chembox ImageFile Pteridin Pteridine.svg ImageSize 160px ImageName Skeletal formula of pteridine ImageFile1 Pteridine 3D balls.png ImageName1 Ball and stick model IUPACName pteridine OtherNames Section1 Chembox Identifiers CASNo 91 18 9 PubChem 1043 SMILES C1 CN C2C N1 C NC N2 MeSHName Section2 Chembox Properties Formula C sub 6 sub H sub 4 sub N sub 4 sub MolarMass 132.123 Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Pteridine is a chemical compound composed of fused pyrimidine and pyrazine rings. A pteridine is also a group of heterocyclic compounds containing a wide variety of substitutions on this structure. Pterin s and Flavin group flavin s are classes of substituted pteridines that have important biological activity. See also Pterin Flavin group References Voet, D. Voet, J.G. 2004 . Biochemistry 3rd ed. . John Wiley & Sons. ISBN 0 471 39223 5 External links Category Pteridines heterocyclic stub de Pteridin es Pteridina eo Pteridino fr Pt ridine it Pteridina hu Pteridin nl Pteridine ja pt Pteridina ru sr Pteridin zh ... more details
enzyme Name pteridine oxidase EC number 1.17.3.1 CAS number 74082 65 8 IUBMB EC number 1 17 3 1 GO code 0050227 image width caption In enzymology , a pteridine oxidase EC number 1.17.3.1 is an enzyme that catalysis catalyzes the chemical reaction 2 amino 4 hydroxypteridine O sub 2 sub math rightleftharpoons math 2 amino 4,7 dihydroxypteridine ? Thus, the two substrate biochemistry substrates of this enzyme are 2 amino 4 hydroxypteridine and oxygen O sub 2 sub , whereas its product chemistry product is 2 amino 4,7 dihydroxypteridine . This enzyme belongs to the family of oxidoreductase s, specifically those acting on CH or CH2 group with oxygen as acceptor. The systematic name of this enzyme class is 2 amino 4 hydroxypteridine oxygen oxidoreductase 7 hydroxylating . References reflist 1 cite journal author Yong Y N date 1980 title Detection of a pteridine oxidase in plants journal Plant Sci. Lett. volume 18 pages 169&ndash 175 1.17 enzyme stub Category EC 1.17.3 Category Enzymes of unknown structure it Pteridina ossidasi ja ... more details
enzyme Name Pteridine reductase EC number 1.5.1.33 CAS number 131384 61 7 IUBMB EC number 1 5 1 33 GO code image width caption In enzymology , a pteridine reductase EC number 1.5.1.33 is an enzyme that catalysis catalyzes the chemical reaction 5,6,7,8 tetrahydrobiopterin 2 NADP sup sup math rightleftharpoons math biopterin 2 NADPH 2 H sup sup Thus, the two substrate biochemistry substrates of this enzyme are 5,6,7,8 tetrahydrobiopterin and nicotinamide adenine dinucleotide phosphate NADP sup sup , whereas its 3 product chemistry products are biopterin , nicotinamide adenine dinucleotide phosphate NADPH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH NH group of donors with NAD or NADP as acceptor. The systematic name of this enzyme class is 5,6,7,8 tetrahydrobiopterin NADP oxidoreductase . Other names in common use include PTR1 , and pteridine reductase 1 . Structural studies As of late 2007, 7 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1W0C , PDB link 2BF7 , PDB link 2BFA , PDB link 2BFM , PDB link 2BFO , PDB link 2BFP , and PDB link 2C7V . References reflist 1 cite journal author Nare B, Hardy LW, Beverley SM date 1997 title The roles of pteridine reductase 1 and dihydrofolate reductase thymidylate synthase in pteridine metabolism in the protozoan parasite Leishmania major journal J. Biol. Chem. volume 272 pages 13883&ndash 91 pmid 9153248 doi 10.1074 jbc.272.21.13883 issue 21 cite journal author SM, Hunter WN date 2001 title Pteridine reductase mechanism correlates pterin metabolism with drug resistance in trypanosomatid parasites journal Nat. Struct. Biol. volume 8 pages 521&ndash 5 pmid 11373620 doi 10.1038 88584 last2 Sch ttelkopf first2 AW last3 Leonard first3 GA last4 Luba first4 J last5 Hardy first5 LW last6 Beverley first6 SM last7 Hunter first7 WN issue 6 cite journal author Fitzpatrick PF date 2000 title ... more details
