2.0 2012-08-09 09:25:30 -0600 2015-06-03 17:21:48 -0600 ECMDB21568 M2MDB001963 Precorrin-1 Precorrin-1 is a member of the chemical class known as Precorrins. These are intermediates formed by methylation at one or more of the four rings prior to the formation of the macrocyclic corrin ring. Precorrin-1 is invovled in Proto- and siroheme biosynthesis. 3,3',3'',3'''-[(12S,13S)-3,8,13,17-Tetrakis(carboxylatomethyl)-13-methyl-5,10,12,13,20,24-hexahydroporphyrin-2,7,12,18-tetrayl]tetrapropanoate 3,3',3'',3'''-[(12S,13S)-3,8,13,17-Tetrakis(carboxylatomethyl)-13-methyl-5,10,12,13,20,24-hexahydroporphyrin-2,7,12,18-tetrayl]tetrapropanoic acid Precorrin-1 Precorrin-1 octaanion C41H46N4O16 850.8211 850.290881444 3-[(4S,5S)-10,14,19-tris(2-carboxyethyl)-5,9,15,20-tetrakis(carboxymethyl)-5-methyl-21,22,23,24-tetraazapentacyclo[16.2.1.1³,⁶.1⁸,¹¹.1¹³,¹⁶]tetracosa-1(20),3(24),6,8,10,13,15,18-octaen-4-yl]propanoic acid 3-[(4S,5S)-10,14,19-tris(2-carboxyethyl)-5,9,15,20-tetrakis(carboxymethyl)-5-methyl-21,22,23,24-tetraazapentacyclo[16.2.1.1³,⁶.1⁸,¹¹.1¹³,¹⁶]tetracosa-1(20),3(24),6,8,10,13,15,18-octaen-4-yl]propanoic acid C[C@]1(CC(O)=O)[C@H](CCC(O)=O)C2=N\C1=C/C1=C(CC(O)=O)C(CCC(O)=O)=C(CC3=C(CCC(O)=O)C(CC(O)=O)=C(CC4=C(CCC(O)=O)C(CC(O)=O)=C(C2)N4)N3)N1 InChI=1S/C41H46N4O16/c1-41(17-40(60)61)24(5-9-36(52)53)31-15-29-22(11-38(56)57)19(3-7-34(48)49)27(43-29)14-28-21(10-37(54)55)18(2-6-33(46)47)25(42-28)13-26-20(4-8-35(50)51)23(12-39(58)59)30(44-26)16-32(41)45-31/h16,24,42-44H,2-15,17H2,1H3,(H,46,47)(H,48,49)(H,50,51)(H,52,53)(H,54,55)(H,56,57)(H,58,59)(H,60,61)/b32-16-/t24-,41+/m1/s1 CJLVUWULFKHGFB-NZCAJUPMSA-N Cytoplasm logp 0.82 ALOGPS logs -4.30 ALOGPS solubility 4.31e-02 g/l ALOGPS logp 1.57 ChemAxon pka_strongest_acidic 3.18 ChemAxon iupac 3-[(4S,5S)-10,14,19-tris(2-carboxyethyl)-5,9,15,20-tetrakis(carboxymethyl)-5-methyl-21,22,23,24-tetraazapentacyclo[16.2.1.1³,⁶.1⁸,¹¹.1¹³,¹⁶]tetracosa-1(20),3(24),6,8,10,13,15,18-octaen-4-yl]propanoic acid ChemAxon average_mass 850.8211 ChemAxon mono_mass 850.290881444 ChemAxon smiles C[C@]1(CC(O)=O)[C@H](CCC(O)=O)C2=N\C1=C/C1=C(CC(O)=O)C(CCC(O)=O)=C(CC3=C(CCC(O)=O)C(CC(O)=O)=C(CC4=C(CCC(O)=O)C(CC(O)=O)=C(C2)N4)N3)N1 ChemAxon formula C41H46N4O16 ChemAxon inchi InChI=1S/C41H46N4O16/c1-41(17-40(60)61)24(5-9-36(52)53)31-15-29-22(11-38(56)57)19(3-7-34(48)49)27(43-29)14-28-21(10-37(54)55)18(2-6-33(46)47)25(42-28)13-26-20(4-8-35(50)51)23(12-39(58)59)30(44-26)16-32(41)45-31/h16,24,42-44H,2-15,17H2,1H3,(H,46,47)(H,48,49)(H,50,51)(H,52,53)(H,54,55)(H,56,57)(H,58,59)(H,60,61)/b32-16-/t24-,41+/m1/s1 ChemAxon inchikey CJLVUWULFKHGFB-NZCAJUPMSA-N ChemAxon polar_surface_area 358.13 ChemAxon refractivity 211.01 ChemAxon polarizability 85.29 ChemAxon rotatable_bond_count 20 ChemAxon acceptor_count 17 ChemAxon donor_count 11 ChemAxon physiological_charge -8 ChemAxon formal_charge 0 ChemAxon Porphyrin and chlorophyll metabolism ec00860 Metabolic pathways eco01100 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::EiMs 4372 Specdb::MsMs 37010 Specdb::MsMs 37011 Specdb::MsMs 37012 Specdb::MsMs 39458 Specdb::MsMs 39459 Specdb::MsMs 39460 25245954 26331420 C15527 58893 Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948. 18331064 Putative uroporphyrinogen-III C-methyltransferase P09127 HEMX_ECOLI hemX http://ecmdb.ca/proteins/P09127.xml Siroheme synthase P0AEA8 CYSG_ECOLI cysG http://ecmdb.ca/proteins/P0AEA8.xml S-adenosyl-L-methionine + Uroporphyrinogen III > S-Adenosylhomocysteine + Precorrin-1 S-adenosyl-L-methionine + Precorrin-1 > S-Adenosylhomocysteine + Precorrin-2 2 S-Adenosylmethionine + Uroporphyrinogen III + Precorrin-1 <>2 S-Adenosylhomocysteine + Precorrin 2 R03194 Uroporphyrinogen III + S-adenosyl-L-methionine > Hydrogen ion + S-Adenosylhomocysteine + Precorrin-1 PW_R003489