2.0 2012-05-31 13:55:48 -0600 2015-06-03 15:54:15 -0600 ECMDB02158 M2MDB000442 Coproporphyrinogen I Coproporphyrinogen is formed by Uroporphyrinogen decarboxylase from Uroporphyrinogen by decarboxylation of 4 acetates. 3,8,13,18-Tetramethyl-5,10,15,20,22,24-hexahydroporphyrin-2,7,12,17-tetrapropanoate 3,8,13,18-Tetramethyl-5,10,15,20,22,24-hexahydroporphyrin-2,7,12,17-tetrapropanoic acid C36H44N4O8 660.7566 660.315914404 3-[9,14,19-tris(2-carboxyethyl)-5,10,15,20-tetramethyl-21,22,23,24-tetraazapentacyclo[16.2.1.1³,⁶.1⁸,¹¹.1¹³,¹⁶]tetracosa-1(20),3,5,8,10,13,15,18-octaen-4-yl]propanoic acid coproporphyrinogen I 31110-56-2 CC1=C2CC3=C(CCC(O)=O)C(C)=C(CC4=C(CCC(O)=O)C(C)=C(CC5=C(CCC(O)=O)C(C)=C(CC(N2)=C1CCC(O)=O)N5)N4)N3 InChI=1S/C36H44N4O8/c1-17-21(5-9-33(41)42)29-14-26-19(3)23(7-11-35(45)46)31(39-26)16-28-20(4)24(8-12-36(47)48)32(40-28)15-27-18(2)22(6-10-34(43)44)30(38-27)13-25(17)37-29/h37-40H,5-16H2,1-4H3,(H,41,42)(H,43,44)(H,45,46)(H,47,48) WIUGGJKHYQIGNH-UHFFFAOYSA-N Solid Inner membrane Membrane Outer membrane logp 1.97 ALOGPS logs -4.77 ALOGPS solubility 1.11e-02 g/l ALOGPS melting_point 171 - 174 oC logp 4.89 ChemAxon pka_strongest_acidic 3.85 ChemAxon iupac 3-[9,14,19-tris(2-carboxyethyl)-5,10,15,20-tetramethyl-21,22,23,24-tetraazapentacyclo[16.2.1.1³,⁶.1⁸,¹¹.1¹³,¹⁶]tetracosa-1(20),3,5,8,10,13,15,18-octaen-4-yl]propanoic acid ChemAxon average_mass 660.7566 ChemAxon mono_mass 660.315914404 ChemAxon smiles CC1=C2CC3=C(CCC(O)=O)C(C)=C(CC4=C(CCC(O)=O)C(C)=C(CC5=C(CCC(O)=O)C(C)=C(CC(N2)=C1CCC(O)=O)N5)N4)N3 ChemAxon formula C36H44N4O8 ChemAxon inchi InChI=1S/C36H44N4O8/c1-17-21(5-9-33(41)42)29-14-26-19(3)23(7-11-35(45)46)31(39-26)16-28-20(4)24(8-12-36(47)48)32(40-28)15-27-18(2)22(6-10-34(43)44)30(38-27)13-25(17)37-29/h37-40H,5-16H2,1-4H3,(H,41,42)(H,43,44)(H,45,46)(H,47,48) ChemAxon inchikey WIUGGJKHYQIGNH-UHFFFAOYSA-N ChemAxon polar_surface_area 212.36 ChemAxon refractivity 181.86 ChemAxon polarizability 71.34 ChemAxon rotatable_bond_count 12 ChemAxon acceptor_count 8 ChemAxon donor_count 8 ChemAxon physiological_charge -4 ChemAxon formal_charge 0 ChemAxon Porphyrin and chlorophyll metabolism ec00860 Porphyrin metabolism The metabolism of porphyrin begins with with glutamic acid being processed by an ATP-driven glutamyl-tRNA synthetase by interacting with hydrogen ion and tRNA(Glu), resulting in amo, pyrophosphate and L-glutamyl-tRNA(Glu) Glutamic acid. Glutamic acid can be obtained as a result of L-glutamate metabolism pathway, glutamate / aspartate : H+ symporter GltP, glutamate:sodium symporter or a glutamate / aspartate ABC transporter . L-glutamyl-tRNA(Glu) Glutamic acid interacts with a NADPH glutamyl-tRNA reductase resulting in a NADP, a tRNA(Glu) and a (S)-4-amino-5-oxopentanoate. This compound interacts with a glutamate-1-semialdehyde aminotransferase resulting a 5-aminolevulinic acid. This compound interacts with a porphobilinogen synthase resulting in a hydrogen ion, water and porphobilinogen. The latter compound interacts with water resulting in