position on the pteridine ring. They are critical compounds in a large number of biological group ... depending on its function. Tetrahydrobiopterin , the major unconjugated pteridine in vertebrates ... is a substituted pteridine that binds molybdenum to give redox enzymes involved in biological ... in methanogenic organisms. Cyanopterin is a glycosylated version of pteridine of unknown function in cyanobacteria . See also Pteridine Tetrahydrobiopterin Molybdopterin Cyanopterin Tetrahydromethanopterin ... more details
enzyme Name anthranilate 3 monooxygenase EC number 1.14.16.3 CAS number 37256 79 4 IUBMB EC number 1 14 16 3 GO code 0050478 image width caption In enzymology , an anthranilate 3 monooxygenase EC number 1.14.16.3 is an enzyme that catalysis catalyzes the chemical reaction anthranilate tetrahydrobiopterin O sub 2 sub math rightleftharpoons math 3 hydroxyanthranilate dihydrobiopterin H sub 2 sub O The 3 substrate biochemistry substrates of this enzyme are Anthranilic acid anthranilate , tetrahydrobiopterin , and oxygen O sub 2 sub , whereas its 3 product chemistry products are 3 hydroxyanthranilate , dihydrobiopterin , and water H sub 2 sub O . This enzyme belongs to the family of oxidoreductase s, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced pteridine as one donor, and incorporation of one ato of oxygen into the other donor. The systematic name of this enzyme class is anthranilate,tetrahydrobiopterin oxygen oxidoreductase 3 hydroxylating . Other names in common use include anthranilate 3 hydroxylase , anthranilate hydroxylase , anthranilic hydroxylase , and anthranilic acid hydroxylase . This enzyme participates in tryptophan metabolism . It employs one cofactor biochemistry cofactor , iron . References reflist 1 cite journal author Jequier E, Robinson DS, Lovenberg W, Sjoerdsma A date 1969 title Further studies on tryptophan hydroxylase in rat brainstem and beef pineal journal Biochem. Pharmacol. volume 18 pages 1071&ndash 81 pmid 5789774 doi 10.1016 0006 2952 69 90111 7 issue 5 cite journal author Nair PM and Vaidyanathan CS date 1965 title Anthranilic acid hydroxylase from Tecoma stans journal Biochim. Biophys. Acta volume 110 pages 521&ndash 531 1.14 enzyme stub Category EC 1.14.16 Category Iron enzymes Category Enzymes of unknown structure it Antranilato 3 monoossigenasi ja 3 ... more details
enzyme Name mandelate 4 monooxygenase EC number 1.14.16.6 CAS number 39459 82 0 IUBMB EC number 1 14 16 6 GO code 0050481 image width caption In enzymology , a mandelate 4 monooxygenase EC number 1.14.16.6 is an enzyme that catalysis catalyzes the chemical reaction S 2 hydroxy 2 phenylacetate tetrahydrobiopterin O sub 2 sub math rightleftharpoons math S 4 hydroxymandelate dihydrobiopterin H sub 2 sub O The 3 substrate biochemistry substrates of this enzyme are S 2 hydroxy 2 phenylacetate , tetrahydrobiopterin , and oxygen O sub 2 sub , whereas its 3 product chemistry products are S 4 hydroxymandelate , dihydrobiopterin , and water H sub 2 sub O . This enzyme belongs to the family of oxidoreductase s, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced pteridine as one donor, and incorporation of one ato of oxygen into the other donor. The systematic name of this enzyme class is S 2 hydroxy 2 phenylacetate,tetrahydrobiopterin oxygen oxidoreductase 4 hydroxylating . Other names in common use include L mandelate 4 hydroxylase , and mandelic acid 4 hydroxylase . It employs one cofactor biochemistry cofactor , iron . References reflist 1 cite journal author Bhat SG, Vaidyanathan CS date 1976 title Purifications and properties of L mandelate 4 hydroxylase from Pseudomonas convexa journal Arch. Biochem. Biophys. volume 176 pages 314&ndash 23 pmid 9909 doi 10.1016 0003 9861 76 90170 3 issue 1 1.14 enzyme stub Category EC 1.14.16 Category Iron enzymes Category Enzymes of unknown structure it Mandelato 4 monoossigenasi ja 4 ... more details
