2.02012-05-31 10:28:18 -06002015-09-13 12:56:08 -0600ECMDB00657M2MDB000166CopperCopper is s a ductile metal with very high thermal and electrical conductivity. Pure copper is soft and malleable; a freshly exposed surface has a reddish-orange color. The catalytic activity of copper is used by the enzymes that it is associated with and is thus only toxic when unsequestered and unmediated. Copper(II) ions are water-soluble, where they function at low concentration as bacteriostatic substances, fungicides, and wood preservatives.Ci(II)CopperCuCu++Cu+2Cu<SUP>++</SUP>Cu<SUP>+2</SUP>Cupric copperCupric ionCu63.54662.929601079copper(2+) ioncopper(2+) ion7440-50-8[Cu++]InChI=1S/Cu/q+2JPVYNHNXODAKFH-UHFFFAOYSA-NSolidCytosolExtra-organismPeriplasmmelting_point1083 oClogp0.16pka_strongest_acidic3.09iupaccopper(2+) ionaverage_mass63.546mono_mass62.929601079smiles[Cu++]formulaCuinchiInChI=1S/Cu/q+2inchikeyJPVYNHNXODAKFH-UHFFFAOYSA-Npolar_surface_area0refractivity0polarizability1.78rotatable_bond_count0acceptor_count0donor_count0physiological_charge2formal_charge2Oxidative phosphorylationThe process of oxidative phosphorylation involves multiple interactions of ubiquinone with succinic acid, resulting in a fumaric acid and ubiquinol.
Ubiquinone interacts with succinic acid through a succinate:quinone oxidoreductase resulting in a fumaric acid an ubiquinol. This enzyme has various cofactors, ferroheme b, 2FE-2S, FAD, and 3Fe-4S iron-sulfur cluster.
Then 2 ubiquinol interact with oxygen and 4 hydrogen ion through a cytochrome bd-I terminal oxidase resulting in a 4 hydrogen ion transferred into the periplasmic space, 2 water returned into the cytoplasm and 2 ubiquinone, which stay in the inner membrane.
The ubiquinone interacts with succinic acid through a succinate:quinone oxidoreductase resulting in a fumaric acid an ubiquinol.
Then 2 ubiquinol interacts with oxygen and 4 hydrogen ion through a cytochrome bd-II terminal oxidase resulting in a 4 hydrogen ion transferred into the periplasmic space, 2 water returned into the cytoplasm and 2 ubiquinone, which stay in the inner membrane.
The ubiquinone interacts with succinic acid through a succinate:quinone oxidoreductase resulting in a fumaric acid an ubiquinol.
The 2 ubiquinol interact with oxygen and 8 hydrogen ion through a cytochrome bo terminal oxidase resulting in a 8 hydrogen ion transferred into the periplasmic space, 2 water returned into the cytoplasm and 2 ubiquinone, which stays in the inner membrane.
The ubiquinone then interacts with 5 hydrogen ion through a NADH dependent ubiquinone oxidoreductase I resulting in NAD, hydrogen ion released into the periplasmic space and an ubiquinol.
The ubiquinol is then processed reacting with oxygen, and 4 hydrogen through a ion cytochrome bd-I terminal oxidase resulting in 4 hydrogen ions released into the periplasmic space, 2 water molecules into the cytoplasm and 2 ubiquinones.
The ubiquinone then interacts with 5 hydrogen ion through a NADH dependent ubiquinone oxidoreductase I resulting in NAD, hydrogen ion released into the periplasmic space and an ubiquinol.
The 2 ubiquinol interact with oxygen and 8 hydrogen ion through a cytochrome bo terminal oxidase resulting in a 8 hydrogen ion transferred into the periplasmic space, 2 water returned into the cytoplasm and 2 ubiquinone, which stays in the inner membrane.
PW000919ec00190MetabolicTwo-component systemec02020Phenylethylamine metabolismThe process of phenylethylamine metabolism starts with 2-phenylethylamine interacting with an oxygen molecule and a water molecule in the periplasmic space through a phenylethylamine oxidase. This reaction results in the release of a hydrogen peroxide, ammonium and phenylacetaldehyde.