hydroxymethylbilane synthase resulting in ammonium, and hydroxymethylbilane. Hydroxymethylbilane can either be dehydrated to produce uroporphyrinogen I or interact with a uroporphyrinogen III synthase resulting in a water molecule and a uroporphyrinogen III. Uroporphyrinogen I interacts with hydrogen ion through a uroporphyrinogen decarboxylase resulting in a carbon dioxide and a coproporphyrinogen I Uroporphyrinogen III can be metabolized into precorrin by interacting with a S-adenosylmethionine through a siroheme synthase resulting in hydrogen ion, an s-adenosylhomocysteine and a precorrin-1. On the other hand, Uroporphyrinogen III interacts with hydrogen ion through a uroporphyrinogen decarboxylase resulting in a carbon dioxide and a Coproporphyrinogen III. Precorrin-1 reacts with a S-adenosylmethionine through a siroheme synthase resulting in a S-adenosylhomocysteine and a Precorrin-2. The latter compound is processed by a NAD dependent uroporphyrin III C-methyltransferase [multifunctional] resulting in a NADH and a sirohydrochlorin. This compound then interacts with Fe 2+ uroporphyrin III C-methyltransferase [multifunctional] resulting in a hydrogen ion and a siroheme. The siroheme is then processed in sulfur metabolism pathway. Uroporphyrinogen III can be processed in anaerobic or aerobic condition. Anaerobic: Uroporphyrinogen III interacts with an oxygen molecule, a hydrogen ion through a coproporphyrinogen III oxidase resulting in water, carbon dioxide and protoporphyrinogen IX. The latter compound then interacts with an 3 oxygen molecule through a protoporphyrinogen oxidase resulting in 3 hydrogen peroxide and a Protoporphyrin IX Aerobic: Uroporphyrinogen III reacts with S-adenosylmethionine through a coproporphyrinogen III dehydrogenase resulting in carbon dioxide, 5-deoxyadenosine, L-methionine and protoporphyrinogen IX. The latter compound interacts with a meanquinone through a protoporphyrinogen oxidase resulting in protoporphyrin IX. The protoporphyrin IX interacts with Fe 2+ through a ferrochelatase resulting in a hydrogen ion and a ferroheme b. The ferroheme b can either be incorporated into the oxidative phosphorylation as a cofactor of the enzymes involved in that pathway or it can interact with hydrogen peroxide through a catalase HPII resulting in a heme D. Heme D can then be incorporated into the oxidative phosphyrlation pathway as a cofactor of the enzymes involved in that pathway. Ferroheme b can also interact with water and a farnesyl pyrophosphate through a heme O synthase resulting in a release of pyrophosphate and heme O. Heme O is then incorporated into the Oxidative phosphorylation pathway. PW000936 Metabolic Specdb::CMs 23767 Specdb::CMs 674449 Specdb::CMs 674450 Specdb::CMs 674451 Specdb::CMs 674452 Specdb::CMs 674453 Specdb::CMs 674454 Specdb::CMs 674455 Specdb::CMs 674456 Specdb::CMs 674457 Specdb::CMs 674458 Specdb::CMs 674459 Specdb::CMs 674460 Specdb::CMs 674461 Specdb::CMs 674462 Specdb::CMs 674463 Specdb::CMs 674464 Specdb::CMs 674465 