="1.0" encoding="UTF-8"?>
<compound>
  <id type="integer">1233</id>
  <title>T3D1229</title>
  <common-name>Copper acetylacetonate</common-name>
  <description>Copper acetylacetonate is a solid compound with the formula C10H14CuO4 and an average molecular weight of 261.76 g/mol. Copper acetylacetonate belongs to the carbonyl compounds, a subclass of organooxygen compounds within the organic compounds. This exogenous substance is used as an industrial catalyst. It has been recorded in sources including ladders in building and construction, as well as electrical and electronic equipment such as antennas, amplifiers, coils, auxiliary devices, and communication cables or conductors.

The compound interacts with several protein targets. Copper binds to alpha-synuclein (SNCA), which initiates protein aggregation and likely contributes to the development of Alzheimer's disease and Parkinson's disease. It also binds the N-terminal region of amyloid-beta precursor protein (APP), promoting the generation of beta-amyloid, which is believed to contribute to the development of Alzheimer's disease and Parkinson's disease. Additionally, copper inhibits sulfhydryl group enzymes that protect the cell from free oxygen, specifically serum paraoxonase/lactonase 3 (PON3), serum paraoxonase/arylesterase 1 (PON1), mitochondrial glutathione reductase (GSR), and glucose-6-phosphate 1-dehydrogenase (G6PD). Copper hepatotoxicity is believed to occur when copper accumulates in the nucleus and lysosomes become saturated, causing nuclear damage possibly resulting from oxidative damage and lipid peroxidation. In this process, excess copper is complexed with metallothionein within hepatocyte lysosomes.</description>
  <cas>13395-16-9</cas>
  <pubchem-id>11149677</pubchem-id>
  <chemical-formula>C10H14CuO4</chemical-formula>
  <weight>261.018810</weight>
  <appearance>Blue powder.</appearance>
  <melting-point></melting-point>
  <boiling-point nil="true"/>
  <density nil="true"/>
  <solubility></solubility>
  <specific-gravity nil="true"/>
  <flash-point nil="true"/>
  <vapour-pressure nil="true"/>
  <route-of-exposure>Oral  (L277) ; inhalation  (L277) ; dermal (L277)</route-of-exposure>
  <target nil="true"/>
  <mechanism-of-toxicity>Excess copper is sequestered within hepatocyte lysosomes, where it is complexed with metallothionein. Copper hepatotoxicity is believed to occur when the lysosomes become saturated and copper accumulates in the nucleus, causing nuclear damage. This damage is possibly a result of oxidative damage, including lipid peroxidation. Copper inhibits the sulfhydryl group enzymes such as glucose-6-phosphate 1-dehydrogenase, glutathione reductase, and paraoxonases, which protect the cell from free oxygen radicals. It also influences gene expression and is a co-factor for oxidative enzymes such as cytochrome C oxidase and lysyl oxidase. In addition, the oxidative stress induced by copper is thought to activate acid sphingomyelinase, which lead to the production of ceramide, an apoptotic signal, as well as cause hemolytic anemia. Copper-induced emesis results from stimulation of the vagus nerve. (L277, T49, A174, L280)</mechanism-of-toxicity>
  <metabolism>Copper is mainly absorbed through the gastrointestinal tract, but it can also be inhalated and absorbed dermally. It passes through the basolateral membrane, possibly via regulatory copper transporters, and is transported to the liver and kidney bound to serum albumin. The liver is the critical organ for copper homoeostasis. In the liver and other tissues, copper is stored bound to metallothionein, amino acids, and in association with copper-dependent enzymes, then partitioned for excretion through the bile or incorporation into intra- and extracellular proteins. The transport of copper to the peripheral tissues is accomplished through the plasma attached to serum albumin, ceruloplasmin or low-molecular-weight complexes. Copper may induce the production of metallothionein and ceruloplasmin. The membrane-bound copper transporting adenosine triphosphatase (Cu-ATPase) transports copper ions into and out of cells. Physiologically normal levels of copper in the body are held constant by alterations in the rate and amount of copper absorption, compartmental distribution, and excretion. (L277, L279)</metabolism>
  <toxicity nil="true"/>
  <lethaldose>10 to 20 grams for an adult human (copper salts). (T17)</lethaldose>
  <carcinogenicity>No indication of carcinogenicity to humans (not listed by IARC).</carcinogenicity>
  <use-source nil="true"/>
  <min-risk-level>Acute Oral: 0.01 mg/kg/day (L134) 
Intermediate Oral: 0.01 mg/kg/day (L134)</min-risk-level>
  <health-effects>People must absorb small amounts of copper every day because copper is essential for good health, however, high levels of copper can be harmful. Very-high doses of copper can cause damage to your liver and kidneys, and can even cause death. Copper may induce allergic responses in sensitive individuals. (L278, L279)</health-effects>