enzyme Name lactaldehyde dehydrogenase EC number 1.2.1.22 CAS number 37250 90 1 IUBMB EC number 1 2 1 22 GO code 0008911 image width caption In enzymology , a lactaldehyde dehydrogenase EC number 1.2.1.22 is an enzyme that catalysis catalyzes the chemical reaction S lactaldehyde NAD sup sup H sub 2 sub O math rightleftharpoons math S lactate NADH 2 H sup sup The 3 substrate biochemistry substrates of this enzyme are S lactaldehyde , nicotinamide adenine dinucleotide NAD sup sup , and water H sub 2 sub O , whereas its 3 product chemistry products are S lactate , nicotinamide adenine dinucleotide NADH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the aldehyde or oxo group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is S lactaldehyde NAD oxidoreductase . Other names in common use include L lactaldehyde NAD oxidoreductase , and nicotinamide adenine dinucleotide NAD linked dehydrogenase . This enzyme participates in pyruvate metabolism . Structural studies As of late 2007, 4 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 2HG2 , PDB link 2ILU , PDB link 2IMP , and PDB link 2OPX . References reflist 1 cite journal author Rembold H, Simmersbach F date 1969 title Catabolism of pteridine cofactors. II. A specific pterin deaminase in rat liver journal Biochim. Biophys. Acta. volume 184 pages 589&ndash 96 pmid 5821022 issue 3 cite journal author Sridhara S, Wu TT date 1969 title Purification and properties of lactaldehyde dehydrogenase from Escherichia coli journal J. Biol. Chem. volume 244 pages 5233&ndash 8 pmid 4310089 issue 19 1.2 enzyme stub Category EC 1.2.1 Category NADH dependent enzymes Category Enzymes of known structure it Lattaldeide deidrogenasi ja ... more details
enzyme Name pterin deaminase EC number 3.5.4.11 CAS number 9025 04 1 IUBMB EC number 3 5 4 11 GO code 0050228 image width caption In enzymology , a pterin deaminase EC number 3.5.4.11 is an enzyme that catalysis catalyzes the chemical reaction 2 amino 4 hydroxypteridine H sub 2 sub O math rightleftharpoons math 2,4 dihydroxypteridine NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are 2 amino 4 hydroxypteridine and water H sub 2 sub O , whereas its two product chemistry products are 2,4 dihydroxypteridine and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is 2 amino 4 hydroxypteridine aminohydrolase . This enzyme is also called acrasinase . References reflist 1 cite journal author LEVENBERG B, HAYAISHI O date 1959 title A bacterial pterin deaminase journal J. Biol. Chem. volume 234 pages 955&ndash 61 pmid 13654299 issue 4 cite journal author Rembold H, Simmersbach F date 1969 title Catabolism of pteridine cofactors. II. A specific pterin deaminase in rat liver journal Biochim. Biophys. Acta. volume 184 pages 589&ndash 96 pmid 5821022 issue 3 hydrolase stub Category EC 3.5.4 Category Enzymes of unknown structure ... more details