Specdb::CMs 674466 Specdb::CMs 674467 Specdb::CMs 674468 Specdb::CMs 674469 Specdb::CMs 674470 Specdb::CMs 674471 Specdb::CMs 674472 Specdb::NmrOneD 311771 Specdb::NmrOneD 311772 Specdb::NmrOneD 311773 Specdb::NmrOneD 311774 Specdb::NmrOneD 311775 Specdb::NmrOneD 311776 Specdb::NmrOneD 311777 Specdb::NmrOneD 311778 Specdb::NmrOneD 311779 Specdb::NmrOneD 311780 Specdb::NmrOneD 311781 Specdb::NmrOneD 311782 Specdb::NmrOneD 311783 Specdb::NmrOneD 311784 Specdb::NmrOneD 311785 Specdb::NmrOneD 311786 Specdb::NmrOneD 311787 Specdb::NmrOneD 311788 Specdb::NmrOneD 311789 Specdb::NmrOneD 311790 Specdb::MsMs 28370 Specdb::MsMs 28371 Specdb::MsMs 28372 Specdb::MsMs 34928 Specdb::MsMs 34929 Specdb::MsMs 34930 Specdb::MsMs 2382347 Specdb::MsMs 2382348 Specdb::MsMs 2382349 Specdb::MsMs 2580024 Specdb::MsMs 2580025 Specdb::MsMs 2580026 HMDB02158 440776 389645 C05768 COPROPORPHYRINOGEN_I 1CP Coproporphyrinogen I Kanehisa, 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. 22080510 Ding Y, Lin B, Huie CW: Binding studies of porphyrins to human serum albumin using affinity capillary electrophoresis. Electrophoresis. 2001 Jul;22(11):2210-6. 11504054 Gorchein A, Guo R, Lim CK, Raimundo A, Pullon HW, Bellingham AJ: Porphyrins in urine, plasma, erythrocytes, bile and faeces in a case of congenital erythropoietic porphyria (Gunther's disease) treated with blood transfusion and iron chelation: lack of benefit from oral charcoal. Biomed Chromatogr. 1998 Nov-Dec;12(6):350-6. 9861496 Beukeveld GJ, In 't Veld G, Havinga R, Groen AK, Wolthers BG, Kuipers F: Relationship between biliary lipid and protoporphyrin secretion; potential role of mdr2 P-glycoprotein in hepatobiliary organic anion transport. J Hepatol. 1996 Mar;24(3):343-52. 8778203 Pinelli A, Mussini C, Bertolini B, Buratti M, Trivulzio S: Increased excretion of urine coproporphyrins during daunorubicin administration in patients affected by acute myelogenous leukemia. Pharmacol Res. 2003 Nov;48(5):515-8. 12967599 Sakai T, Niinuma Y, Yanagihara S, Ushio K: Liquid-chromatographic separation and determination of coproporphyrins I and III in urine. Clin Chem. 1983 Feb;29(2):350-3. 6821943 Cornford P: Transformation of porphobilinogen into porphyrins by preparations from human erythrocytes. Biochem J. 1964 Apr;91(1):64-73. 5833390 Pannier E, Viot G, Aubry MC, Grange G, Tantau J, Fallet-Bianco C, Muller F, Cabrol D: Congenital erythropoietic porphyria (Gunther's disease): two cases with very early prenatal manifestation and cystic hygroma. Prenat Diagn. 2003 Jan;23(1):25-30. 12533808 Mel'nikova YaI, Kravchuk ZI, Preygerzon VA, Martsev SP: Functional activation of antibodies on modification with Pd(II) coproporphyrin I N-Hydroxysuccinimide ester. Biochemistry (Mosc). 1997 Aug;62(8):924-7. 9360305 Uroporphyrinogen decarboxylase P29680 DCUP_ECOLI hemE http://ecmdb.ca/proteins/P29680.xml Uroporphyrinogen I <> Coproporphyrinogen I +4 Carbon dioxide R04972 Uroporphyrinogen I + 4 Hydrogen ion >4 Carbon dioxide + Coproporphyrinogen I PW_R003481