Phenylacetaldehyde is introduced into the cytosol and degraded into phenylacetate by reaction with a phenylacetaldehyde dehydrogenase. This reaction involves phenylacetaldehyde interacting with NAD, and a water molecule and then resulting in the release of NADH, and 2 hydrogen ion.
Phenylacetate is then degraded. The first step involves phenylacetate interacting with an coenzyme A and an ATP driven phenylacetate-CoA ligase resulting in the release of a AMP, a diphosphate and a phenylacetyl-CoA. This resulting compound the interacts with a hydrogen ion, NADPH, and oxygen molecule through a ring 1,2-phenylacetyl-CoA epoxidase protein complex resulting in the release of a water molecule, an NADP and a 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA. This compound is then metabolized by a ring 1,2 epoxyphenylacetyl-CoA isomerase resulting in a 2-oxepin-2(3H)-ylideneacetyl-CoA. This compound is then hydrolated through a oxepin-CoA hydrolase resulting in a 3-oxo-5,6-didehydrosuberyl-CoA semialdehyde. This commpound then interacts with a water molecule and NADP driven 3-oxo-5,6-dehydrosuberyl-CoA semialadehyde dehydrogenase resulting in 2 hydrogen ions, a NADPH and a 3-oxo-5,6-didehydrosuberyl-CoA. The resulting compound interacts with a coenzyme A and a 3-oxo-5,6 dehydrosuberyl-CoA thiolase resulting in an acetyl-CoA and a 2,3-didehydroadipyl-CoA. This resulting compound is the hydrated by a 2,3-dehydroadipyl-CoA hydratas resulting in a 3-hydroxyadipyl-CoA whuch is dehydrogenated through an NAD driven 3-hydroxyadipyl-CoA dehydrogenase resulting in a NADH, a hydrogen ion and a 3-oxoadipyl-CoA. The latter compound then interacts with conezyme A through a beta-ketoadipyl-CoA thiolase resulting in an acetyl-CoA and a succinyl-CoA. The succinyl-CoA is then integrated into the TCA cycle.PW002027MetabolicL-threonine degradation to methylglyoxalL-threonine is degrade into methylglyoxal (pyruvaldehyde) by first reacting with a NDA dependent threonine dehydrogenase resulting in the release of a hydrogen ion, an NADH and a 2-amino-3-oxobutanoate. The latter compound reacts spontaneously with a hydrogen ion resulting in the release of a carbon dioxide and a aminoacetone. The aminoacetone in turn reacts with an oxygen and a water molecule through an aminoacetone oxidase resulting in the release of a hydrogen peroxide, ammonium and a methylglyoxal which can then be incorporated in the methylglyoxal degradation pathways.PW002106MetabolicSpecdb::MsMs61950Specdb::MsMs61951Specdb::MsMs61952Specdb::MsMs118584Specdb::MsMs118585Specdb::MsMs118586HMDB006572397825221C0007030052CU+2CUCopperKeseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590.21097882Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114.22080510Kedzierska E: [Concentrations of selected bioelements and toxic metals and their influence on health status of children and youth residing in Szczecin] Ann Acad Med Stetin. 2003;49:131-43.15552844Koury JC, de Olilveria AV Jr, Portella ES, de Olilveria CF, Lopes GC, Donangelo CM: Zinc and copper biochemical indices of antioxidant status in elite athletes of different modalities. Int J Sport Nutr Exerc Metab. 