chembox ImageFile Xanthopterin.svg ImageSize 100px IUPACName Xanthopterin OtherNames Section1 Chembox Identifiers CASNo 119 44 8 PubChem 8397 ChemSpiderID 8091 SMILES O C1 N C NC 2 N C C O NC1 2 N InChI InChI 1S C6H5N5O2 c7 6 10 4 3 5 13 11 6 9 2 12 1 8 4 h1H, H,9,12 H3,7,8,10,11,13 Section2 Chembox Properties Formula C sub 6 sub H sub 5 sub N sub 5 sub O sub 2 sub MolarMass Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Xanthopterin is a yellow, crystalline solid ref name cancerweb.ncl.ac.uk http cancerweb.ncl.ac.uk cgi bin omd?xanthopterin ref , that occurs mainly in the wings of butterfly butterflies and in the urine of mammal s ref name cancerweb.ncl.ac.uk . Small microorganisms convert it into folic acid ref http medical.merriam webster.com medical xanthopterin ref . It is the end product of a non conjugated pteridine compound ref name content.karger.com http content.karger.com ProdukteDB produkte.asp?Doi 46271 ref , and inhibits the growth of lymphocytes produced by concanovalin ref name content.karger.com . High levels of the chemical were found in patients with liver disease and hemolysis, the latter increasing levels by 35 ref http www.wikigenes.org e ref e 8490058.html ref ref http www.wikigenes.org e ref e 1481869.html ref . It has been suggested that the Oriental hornet uses xanthopterin as a light harvesting molecule to transform light into electrical energy, which may explain why the insects are more active when light intensity is greater. Although no explicit biochemical mechanism has been determined for this animal light to energy conversion system, it remains an active and important area of scientific research Plotkin et al., Naturwissenschaften 2010 97 1067 1076 . ref Cite web url http news.bbc.co.uk earth hi earth news newsid 9254000 9254445.stm title Oriental hornets powered by solar energy first Matt last Walker publisher BBC ref References reflist Category Natural products Category Pt ... more details
Drugbox verifiedrevid 413117976 IUPAC name 4 vinylbenzene 1,2 diol image 3,4 Dihydroxystyrene.png image2 3,4 dihydroxystyrene 3D balls.png KEGG Ref keggcite correct kegg KEGG C06224 InChI 1 C8H8O2 c1 2 6 3 4 7 9 8 10 5 6 h2 5,9 10H,1H2 InChIKey FBTSUTGMWBDAAC UHFFFAOYAL StdInChI Ref stdinchicite correct chemspider StdInChI 1S C8H8O2 c1 2 6 3 4 7 9 8 10 5 6 h2 5,9 10H,1H2 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey FBTSUTGMWBDAAC UHFFFAOYSA N CAS number 6053 02 7 ATC prefix none ATC suffix PubChem 151398 ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 133430 chemical formula C sub 8 sub H sub 8 sub O sub 2 sub molecular weight 136.15 g mol smiles Oc1ccc C C cc1O bioavailability metabolism elimination half life excretion pregnancy category legal status Uncontrolled routes of administration 3,4 Dihydroxystyrene DHS is a central nervous system centrally acting enzyme inhibitor inhibitor of the enzyme phenylalanine hydroxylase PH . ref name pmid6148105 cite journal author Koizumi S, Matsushima Y, Nagatsu T, Iinuma H, Takeuchi T, Umezawa H title 3,4 dihydroxystyrene, a novel microbial inhibitor for phenylalanine hydroxylase and other pteridine dependent monooxygenases journal Biochimica Et Biophysica Acta volume 789 issue 2 pages 111 8 year 1984 month September pmid 6148105 doi url http linkinghub.elsevier.com retrieve pii 0167 4838 84 90194 8 ref It is likely that DHS and other PH inhibitors will never have Illness clinical applications on account of their capacity for inducing hyperphenylalaninemia and phenylketonuria . See also Phenylalanine hydroxylase References Reflist 2 Enzyme inhibition Adrenergics Dopaminergics DEFAULTSORT Dihydroxystyrene, 3,4 Category Catechols Pharmacology stub ... more details
