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Record Information
Version5.0
StatusDetected and Quantified
Creation Date2006-08-16 11:03:30 UTC
Update Date2022-03-07 02:49:05 UTC
HMDB IDHMDB0000657
Secondary Accession Numbers
  • HMDB00657
Metabolite Identification
Common NameCopper
Description
Structure
Data?1592420286
Synonyms
ValueSource
COPPER (II) ionChEBI
Copper(II) cationChEBI
Copper, ion (cu2+)ChEBI
Cu(II)ChEBI
Cu2+ChEBI
Cu(2+)ChEBI
Cupric ionChEBI
CuHMDB
Chemical FormulaCu
Average Molecular Weight63.546
Monoisotopic Molecular Weight62.929601079
IUPAC Namecopper(2+) ion
Traditional Namecopper(2+) ion
CAS Registry Number7440-50-8
SMILES
[Cu++]
InChI Identifier
InChI=1S/Cu/q+2
InChI KeyJPVYNHNXODAKFH-UHFFFAOYSA-N
Chemical Taxonomy
Description Belongs to the class of inorganic compounds known as homogeneous transition metal compounds. These are inorganic compounds containing only metal atoms,with the largest atom being a transition metal atom.
KingdomInorganic compounds
Super ClassHomogeneous metal compounds
ClassHomogeneous transition metal compounds
Sub ClassNot Available
Direct ParentHomogeneous transition metal compounds
Alternative ParentsNot Available
Substituents
  • Homogeneous transition metal
Molecular FrameworkNot Available
External Descriptors
Ontology
Not AvailableNot Available
Physical Properties
StateSolid
Experimental Molecular Properties
PropertyValueReference
Melting Point1083 °CNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Experimental Chromatographic PropertiesNot Available
Predicted Molecular Properties
PropertyValueSource
logP0.16ChemAxon
pKa (Strongest Acidic)3.09ChemAxon
Physiological Charge2ChemAxon
Hydrogen Acceptor Count0ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area0 ŲChemAxon
Rotatable Bond Count0ChemAxon
Refractivity0 m³·mol⁻¹ChemAxon
Polarizability1.78 ųChemAxon
Number of Rings0ChemAxon
BioavailabilityYesChemAxon
Rule of FiveYesChemAxon
Ghose FilterNoChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleNoChemAxon
Predicted Chromatographic Properties
Spectra

