2.0 2012-05-31 10:28:18 -0600 2015-09-13 12:56:08 -0600 ECMDB00657 M2MDB000166 Copper Copper 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) Copper Cu Cu++ Cu+2 Cu<SUP>++</SUP> Cu<SUP>+2</SUP> Cupric copper Cupric ion Cu 63.546 62.929601079 copper(2+) ion copper(2+) ion 7440-50-8 [Cu++] InChI=1S/Cu/q+2 JPVYNHNXODAKFH-UHFFFAOYSA-N Solid Cytosol Extra-organism Periplasm melting_point 1083 oC logp 0.16 ChemAxon pka_strongest_acidic 3.09 ChemAxon iupac copper(2+) ion ChemAxon average_mass 63.546 ChemAxon mono_mass 62.929601079 ChemAxon smiles [Cu++] ChemAxon formula Cu ChemAxon inchi InChI=1S/Cu/q+2 ChemAxon inchikey JPVYNHNXODAKFH-UHFFFAOYSA-N ChemAxon polar_surface_area 0 ChemAxon refractivity 0 ChemAxon polarizability 1.78 ChemAxon rotatable_bond_count 0 ChemAxon acceptor_count 0 ChemAxon donor_count 0 ChemAxon physiological_charge 2 ChemAxon formal_charge 2 ChemAxon Oxidative phosphorylation The 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. PW000919 ec00190 Metabolic Two-component system ec02020 Phenylethylamine metabolism The 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. PW002027 Metabolic L-threonine degradation to methylglyoxal L-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. PW002106 Metabolic Specdb::MsMs 61950 Specdb::MsMs 61951 Specdb::MsMs 61952 Specdb::MsMs 118584 Specdb::MsMs 118585 Specdb::MsMs 118586 HMDB00657 23978 25221 C00070 30052 CU+2 CU Copper Keseler, 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. 21097882 Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). 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Eur J Gastroenterol Hepatol. 2006 Jan;18(1):43-7. 16357618 Kodama 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. 16435190 Cengiz 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. 14997023 Langner C, Denk H: Wilson disease. Virchows Arch. 2004 Aug;445(2):111-8. Epub 2004 Jun 17. 15205951 Kitzberger R, Madl C, Ferenci P: Wilson disease. Metab Brain Dis. 2005 Dec;20(4):295-302. 16382340 Chen 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. 17079463 Briviba 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. 15113949 Pizent 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. 14968933 Squitti 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. 16832081 Odland 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. 15253483 Venelinov 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. 14991216 Attri 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. 16549536 Jablonska-Kaszewska I, Dabrowska E, Drobinska Jurowiecka A, Falkiewicz B: Treatment of Wilson's disease. Med Sci Monit. 2003 Aug;9 Suppl 3:5-8. 15156602 Daniel KG, Harbach RH, Guida WC, Dou QP: Copper storage diseases: Menkes, Wilsons, and cancer. Front Biosci. 2004 Sep 1;9:2652-62. 15358588 Aoki 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. 15773321 Meng 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. 15511628 Gorter 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. 15543084 http://hmdb.ca/system/metabolites/msds/000/000/576/original/HMDB00657.pdf?1358893949 NADH dehydrogenase P00393 DHNA_ECOLI ndh http://ecmdb.ca/proteins/P00393.xml Molybdopterin synthase sulfur carrier subunit P30748 MOAD_ECOLI moaD http://ecmdb.ca/proteins/P30748.xml Molybdopterin synthase catalytic subunit P30749 MOAE_ECOLI moaE http://ecmdb.ca/proteins/P30749.xml Blue copper oxidase cueO P36649 CUEO_ECOLI cueO http://ecmdb.ca/proteins/P36649.xml Lead, cadmium, zinc and mercury-transporting ATPase P37617 ATZN_ECOLI zntA http://ecmdb.ca/proteins/P37617.xml Copper-exporting P-type ATPase A Q59385 COPA_ECOLI copA http://ecmdb.ca/proteins/Q59385.xml Molybdopterin molybdenumtransferase P12281 MOEA_ECOLI moeA http://ecmdb.ca/proteins/P12281.xml Zinc transporter zupT P0A8H3 ZUPT_ECOLI zupT http://ecmdb.ca/proteins/P0A8H3.xml Cation efflux system protein cusB P77239 CUSB_ECOLI cusB http://ecmdb.ca/proteins/P77239.xml Outer membrane protein N P77747 OMPN_ECOLI ompN http://ecmdb.ca/proteins/P77747.xml Cation efflux system protein cusA P38054 CUSA_ECOLI cusA http://ecmdb.ca/proteins/P38054.xml Outer membrane pore protein E P02932 PHOE_ECOLI phoE http://ecmdb.ca/proteins/P02932.xml Cation efflux system protein cusF P77214 CUSF_ECOLI cusF http://ecmdb.ca/proteins/P77214.xml Cation efflux system protein cusC P77211 CUSC_ECOLI cusC http://ecmdb.ca/proteins/P77211.xml Outer membrane protein F P02931 OMPF_ECOLI ompF http://ecmdb.ca/proteins/P02931.xml Outer membrane protein C P06996 OMPC_ECOLI ompC http://ecmdb.ca/proteins/P06996.xml Cyclic pyranopterin monophosphate + Copper + 2 MoaD Protein with thiocarboxylate >5 Hydrogen ion +2 MoaD Protein with carboxylate + Molybdopterin 4 Copper + 4 Hydrogen ion + Oxygen >4 Copper +2 Water 4 Copper + 4 Hydrogen ion + Oxygen >4 Copper +2 Water Adenosine triphosphate + Copper + Water > ADP + Hydrogen ion + Phosphate + Copper Adenosine triphosphate + Copper + Water > ADP + Hydrogen ion + Phosphate + Copper Molybdopterin + Adenylated molybdopterin > Adenosine monophosphate + bis-molybdenum cofactor + Copper Adenylated molybdopterin + tungsten binding cofactor > Adenosine monophosphate + tungsten bispterin cofactor + Copper 2 Hydrogen ion + Molybdate + Adenylated molybdopterin > Adenosine monophosphate + Copper + Water + Molybdopterin 2 Hydrogen ion + Adenylated molybdopterin + Tungstate > Adenosine monophosphate + Copper + Water + tungsten binding cofactor NADH + Copper Hydrogen ion + NAD + Cu<SUP>+</SUP> R170-RXN Cu<SUP>+</SUP> + Hydrogen ion + Oxygen > Copper + Water RXN0-2945 Copper + NADH > NAD + Cu(+) PW_R003845 4000.0 uM 0.0 K-12 16000000 0 1. 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.