2004 Jun;14(3):358-72.15256695Hoogenraad TU: Paradigm shift in treatment of Wilson's disease: zinc therapy now treatment of choice. Brain Dev. 2006 Apr;28(3):141-6. Epub 2006 Feb 7.16466879Dib N, Valsesia E, Malinge MC, Mauras Y, Misrahi M, Cales P: Late onset of Wilson's disease in a family with genetic haemochromatosis. Eur J Gastroenterol Hepatol. 2006 Jan;18(1):43-7.16357618Kodama H, Sato E, Gu YH, Shiga K, Fujisawa C, Kozuma T: Effect of copper and diethyldithiocarbamate combination therapy on the macular mouse, an animal model of Menkes disease. J Inherit Metab Dis. 2005;28(6):971-8.16435190Cengiz B, Soylemez F, Ozturk E, Cavdar AO: Serum zinc, selenium, copper, and lead levels in women with second-trimester induced abortion resulting from neural tube defects: a preliminary study. Biol Trace Elem Res. 2004 Mar;97(3):225-35.14997023Langner C, Denk H: Wilson disease. Virchows Arch. 2004 Aug;445(2):111-8. Epub 2004 Jun 17.15205951Kitzberger R, Madl C, Ferenci P: Wilson disease. Metab Brain Dis. 2005 Dec;20(4):295-302.16382340Chen D, Cui QC, Yang H, Dou QP: Disulfiram, a clinically used anti-alcoholism drug and copper-binding agent, induces apoptotic cell death in breast cancer cultures and xenografts via inhibition of the proteasome activity. Cancer Res. 2006 Nov 1;66(21):10425-33.17079463Briviba K, Schnabele K, Rechkemmer G, Bub A: Supplementation of a diet low in carotenoids with tomato or carrot juice does not affect lipid peroxidation in plasma and feces of healthy men. J Nutr. 2004 May;134(5):1081-3.15113949Pizent A, Jurasovic J, Telisman S: Serum calcium, zinc, and copper in relation to biomarkers of lead and cadmium in men. J Trace Elem Med Biol. 2003;17(3):199-205.14968933Squitti R, Barbati G, Rossi L, Ventriglia M, Dal Forno G, Cesaretti S, Moffa F, Caridi I, Cassetta E, Pasqualetti P, Calabrese L, Lupoi D, Rossini PM: Excess of nonceruloplasmin serum copper in AD correlates with MMSE, CSF [beta]-amyloid, and h-tau. Neurology. 2006 Jul 11;67(1):76-82.16832081Odland JO, Nieboer E, Romanova N, Thomassen Y: Elements in placenta and pregnancy outcome in arctic and subarctic areas. Int J Circumpolar Health. 2004 May;63(2):169-87.15253483Venelinov TI, Davies IM, Beattie JH: Dialysis-Chelex method for determination of exchangeable copper in human plasma. Anal Bioanal Chem. 2004 Jul;379(5-6):777-80. Epub 2004 Feb 26.14991216Attri S, Sharma N, Jahagirdar S, Thapa BR, Prasad R: Erythrocyte metabolism and antioxidant status of patients with Wilson disease with hemolytic anemia. Pediatr Res. 2006 Apr;59(4 Pt 1):593-7.16549536Jablonska-Kaszewska I, Dabrowska E, Drobinska Jurowiecka A, Falkiewicz B: Treatment of Wilson's disease. Med Sci Monit. 2003 Aug;9 Suppl 3:5-8.15156602Daniel KG, Harbach RH, Guida WC, Dou QP: Copper storage diseases: Menkes, Wilsons, and cancer. Front Biosci. 2004 Sep 1;9:2652-62.15358588Aoki T: [Genetic disorders of copper transport--diagnosis and new treatment for the patients of Wilson's disease] No To Hattatsu. 