*  6,7-dihydropteridine reductase - Wikipedia
In enzymology, a 6,7-dihydropteridine reductase (EC is an enzyme that catalyzes the chemical reaction a 5,6,7,8-tetrahydropteridine + NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } a 6,7-dihydropteridine + NAD(P)H + H+ The 3 substrates of this enzyme are 5,6,7,8-tetrahydropteridine, NAD+, and NADP+, whereas its 4 products are 6,7-dihydropteridine, NADH, NADPH, and H+. This enzyme participates in folate biosynthesis. This enzyme belongs to the family of oxidoreductases, 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-tetrahydropteridine:NAD(P)+ oxidoreductase. Other names in common use include 6,7-dihydropteridine:NAD(P)H oxidoreductase, DHPR, NAD(P)H:6,7-dihydropteridine oxidoreductase, NADH-dihydropteridine reductase, NADPH-dihydropteridine reductase, NADPH-specific dihydropteridine reductase, dihydropteridine (reduced nicotinamide adenine dinucleotide), reductase, dihydropteridine reductase, ...
*  Phenylalanine hydroxylase - Wikipedia
Phenylalanine hydroxylase (PAH) (EC is an enzyme that catalyzes the hydroxylation of the aromatic side-chain of phenylalanine to generate tyrosine. PAH is one of three members of the biopterin-dependent aromatic amino acid hydroxylases, a class of monooxygenase that uses tetrahydrobiopterin (BH4, 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 BH4 and phenylalanine substrate. 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. The enzyme is also interesting from a human health perspective because mutations in PAH, the encoding gene, can lead to phenylketonuria, a severe metabolic disorder. The reaction is thought to proceed through the following steps: formation of a ...
*  Dihydropteridine Reductase - 6,7 Dihydropteridine Reductase Summary Report | CureHunter
Dihydropteridine Reductase: An enzyme that catalyzes the reduction of 6,7-dihydropteridine to 5,6,7,8-tetrahydropteridine in the presence of NADP+. Defects in the enzyme are a cause of PHENYLKETONURIA II. Formerly listed as EC
*  Center for Structural Genomics of Infectious Diseases - Deposits
GTP cyclohydrolase I (encoded by gene folE) is the first Zn(2+)-dependent enzyme of the de novo tetrahydrofolate biosynthetic pathway. It presents in bacteria, fungi, and plants. It catalyzes the conversion of GTP to 7,8-dihydroneopterin triphosphate. The 2.1A resolution structure of GTP cyclohydrolase I from Yersinia pestis CO92 is a pentomer in the asymmetric unit. The structure contains, in the active site, five GTP molecules and Ca(2+) ions probably from crystallization in place of Zn(2+) determined by atomic distances and fluorescence spectrum ...
*  Bestowing inducibility on the cloned methanol dehydrogenase promoter (PmxaF) of Methylobacterium extorquens by applying...
Bestowing inducibility on the cloned methanol dehydrogenase promoter (PmxaF) of Methylobacterium extorquens by applying regulatory elements of Pseudomonas putida F1
*  Methylobacterium extorquens (Urakami and Komagata) Bousfield and Green
Methylobacterium extorquens ATCC ® 14718™ Designation: NCIB 9133 TypeStrain=False Application: Produces glutamate dehydrogenase (NADP+) NADP+-dependent glutamate dehydrogenase, glutamate dehydrogenase (NADP-dependent) Biotechnology
*  Methylobacterium extorquens (Urakami and Komagata) Bousfield and Green
Methylobacterium extorquens ATCC ® 14718™ Designation: NCIB 9133 TypeStrain=False Application: Produces glutamate dehydrogenase (NADP+) NADP+-dependent glutamate dehydrogenase, glutamate dehydrogenase (NADP-dependent) Biotechnology
*  Tetrahydrobiopterin deficiency - Wikipedia
Tetrahydrobiopterin deficiency (THBD, BH4D), also called THB or BH4 deficiency, is a rare metabolic disorder that increases the blood levels of phenylalanine. Phenylalanine is an amino acid obtained through the diet. It is found in all proteins and in some artificial sweeteners. If tetrahydrobiopterin deficiency is not treated, excess phenylalanine can build up to harmful levels in the body, causing intellectual disability and other serious health problems. High levels of phenylalanine are present from infancy in people with untreated tetrahydrobiopterin (THB, BH4) deficiency. The resulting signs and symptoms range from mild to severe. Mild complications may include temporary low muscle tone. Severe complications include intellectual disability, movement disorders, difficulty swallowing, seizures, behavioral problems, progressive problems with development, and an inability to control body temperature. It was first characterized in 1975. This condition is inherited in an autosomal recessive ...
*  Deficits in the Activation and Phosphorylation of Hippocampal Tyrosine Hydroxylase in the Aged Fischer 344 Rat Following...
Abstract: Tyrosine hydroxylase activity was measured under optimal and suboptimal assay conditions in hippocampal extracts from young (2 month), mature (12 month), and old (24 month) Fischer 344 male rats 72 h after the infusion of 200 µg of the neurotoxin 6-hydroxydopamine or vehicle into the lateral ventricle. The lesion resulted in a 45-55% decrease of tyrosine hydroxylase activity measured under optimal conditions (pH 6.1, 3.0 mM 6-methyl-5,6,7,8-tetrahydropterin) and an ∼35% decrease in the relative concentration of immunoreactive tyrosine hydroxylase. When measured under suboptimal conditions (pH 6.6, 0.7 mM 6-methyl-5,6,7,8-tetrahydropterin), tyrosine hydroxylase activity in 2- and 12-month-old lesioned animals was twice that measured in vehicle-treated animals. However, in the old lesioned animals, tyrosine hydroxylase activity measured under suboptimal conditions was not different from that measured in age-matched vehicle-treated animals. Isoforms of tyrosine hydroxylase were ...
