chembox verifiedrevid 444074048 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 Ref cascite correct ?? CASNo 91 18 9 PubChem 1043 UNII Ref fdacite correct FDA UNII 6EZF26XQ81 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
to the methyl group at position 6 of the pteridine ring system. They are critical compounds in a large ... unconjugated pteridine in vertebrates, is a co factor in the hydroxylation of aromatic compounds and synthesis of nitric oxide. Molybdopterin is a substituted pteridine that binds molybdenum to give ... of pteridine of unknown function in cyanobacteria . See also Pteridine Tetrahydrobiopterin Molybdopterin ... 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
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
Drugbox verifiedrevid 445085839 IUPAC name 4 vinylbenzene 1,2 diol image 3,4 Dihydroxystyrene.png image2 3,4 dihydroxystyrene 3D balls.png Clinical data tradename pregnancy category legal status Uncontrolled routes of administration Pharmacokinetic data bioavailability metabolism elimination half life excretion Identifiers CAS number 6053 02 7 ATC prefix none ATC suffix PubChem 151398 ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 133430 KEGG Ref keggcite correct kegg KEGG C06224 Chemical data 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 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 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 10.1016 0167 4838 84 90194 8 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 nervous system drug stub ... more details
enzyme Name alkylglycerol monooxygenase EC number 1.14.16.5 CAS number 37256 82 9 IUBMB EC number 1 14 16 5 GO code 0050479 image width caption Alkylglycerol monooxygenase AGMO , EC number 1.14.16.5 is an enzyme that catalyzes the hydroxylation of alkylglycerols, a specific subclass of ether lipid s. This enzyme was first described in 1964 as a pteridine dependent etherlipid cleaving enzyme . ref cite journal last Tietz first AA coauthors Lindberg, M, Kennedy, EP title A New Pteridine Requiring Enzyme System For The Oxidation Of Glyceryl Ethers. journal The Journal of biological chemistry date 1964 Dec year 1964 volume 239 pages 4081 90 pmid 14247652 ref In 2010 finally, the gene coding for alkylglycerol monooxygenase was discovered as transmembrane protein 195 TMEM195 on chromosome 7. ref cite journal last Watschinger first K title Identification of the gene encoding alkylglycerol monooxygenase defines a third class of tetrahydrobiopterin dependent enzymes journal Proc. Natl. Acad. Sci. U.S.A year 2010 volume 107 pages 13672 13677 pmid 20643956 ref In analogy to the enzymes phenylalanine hydroxylase , tyrosine hydroxylase , tryptophan hydroxylase and nitric oxide synthase , alkylglycerol monooxygenase critically depends on the cofactor biochemistry cofactor tetrahydrobiopterin and iron . The reaction catalysis catalyzed by alkylglycerol monooxygenase 1 alkyl sn glycerol tetrahydrobiopterin O sub 2 sub math rightleftharpoons math 1 hydroxyalkyl sn glycerol 6,7 8H dihydrobiopterin H sub 2 sub O The unstable intermediate product 1 hydroxyalkyl sn glycerol rearranges into the fatty aldehyde and the free glycerol derivative. The fatty aldehyde is then further oxidized to the corresponding acid by fatty aldehyde dehydrogenase . Deleted image removed Image chemical reaction.png thumb Alkylglycerol monoooxygenase catalyzed degradation of an alkylglycerol into the glycerol derivative and the respective aldehyde via an instabile hemiacetale. Taken from sup 2 sup . Alkylglyce ... more details
chembox verifiedrevid 444023988 ImageFile Neopterin.svg ImageSize IUPACName 2 amino 6 1,2,3 trihydroxypropyl 1 H pteridin 4 one OtherNames Section1 Chembox Identifiers CASNo Ref cascite correct CAS CASNo 2009 64 5 PubChem 448839 ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 395518 DrugBank Ref drugbankcite correct drugbank DrugBank DB02385 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 DrugBank Ref drugbankcite correct drugbank DrugBank DB02385 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 a ... more details
chembox verifiedrevid 452026764 ImageFile Xanthopterin.svg ImageSize 100px IUPACName Xanthopterin OtherNames Section1 Chembox Identifiers CASNo 119 44 8 PubChem 8397 ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 8091 UNII Ref fdacite correct FDA UNII V66551EU1R StdInChI Ref stdinchicite correct chemspider StdInChI 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 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey VURKRJGMSKJIQX UHFFFAOYSA N 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 concanavalin . 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 a ... 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 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 author separator , author2 Werner Felmayer G author3 Fuchs D display authors 3 last4 Hausen first4 A. last5 Reibnegger first5 R. last6 Yim first6 J.J. last7 Wachter first7 H. 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 issue 1 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. Unusua ... more details
1 ref The biochromes include true pigments, such as carotenoid s and pteridine s. These pigments selectively ... amounts 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 ... as pterorhodin , a pteridine Dimer chemistry dimer that accumulates around eumelanin core, and it is also ... more details
PBB geneid 5053 Phenylalanine hydroxylase PheOH, alternatively PheH or PAH EC number 1.14.16.1 is an enzyme that catalyzes the hydroxylation of the aromatic side chain of phenylalanine to generate tyrosine . PheOH is one of three members of the pterin dependent amino acid hydroxylases, a class of monooxygenase that uses tetrahydrobiopterin BH sub 4 sub , a pteridine cofactor and a non heme iron for catalysis. During the reaction, molecular oxygen is heterolytically cleaved with sequential incorporation of one oxygen atom into BH sub 4 sub and phenylalanine substrate. ref name Fitzpatrick1999 cite journal author Fitzpatrick PF title Tetrahydropterin dependent amino acid hydroxylases journal Annu. Rev. Biochem. volume 68 issue pages 355 81 year 1999 pmid 10872454 doi 10.1146 annurev.biochem.68.1.355 ref File Overallreaction.png thumb alt Reaction catalyzed by PheOH. Reaction catalyzed by PheOH. Phenylalanine hydroxylase is the rate limiting enzyme of the metabolic pathway that degrades excess phenylalanine. Research on phenylalanine hydroxylase by Seymour Kaufman led to the discovery of tetrahydrobiopterin as a biological cofactor. ref name pmid13525410 cite journal author KAUFMAN S title A new cofactor required for the enzymatic conversion of phenylalanine to tyrosine journal J. Biol. Chem. volume 230 issue 2 pages 931 9 year 1958 month February pmid 13525410 doi ref The enzyme is also interesting from a human health perspective because mutations in PAH gene PAH , the encoding gene, can lead to phenylketonuria, a severe metabolic disorder. Enzyme Mechanism The reaction is thought to proceed through the following steps formation of a Fe II O O BH sub 4 sub bridge. heterolytic cleavage of the O O bond to yield the ferryl oxo hydroxylating intermediate Fe IV O attack on Fe IV O to hydroxylate phenylalanine substrate to tyrosine. ref name Fitzpatrick 2003 cite journal author Fitzpatrick PF title Mechanism of aromatic amino acid hydroxylation journal Biochemistry volume 4 ... more details
Encyclopedia
top