  <symptoms>Breathing high levels of copper can cause irritation of the nose and throat. Ingesting high levels of copper can cause nausea, vomiting, diarrhea, headache, dizziness, and respiratory difficulty. (L278, L279)</symptoms>
  <treatment nil="true"/>
  <created-at type="dateTime">2009-06-19T21:58:29Z</created-at>
  <updated-at type="dateTime">2026-04-06T12:55:17Z</updated-at>
  <interacting-proteins>High affinity copper uptake protein 1 (O15431) Probable low affinity copper uptake protein 2 (O15432) Serum albumin (P02768) Ceruloplasmin (P00450) Copper-transporting ATPase 1 (Q04656) Copper-transporting ATPase 2 (P35670) Copper transport protein ATOX1 (O00244) Copper chaperone for superoxide dismutase (O14618) Cytochrome c oxidase copper chaperone (Q14061) Metallothionein-2 (P02795) Metallothionein-1G (P13640) Metallothionein-1H (P80294) Metallothionein-3 (P25713) Metallothionein-1F (P04733) Metallothionein-1E (P04732) Metallothionein-1X (P80297) Metallothionein-1A (P04731) Metallothionein-1B (P07438) Metallothionein-1M (Q8N339) Metallothionein-4 (P47944) Metallothionein-1L (Q93083) (L277, A176)</interacting-proteins>
  <wikipedia nil="true"/>
  <uniprot-id nil="true"/>
  <kegg-compound-id></kegg-compound-id>
  <omim-id></omim-id>
  <chebi-id></chebi-id>
  <biocyc-id>CUSO4</biocyc-id>
  <ctd-id nil="true"/>
  <stitch-id>Copper acetylacetonate</stitch-id>
  <drugbank-id nil="true"/>
  <pdb-id nil="true"/>
  <actor-id nil="true"/>
  <organism nil="true"/>
  <export type="boolean">true</export>
  <metabolizing-proteins nil="true"/>
  <transporting-proteins>High affinity copper uptake protein 1 (O15431) 
Probable low affinity copper uptake protein 2 (O15432) 
Serum albumin (P02768) 
Ceruloplasmin (P00450) 
Copper-transporting ATPase 1 (Q04656) 
Copper-transporting ATPase 2 (P35670) 
Copper transport protein ATOX1 (O00244) 
Copper chaperone for superoxide dismutase (O14618) 
Cytochrome c oxidase copper chaperone (Q14061) 
Metallothionein-2 (P02795) 
Metallothionein-1G (P13640) 
Metallothionein-1H (P80294) 
Metallothionein-3 (P25713) 
Metallothionein-1F (P04733) 
Metallothionein-1E (P04732) 
Metallothionein-1X (P80297) 
Metallothionein-1A (P04731) 
Metallothionein-1B (P07438) 
Metallothionein-1M (Q8N339) 
Metallothionein-4 (P47944) 
Metallothionein-1L (Q93083) 
(L277, A176)</transporting-proteins>
  <moldb-smiles>CC(=O)\C=C(\C)O[Cu]O\C(C)=C\C(C)=O</moldb-smiles>
  <moldb-formula>C10H14CuO4</moldb-formula>
  <moldb-inchi>InChI=1S/2C5H8O2.Cu/c2*1-4(6)3-5(2)7;/h2*3,6H,1-2H3;/q;;+2/p-2/b4-3+;4-3-;</moldb-inchi>
  <moldb-inchikey>QYJPSWYYEKYVEJ-OHSCNOFNSA-L</moldb-inchikey>
  <moldb-average-mass type="decimal">261.762</moldb-average-mass>
  <moldb-mono-mass type="decimal">261.018810015</moldb-mono-mass>
  <origin>Exogenous</origin>
  <state>Solid</state>
  <logp nil="true"/>
  <hmdb-id nil="true"/>
  <chembl-id nil="true"/>
  <chemspider-id>30780125</chemspider-id>
  <structure-image-file-name nil="true"/>
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  <structure-image-file-size type="integer" nil="true"/>
  <structure-image-updated-at type="dateTime" nil="true"/>
  <biodb-id nil="true"/>
  <synthesis-reference></synthesis-reference>
  <structure-image-caption nil="true"/>
  <chemdb-id>CHEM001052</chemdb-id>
  <dsstox-id nil="true"/>
  <toxcast-id nil="true"/>
  <stoff-ident-origin nil="true"/>
  <stoff-ident-id nil="true"/>
  <susdat-id>NS00124868</susdat-id>
  <iupac nil="true"/>
  <moldb-polar-surface-area>52.6</moldb-polar-surface-area>
  <moldb-refractivity>54.84980000000001</moldb-refractivity>
  <moldb-polarizability>22.45644403263839</moldb-polarizability>
  <moldb-rotatable-bond-count>6</moldb-rotatable-bond-count>
  <moldb-acceptor-count>4</moldb-acceptor-count>
  <moldb-donor-count>0</moldb-donor-count>
  <moldb-pka-strongest-acidic>19.13614049234866</moldb-pka-strongest-acidic>
  <moldb-pka-strongest-basic>-4.622114548650297</moldb-pka-strongest-basic>
  <moldb-physiological-charge>0</moldb-physiological-charge>
  <moldb-number-of-rings>0</moldb-number-of-rings>
  <moldb-alogps-logp>1.08</moldb-alogps-logp>
  <moldb-alogps-logs>-1.96</moldb-alogps-logs>
  <moldb-alogps-solubility>2.90e+00 g/l</moldb-alogps-solubility>
  <kingdom>Organic compounds</kingdom>
  <superklass>Organic oxygen compounds</superklass>
  <klass>Organooxygen compounds</klass>
  <subklass>Carbonyl compounds</subklass>
  <paper-count type="integer">27</paper-count>
  <sync-id>CED0011843</sync-id>
  <structure-inchikey>QYJPSWYYEKYVEJ-OHSCNOFNSA-L</structure-inchikey>
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</structure-pickle>
  <structure-indexed-at type="dateTime">2026-09-19T04:00:02Z</structure-indexed-at>
</compound>