MS/MS Spectra

Spectrum TypeDescriptionSplash KeyDeposition DateSourceView
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Copper 10V, Positive-QTOFsplash10-03di-9000000000-59c652eccc13cc365f652016-08-01Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Copper 20V, Positive-QTOFsplash10-03di-9000000000-59c652eccc13cc365f652016-08-01Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Copper 40V, Positive-QTOFsplash10-03di-9000000000-59c652eccc13cc365f652016-08-01Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Copper 10V, Negative-QTOFsplash10-03di-9000000000-9acd78ab9faeb89677a72016-08-03Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Copper 20V, Negative-QTOFsplash10-03di-9000000000-9acd78ab9faeb89677a72016-08-03Wishart LabView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - Copper 40V, Negative-QTOFsplash10-03di-9000000000-9acd78ab9faeb89677a72016-08-03Wishart LabView Spectrum
Biological Properties
Cellular Locations
  • Cytoplasm (predicted from logP)
Biospecimen Locations
  • Blood
  • Cerebrospinal Fluid (CSF)
  • Saliva
  • Urine
Tissue Locations
  • Brain
  • Erythrocyte
  • Hair
  • Intestine
  • Kidney
  • Liver
Pathways
Normal Concentrations
Abnormal Concentrations
Associated Disorders and Diseases
Disease References
Multiple sclerosis
  1. Forte G, Visconti A, Santucci S, Ghazaryan A, Figa-Talamanca L, Cannoni S, Bocca B, Pino A, Violante N, Alimonti A, Salvetti M, Ristori G: Quantification of chemical elements in blood of patients affected by multiple sclerosis. Ann Ist Super Sanita. 2005;41(2):213-6. [PubMed:16244395 ]
Parkinson's disease
  1. Forte G, Alimonti A, Pino A, Stanzione P, Brescianini S, Brusa L, Sancesario G, Violante N, Bocca B: Metals and oxidative stress in patients with Parkinson's disease. Ann Ist Super Sanita. 2005;41(2):189-95. [PubMed:16244392 ]
Hyperzincaemia and hypercalprotectinaemia
  1. Isidor B, Poignant S, Corradini N, Fouassier M, Quartier P, Roth J, Picherot G: Hyperzincemia and hypercalprotectinemia: unsuccessful treatment with tacrolimus. Acta Paediatr. 2009 Feb;98(2):410-2. doi: 10.1111/j.1651-2227.2008.01092.x. Epub 2008 Nov 4. [PubMed:18983438 ]
Menkes disease
  1. Kaler SG, Das S, Levinson B, Goldstein DS, Holmes CS, Patronas NJ, Packman S, Gahl WA: Successful early copper therapy in Menkes disease associated with a mutant transcript containing a small In-frame deletion. Biochem Mol Med. 1996 Feb;57(1):37-46. [PubMed:8812725 ]
Aceruloplasminemia
  1. Roberti Mdo R, Borges Filho HM, Goncalves CH, Lima FL: Aceruloplasminemia: a rare disease - diagnosis and treatment of two cases. Rev Bras Hematol Hemoter. 2011;33(5):389-92. doi: 10.5581/1516-8484.20110104. [PubMed:23049345 ]
Congenital cataracts, hearing loss, and neurodegeneration
  1. Horvath R, Freisinger P, Rubio R, Merl T, Bax R, Mayr JA, Shawan, Muller-Hocker J, Pongratz D, Moller LB, Horn N, Jaksch M: Congenital cataract, muscular hypotonia, developmental delay and sensorineural hearing loss associated with a defect in copper metabolism. J Inherit Metab Dis. 2005;28(4):479-92. doi: 10.1007/s10545-005-0479-x. [PubMed:15902551 ]
Mental retardation, enteropathy, deafness, peripheral neuropathy, ichthyosis, and keratoderma
  1. Martinelli D, Travaglini L, Drouin CA, Ceballos-Picot I, Rizza T, Bertini E, Carrozzo R, Petrini S, de Lonlay P, El Hachem M, Hubert L, Montpetit A, Torre G, Dionisi-Vici C: MEDNIK syndrome: a novel defect of copper metabolism treatable by zinc acetate therapy. Brain. 2013 Mar;136(Pt 3):872-81. doi: 10.1093/brain/awt012. Epub 2013 Feb 18. [PubMed:23423674 ]
Occipital Horn Syndrome
  1. Kuivaniemi H, Peltonen L, Palotie A, Kaitila I, Kivirikko KI: Abnormal copper metabolism and deficient lysyl oxidase activity in a heritable connective tissue disorder. J Clin Invest. 1982 Mar;69(3):730-3. [PubMed:6120954 ]
Alzheimer's disease
  1. Molina JA, Jimenez-Jimenez FJ, Aguilar MV, Meseguer I, Mateos-Vega CJ, Gonzalez-Munoz MJ, de Bustos F, Porta J, Orti-Pareja M, Zurdo M, Barrios E, Martinez-Para MC: Cerebrospinal fluid levels of transition metals in patients with Alzheimer's disease. J Neural Transm (Vienna). 1998;105(4-5):479-88. [PubMed:9720975 ]
  2. Bocca B, Forte G, Petrucci F, Pino A, Marchione F, Bomboi G, Senofonte O, Giubilei F, Alimonti A: Monitoring of chemical elements and oxidative damage in patients affected by Alzheimer's disease. Ann Ist Super Sanita. 2005;41(2):197-203. [PubMed:16244393 ]
Wilson's disease
  1. Weisner B, Hartard C, Dieu C: CSF copper concentration: a new parameter for diagnosis and monitoring therapy of Wilson's disease with cerebral manifestation. J Neurol Sci. 1987 Jun;79(1-2):229-37. [PubMed:3612170 ]
  2. Patil M, Sheth KA, Krishnamurthy AC, Devarbhavi H: A review and current perspective on Wilson disease. J Clin Exp Hepatol. 2013 Dec;3(4):321-36. doi: 10.1016/j.jceh.2013.06.002. Epub 2013 Jul 6. [PubMed:25755520 ]
  3. Sócio D.A., et al. (2010). Wilson's disease in children and adolescents: diagnosis and treatment. Rev Paul Pediatr 28(2):134-40.. Rev Paul Pediatr.
Associated OMIM IDs
  • 126200 (Multiple sclerosis)
  • 168600 (Parkinson's disease)
  • 194470 (Hyperzincaemia and hypercalprotectinaemia)
  • 309400 (Menkes disease)
  • 604290 (Aceruloplasminemia)
  • 614482 (Congenital cataracts, hearing loss, and neurodegeneration)
  • 609313 (Mental retardation, enteropathy, deafness, peripheral neuropathy, ichthyosis, and keratoderma)
  • 304150 (Occipital Horn Syndrome)
  • 104300 (Alzheimer's disease)
  • 277900 (Wilson's disease)
DrugBank IDNot Available
Phenol Explorer Compound IDNot Available
FooDB IDFDB030749
KNApSAcK IDNot Available
Chemspider ID25221
KEGG Compound IDC00070
BioCyc IDCU%2b2
BiGG IDNot Available
Wikipedia LinkCopper
METLIN IDNot Available
PubChem Compound27099
PDB IDNot Available
ChEBI ID29036
Food Biomarker OntologyNot Available
VMH IDCU2
MarkerDB IDMDB00013431
Good Scents IDNot Available
References
Synthesis ReferenceNot Available
Material Safety Data Sheet (MSDS)Download (PDF)
General References

