2.0 2012-05-31 13:52:51 -0600 2015-06-03 15:54:07 -0600 ECMDB01441 M2MDB000390 6,7-Dihydropteridine 6,7-Dihydropteridine is the product of the reduction of 5,6,7,8-Tetrahydropteridine, which is catalyzed by 6,7-dihydropteridine reductase (EC 1.5.1.34). (KEGG) 6,7-Dihydropteridine Dihydropteridine C6H6N4 134.1386 134.059246212 6,7-dihydropteridine dihydropteridine C1CN=C2N=CN=CC2=N1 InChI=1S/C6H6N4/c1-2-9-6-5(8-1)3-7-4-10-6/h3-4H,1-2H2 KVDQMARGGBLIJM-UHFFFAOYSA-N Solid Cytosol logp -0.08 ALOGPS logs -2.48 ALOGPS solubility 4.40e-01 g/l ALOGPS logp -0.37 ChemAxon pka_strongest_basic 2.46 ChemAxon iupac 6,7-dihydropteridine ChemAxon average_mass 134.1386 ChemAxon mono_mass 134.059246212 ChemAxon smiles C1CN=C2N=CN=CC2=N1 ChemAxon formula C6H6N4 ChemAxon inchi InChI=1S/C6H6N4/c1-2-9-6-5(8-1)3-7-4-10-6/h3-4H,1-2H2 ChemAxon inchikey KVDQMARGGBLIJM-UHFFFAOYSA-N ChemAxon polar_surface_area 49.44 ChemAxon refractivity 36.9 ChemAxon polarizability 12.75 ChemAxon rotatable_bond_count 0 ChemAxon acceptor_count 4 ChemAxon donor_count 0 ChemAxon physiological_charge 0 ChemAxon formal_charge 0 ChemAxon Folate biosynthesis The biosynthesis of folic acid begins with a product of purine nucleotides de novo biosynthesis pathway, GTP. This compound is involved in a reaction with water through a GTP cyclohydrolase 1 protein complex, resulting in a hydrogen ion, formic acid and 7,8-dihydroneopterin 3-triphosphate. The latter compound is dephosphatased through a dihydroneopterin triphosphate pyrophosphohydrolase resulting in the release of a pyrophosphate, hydrogen ion and 7,8-dihydroneopterin 3-phosphate. The latter compound reacts with water spontaneously resulting in the release of a phosphate and a 7,8 -dihydroneopterin. This compound reacts with a dihydroneopterin aldolase, releasing a glycoaldehyde and 6-hydroxymethyl-7,9-dihydropterin. The latter compound is phosphorylated with a ATP-driven 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase resulting in a (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate. Chorismate is metabolized by reacting with L-glutamine through a 4-amino-4-deoxychorismate synthase resulting in L-glutamic acid and 4-amino-4-deoxychorismate. The latter compound then reacts through an aminodeoxychorismate lyase resulting in pyruvic acid,hydrogen ion and p-aminobenzoic acid. (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate and p-aminobenzoic acid react through a dihydropteroate synthase resulting in pyrophosphate and 7,8-dihydropteroic acid. This compound reacts with L-glutamic acid through an ATP driven bifunctional folylpolyglutamate synthetase / dihydrofolate synthetase resulting in a 7,8-dihydrofolate monoglutamate. This compound is reduced through an NADPH mediated dihydrofolate reductase resulting in a tetrahydrofate. This product goes on to a one carbon pool by folate pathway. PW000908 ec00790 Metabolic Trinitrotoluene degradation ec00633 Metabolic pathways eco01100 Specdb::CMs 12981 Specdb::CMs 162681 Specdb::NmrOneD 147760 Specdb::NmrOneD 147761 Specdb::NmrOneD 147762 Specdb::NmrOneD 147763 Specdb::NmrOneD 147764 Specdb::NmrOneD 147765 Specdb::NmrOneD 147766 Specdb::NmrOneD 147767 Specdb::NmrOneD 147768 Specdb::NmrOneD 147769 Specdb::NmrOneD 147770 Specdb::NmrOneD 147771 Specdb::NmrOneD 147772 Specdb::NmrOneD 147773 Specdb::NmrOneD 147774 Specdb::NmrOneD 147775 Specdb::NmrOneD 147776 Specdb::NmrOneD 147777 Specdb::NmrOneD 147778 Specdb::NmrOneD 147779 Specdb::MsMs 23453 Specdb::MsMs 23454 Specdb::MsMs 23455 Specdb::MsMs 30251 Specdb::MsMs 30252 Specdb::MsMs 30253 Specdb::MsMs 2812370 Specdb::MsMs 2812371 Specdb::MsMs 2812372 Specdb::MsMs 2897055 Specdb::MsMs 2897056 Specdb::MsMs 2897057 HMDB01441 167 162 C05649 30156 67-DIHYDROPTERIDINE 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). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. 22080510 van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. 17765195 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 Koslow SH, Butler IJ: Biogenic amine synthesis defect in dihydropteridine reductase deficiency. Science. 1977 Nov 4;198(4316):522-3. 20665 Ponzone A, Spada M, Ferraris S, Dianzani I, de Sanctis L: Dihydropteridine reductase deficiency in man: from biology to treatment. Med Res Rev. 2004 Mar;24(2):127-50. 14705166 Flavohemoprotein P24232 HMP_ECOLI hmp http://ecmdb.ca/proteins/P24232.xml Oxygen-insensitive NAD(P)H nitroreductase P38489 NFNB_ECOLI nfnB http://ecmdb.ca/proteins/P38489.xml 6,7-Dihydropteridine + 3 Hydrogen ion + NADH <> NAD + Tetrahydropteridine 6,7-Dihydropteridine + 3 Hydrogen ion + NADPH <> NADP + Tetrahydropteridine NAD(P)⁺ + Tetrahydropteridine <> NAD(P)H + 6,7-Dihydropteridine + Hydrogen ion 1.5.1.34-RXN Tetrahydropteridine + NAD > 6,7-Dihydropteridine + NADH Tetrahydropteridine + NADP > 6,7-Dihydropteridine + NADPH Tetrahydropteridine + NAD + NADP <> 6,7-Dihydropteridine + NADH + NADPH + Hydrogen ion R07354 R07355