2005 Mar;37(2):99-109.15773321Meng Y, Miyoshi I, Hirabayashi M, Su M, Mototani Y, Okamura T, Terada K, Ueda M, Enomoto K, Sugiyama T, Kasai N: Restoration of copper metabolism and rescue of hepatic abnormalities in LEC rats, an animal model of Wilson disease, by expression of human ATP7B gene. Biochim Biophys Acta. 2004 Nov 5;1690(3):208-19.15511628Gorter RW, Butorac M, Cobian EP: Examination of the cutaneous absorption of copper after the use of copper-containing ointments. Am J Ther. 2004 Nov-Dec;11(6):453-8.15543084http://hmdb.ca/system/metabolites/msds/000/000/576/original/HMDB00657.pdf?1358893949NADH dehydrogenaseP00393DHNA_ECOLIndhhttp://ecmdb.ca/proteins/P00393.xmlMolybdopterin synthase sulfur carrier subunitP30748MOAD_ECOLImoaDhttp://ecmdb.ca/proteins/P30748.xmlMolybdopterin synthase catalytic subunitP30749MOAE_ECOLImoaEhttp://ecmdb.ca/proteins/P30749.xmlBlue copper oxidase cueOP36649CUEO_ECOLIcueOhttp://ecmdb.ca/proteins/P36649.xmlLead, cadmium, zinc and mercury-transporting ATPaseP37617ATZN_ECOLIzntAhttp://ecmdb.ca/proteins/P37617.xmlCopper-exporting P-type ATPase AQ59385COPA_ECOLIcopAhttp://ecmdb.ca/proteins/Q59385.xmlMolybdopterin molybdenumtransferaseP12281MOEA_ECOLImoeAhttp://ecmdb.ca/proteins/P12281.xmlZinc transporter zupTP0A8H3ZUPT_ECOLIzupThttp://ecmdb.ca/proteins/P0A8H3.xmlCation efflux system protein cusBP77239CUSB_ECOLIcusBhttp://ecmdb.ca/proteins/P77239.xmlOuter membrane protein NP77747OMPN_ECOLIompNhttp://ecmdb.ca/proteins/P77747.xmlCation efflux system protein cusAP38054CUSA_ECOLIcusAhttp://ecmdb.ca/proteins/P38054.xmlOuter membrane pore protein EP02932PHOE_ECOLIphoEhttp://ecmdb.ca/proteins/P02932.xmlCation efflux system protein cusFP77214CUSF_ECOLIcusFhttp://ecmdb.ca/proteins/P77214.xmlCation efflux system protein cusCP77211CUSC_ECOLIcusChttp://ecmdb.ca/proteins/P77211.xmlOuter membrane protein FP02931OMPF_ECOLIompFhttp://ecmdb.ca/proteins/P02931.xmlOuter membrane protein CP06996OMPC_ECOLIompChttp://ecmdb.ca/proteins/P06996.xmlCyclic pyranopterin monophosphate + Copper + 2 MoaD Protein with thiocarboxylate >5 Hydrogen ion +2 MoaD Protein with carboxylate + Molybdopterin4 Copper + 4 Hydrogen ion + Oxygen >4 Copper +2 Water4 Copper + 4 Hydrogen ion + Oxygen >4 Copper +2 WaterAdenosine triphosphate + Copper + Water > ADP + Hydrogen ion + Phosphate + CopperAdenosine triphosphate + Copper + Water > ADP + Hydrogen ion + Phosphate + CopperMolybdopterin + Adenylated molybdopterin > Adenosine monophosphate + bis-molybdenum cofactor + CopperAdenylated molybdopterin + tungsten binding cofactor > Adenosine monophosphate + tungsten bispterin cofactor + Copper2 Hydrogen ion + Molybdate + Adenylated molybdopterin > Adenosine monophosphate + Copper + Water + Molybdopterin2 Hydrogen ion + Adenylated molybdopterin + Tungstate > Adenosine monophosphate + Copper + Water + tungsten binding cofactorNADH + Copper Hydrogen ion + NAD + Cu<SUP>+</SUP>R170-RXNCu<SUP>+</SUP> + Hydrogen ion + Oxygen > Copper + WaterRXN0-2945Copper + NADH > NAD + Cu(+)PW_R0038454000.0uM0.0K-121600000001. Cybercell Database: <a href='http://ccdb.wishartlab.com/CCDB/cgi-bin/STAT_NEW.cgi'>http://ccdb.wishartlab.com/CCDB/cgi-bin/STAT_NEW.cgi</a> <br>
2. Phillips R., Kondev, J., Theriot, J. (2008) “Physical Biology of the Cell” Garland Science, New York, NY.