Only showing the first 10 proteins. There are 51 proteins in total.

Enzymes

General function:
Involved in oxidoreductase activity
Specific function:
This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6-dihydroxyindole to indole-5,6 quinone.
Gene Name:
TYR
Uniprot ID:
P14679
Molecular weight:
60392.69
General function:
Involved in monooxygenase activity
Specific function:
Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
Gene Name:
PAM
Uniprot ID:
P19021
Molecular weight:
108402.425
General function:
Involved in monooxygenase activity
Specific function:
Conversion of dopamine to noradrenaline.
Gene Name:
DBH
Uniprot ID:
P09172
Molecular weight:
69064.45
General function:
Involved in copper ion binding
Specific function:
Catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis. Placental DAO is thought to play a role in the regulation of the female reproductive function.
Gene Name:
ABP1
Uniprot ID:
P19801
Molecular weight:
85377.1
General function:
Involved in copper ion binding
Specific function:
Cell adhesion protein that participates in lymphocyte recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has a monoamine oxidase activity. May play a role in adipogenesis.
Gene Name:
AOC3
Uniprot ID:
Q16853
Molecular weight:
84621.27
General function:
Involved in copper ion binding
Specific function:
Has a monoamine oxidase activity with substrate specificity for 2-phenylethylamine and tryptamine. May play a role in adipogenesis. May be a critical modulator of signal transmission in retina.
Gene Name:
AOC2
Uniprot ID:
O75106
Molecular weight:
80515.11
General function:
Involved in oxidoreductase activity
Specific function:
Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.
Gene Name:
FTMT
Uniprot ID:
Q8N4E7
Molecular weight:
27537.885
General function:
Involved in oxidoreductase activity
Specific function:
Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity).
Gene Name:
CP
Uniprot ID:
P00450
Molecular weight:
122204.45
General function:
Involved in copper ion binding
Specific function:
Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. In addition to cross-linking of extracellular matrix proteins, may have a direct role in tumor suppression.
Gene Name:
LOX
Uniprot ID:
P28300
Molecular weight:
46943.67
General function:
Involved in iron ion binding
Specific function:
Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
Gene Name:
MT-CO1
Uniprot ID:
P00395
Molecular weight:
57040.91

Transporters

General function:
Involved in ATP binding
Specific function:
Involved in the export of copper out of the cells, such as the efflux of hepatic copper into the bile.
Gene Name:
ATP7B
Uniprot ID:
P35670
Molecular weight:
157261.34
General function:
Involved in ATP binding
Specific function:
May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells.
Gene Name:
ATP7A
Uniprot ID:
Q04656
Molecular weight:
163372.275
General function:
Involved in copper ion transmembrane transporter activity
Specific function:
Involved in high-affinity copper uptake
Gene Name:
SLC31A1
Uniprot ID:
O15431
Molecular weight:
21090.5
General function:
Involved in copper ion transmembrane transporter activity
Specific function:
Involved in low-affinity copper uptake (Potential)
Gene Name:
SLC31A2
Uniprot ID:
O15432
Molecular weight:
15681.3

Only showing the first 10 proteins. There are 51 proteins in total.