2.02012-05-31 13:52:51 -06002015-06-03 15:54:07 -0600ECMDB01441M2MDB0003906,7-Dihydropteridine6,7-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-DihydropteridineDihydropteridineC6H6N4134.1386134.0592462126,7-dihydropteridinedihydropteridineC1CN=C2N=CN=CC2=N1InChI=1S/C6H6N4/c1-2-9-6-5(8-1)3-7-4-10-6/h3-4H,1-2H2KVDQMARGGBLIJM-UHFFFAOYSA-NSolidCytosollogp-0.08logs-2.48solubility4.40e-01 g/llogp-0.37pka_strongest_basic2.46iupac6,7-dihydropteridineaverage_mass134.1386mono_mass134.059246212smilesC1CN=C2N=CN=CC2=N1formulaC6H6N4inchiInChI=1S/C6H6N4/c1-2-9-6-5(8-1)3-7-4-10-6/h3-4H,1-2H2inchikeyKVDQMARGGBLIJM-UHFFFAOYSA-Npolar_surface_area49.44refractivity36.9polarizability12.75rotatable_bond_count0acceptor_count4donor_count0physiological_charge0formal_charge0Folate biosynthesisThe 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.
PW000908ec00790MetabolicTrinitrotoluene degradationec00633Metabolic pathwayseco01100Specdb::CMs12981Specdb::CMs162681Specdb::NmrOneD147760Specdb::NmrOneD147761Specdb::NmrOneD147762Specdb::NmrOneD147763Specdb::NmrOneD147764Specdb::NmrOneD147765Specdb::NmrOneD147766Specdb::NmrOneD147767Specdb::NmrOneD147768Specdb::NmrOneD147769Specdb::NmrOneD147770Specdb::NmrOneD147771Specdb::NmrOneD147772Specdb::NmrOneD147773Specdb::NmrOneD147774Specdb::NmrOneD147775Specdb::NmrOneD147776Specdb::NmrOneD147777Specdb::NmrOneD147778Specdb::NmrOneD147779Specdb::MsMs23453Specdb::MsMs23454Specdb::MsMs23455Specdb::MsMs30251Specdb::MsMs30252Specdb::MsMs30253Specdb::MsMs2812370Specdb::MsMs2812371Specdb::MsMs2812372Specdb::MsMs2897055Specdb::MsMs2897056Specdb::MsMs2897057HMDB01441167162C056493015667-DIHYDROPTERIDINEKeseler, 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-D114.22080510van 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 370:17-25.17765195Winder, 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 80:2939-2948.18331064Koslow SH, Butler IJ: Biogenic amine synthesis defect in dihydropteridine reductase deficiency. Science. 1977 Nov 4;198(4316):522-3.20665Ponzone 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):127-50.14705166FlavohemoproteinP24232HMP_ECOLIhmphttp://ecmdb.ca/proteins/P24232.xmlOxygen-insensitive NAD(P)H nitroreductaseP38489NFNB_ECOLInfnBhttp://ecmdb.ca/proteins/P38489.xml6,7-Dihydropteridine + 3 Hydrogen ion + NADH <> NAD + Tetrahydropteridine6,7-Dihydropteridine + 3 Hydrogen ion + NADPH <> NADP + TetrahydropteridineNAD(P)<sup>+</sup> + Tetrahydropteridine <> NAD(P)H + 6,7-Dihydropteridine + Hydrogen ion1.5.1.34-RXNTetrahydropteridine + NAD > 6,7-Dihydropteridine + NADHTetrahydropteridine + NADP > 6,7-Dihydropteridine + NADPHTetrahydropteridine + NAD + NADP <> 6,7-Dihydropteridine + NADH + NADPH + Hydrogen ionR07354 R07355