chembox Watchedfields changed verifiedrevid 415677430 ImageFile Neopterin.svg ImageSize IUPACName 2 amino 6 1,2,3 trihydroxypropyl 1 H pteridin 4 one OtherNames Section1 Chembox Identifiers CASNo 2009 64 5 PubChem 448839 ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 395518 SMILES O C2 N C Nc1ncc nc12 C H O C H O CO N StdInChI Ref stdinchicite correct chemspider StdInChI 1S C9H11N5O4 c10 9 13 7 5 8 18 14 9 12 3 1 11 7 6 17 4 16 2 15 h1,4,6,15 17H,2H2, H3,10,11,13,14,18 t4 ,6 m1 s1 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey BMQYVXCPAOLZOK XINAWCOVSA N SMILES C1 C N C2C N1 NC NC2 O N C C CO O O MeSHName Neopterin Section2 Chembox Properties Formula C sub 9 sub H sub 11 sub N sub 5 sub O sub 4 sub MolarMass 253.215 g mol Appearance Density MeltingPt BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Neopterin is a catabolic product of guanosine triphosphate GTP , a purine nucleotide . Neopterin belongs to the chemical group known as pteridine s. It is synthesised by macrophage s upon stimulation with the cytokine interferon gamma and is indicative of a pro inflammatory immune status. Neopterin serves as a marker of cell mediated immunity cellular immune system activation. Neopterin as disease marker Measurement of neopterin concentrations in body fluids like blood serum , cerebrospinal fluid or urine provides information about activation of cellular immune activation in humans under the control of T helper cells type 1. High neopterin production is associated with increased production of reactive oxygen species , neopterin concentrations also allow to estimate the extent of oxidative stress elicited by the immune system . Increased neopterin production is found in, but not limited to, the following diseases viral infection s including human immunodeficiency virus HIV , hepatitis B and hepatitis C bacterial infection s by intracellular living bacteria such as Borrelia Lyme Disease and Mycobacterium tuberculos ... more details
1 ref The biochromes include true pigments, such as carotenoid s and pteridine s. These pigments selectively ... of yellow pteridine pigments are named xanthophores those with a preponderance of red orange colour orange carotenoids are termed erythrophores. ref name Cytology Pteridine and carotenoid containing ... identified as pterorhodin , a pteridine Dimer chemistry dimer that accumulates around eumelanin ... more details
PBB geneid 5805 6 pyruvoyltetrahydropterin synthase , also known as PTS , is a human gene which facilitates Folic acid folate biosynthesis . ref name entrez cite web title Entrez Gene PTS 6 pyruvoyltetrahydropterin synthase url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 5805 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text See also 6 pyruvoyltetrahydropterin synthase 6 Pyruvoyltetrahydropterin synthase deficiency References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Werner ER, Werner Felmayer G, Fuchs D, et al. title Biochemistry and function of pteridine synthesis in human and murine macrophages. journal Pathobiology volume 59 issue 4 pages 276 9 year 1991 pmid 1883524 doi 10.1159 000163662 cite journal author Th ny B, Blau N title Mutations in the GTP cyclohydrolase I and 6 pyruvoyl tetrahydropterin synthase genes. journal Hum. Mutat. volume 10 issue 1 pages 11 20 year 1997 pmid 9222755 doi 10.1002 SICI 1098 1004 1997 10 1 11 AID HUMU2 3.0.CO 2 P cite journal author Th ny B, Auerbach G, Blau N title Tetrahydrobiopterin biosynthesis, regeneration and functions. journal Biochem. J. volume 347 Pt 1 issue pages 1 16 year 2000 pmid 10727395 doi 10.1042 0264 6021 3470001 pmc 1220924 cite journal author Th ny B, Leimbacher W, B rgisser D, Heizmann CW title Human 6 pyruvoyltetrahydropterin synthase cDNA cloning and heterologous expression of the recombinant enzyme. journal Biochem. Biophys. Res. Commun. volume 189 issue 3 pages 1437 43 year 1993 pmid 1282802 doi 10.1016 0006 291X 92 90235 D cite journal author Scriver CR, Clow CL, Kaplan P, Niederwieser A title Hyperphenylalaninemia due to deficiency of 6 pyruvoyl tetrahydropterin synthase. Unusual gene dosage effect in heterozygotes. journal Hum. Genet. volume 77 issue 2 pages 168 71 year 1987 pmid 3308682 doi cite journal au ... more details
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