*  Dehalococcoides genomes and cofactors | Philosophical Transactions of the Royal Society B: Biological Sciences
Screening through the annotations of all published Dehalococcoides genomes suggested the use of corrinoids, thiamine, biotin, pyrodoxal-5-phosphate, flavin nucleotides and molybdopterin as enzyme-bound organic cofactors and the soluble cofactors tetrahydrofolate, S-adenosylmethionine and pantothenate/CoA in Dehalococcoides strains. No genes encoding for enzymes containing haem or lipoic acid as cofactors were annotated in the genome. Freely soluble DNA/RNA-forming nucleotides and nicotinic acid derivates (NAD+, NADP+) are predicted to be abundant as in other organisms, whereas no indications were found for the use of archaeal cofactors (i.e. coenzyme F420, tetrahydromethanopterin, coenzyme B, coenzyme M, coenzyme F430, methanofuran). The electronic supplementary material, table S1 gives an overview of proteins predicted to contain one of the enzyme-bound cofactors or interact with tetrahydrofolate-derivates together with results of protein identification by nLC-MS/MS obtained from 30 cultures of ...
*  Trimethoprim
... was commonly (since 1969 in the UK) used in a 1:5 combination with sulfamethoxazole, a sulfonamide antibiotic, which inhibits an earlier step in the folate synthesis pathway (see diagram above). This combination, also known as co-trimoxazole, TMP-sulfa, or TMP-SMX, results in an in vitro synergistic antibacterial effect by inhibiting successive steps in folate synthesis. This claimed benefit was not seen in general clinical use.[3] [4] The combinations use has been declining due to reports of sulfamethoxazole bone marrow toxicity, resistance and lack of greater efficacy in treating common urine and chest infections,[5][6][7][8] and side effects of antibacterial sulfonamides. As a consequence, the use of co-trimoxazole was restricted in 1995 [9] following the availability of trimethoprim (not in combination) in 1980. With its greater efficacy against a limited number of bacteria, Co-trimoxazole remains indicated for some infections; for example, it is used as prophylaxis in patients ...
*  Difference between revisions of "IGEM:Caltech/2008/Project/Vitamins" - OpenWetWare
Although folate is naturally produced in E.coli, the folate biosynthesis pathway in the bacteria Lactococcus lactis has been more heavily characterized and studied. There are six major enzymes involved in folate synthesis, which, in L.lactis, are contained in five genes: folB, folKE, folP, folC, and folA[1]. The first four, which we have chosen to focus on, are located in a gene cluster approximately 4.4kb long. We've chosen not to focus on folA for the time being because folA encodes an enzyme which turns one form of folate (dihydrofolate) into another form of folate(tetrahydrofolate). Since our assay would detect both types of folate as part of the total folate production, folA was not a prime target for overexpression of folate. In previous studies, this folate gene cluster has been successfully transformed into the folate-consuming bacteria L.gasseri, turning the bacteria in to folate-producers[3]. Therefore, we have chosen to also use the folate operon from L.lactis, which also offers the ...
*  More NO-No More ROS | Hypertension
With regard to the attenuation of reduced nicotinamide-adenine dinucleotide oxidase activity and ROS formation, ACE inhibition alone was somewhat more effective than eplerenone; however, the combination led to an additive reduction. The larger decrease in ROS formation by enalapril, as compared with eplerenone monotherapy, may also relate to the more effective prevention of tetrahydrobiopterin oxidation and subsequent endothelial NO synthase (eNOS) uncoupling by ACE inhibition. eNOS uncoupling, a condition that leads to eNOS-mediated superoxide anion production instead of NO, possibly resulting from a mismatch between eNOS and its cofactor tetrahydrobiopterin, is increasingly recognized as an important mechanism underlying endothelial dysfunction.4 The unique bradykinin-mediated stimulation of eNOS protein expression by ACE inhibitors,8,11 together with the effective attenuation of ROS formation, may explain the greater effect of enalapril compared with eplerenone monotherapy on basal and ...
*  Responsividade à tetrahidrobiopterina em pacientes com deficiência de fenilalanina hidroxilase
GIUGLIANI, Luciana et al. Tetrahydrobiopterin responsiveness of patients with phenylalanine hydroxylase deficiency. J. Pediatr. (Rio J.) [online]. 2011, vol.87, n.3, pp.245-251. ISSN 0021-7557. http://dx.doi.org/10.2223/JPED.2090.. OBJECTIVE: To identify patients responsive to tetrahydrobiopterin (BH4) in a sample of Brazilians with hyperphenylalaninemia due to phenylalanine hydroxylase deficiency (HPA-PAH). METHODS: Interventional study, convenience sampling. The inclusion criteria were: diagnosis of HPA-PAH; age , 7 years; phenylalanine-restricted diet and phenylalanine (Phe) levels , 6 mg/dL in all blood tests 1 year before inclusion. Blood samples were obtained the day before (day 1) and at 0, 4, 8 (day 2) and 24 h (day 3) after BH4 intake. Phe levels were measured using tandem mass spectrometry. The criteria used to define responsiveness to BH4 were: criterion 1- Phe reduction , 30% 8 h after BH4 administration; criterion 2 - Phe reduction , 30% 24 h after BH4 administration. RESULTS: ...
*  RCSB PDB - 1KW0: Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) in Complex with Tetrahydrobiopterin and...
1KW0: Crystal Structure of the Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase with Tetrahydrobiopterin and 3-(2-thienyl)-L-alanine, and its Implications for the Mechanism of Catalysis and Substrate Activation
*  RCSB PDB - 1J8U: Catalytic Domain of Human Phenylalanine Hydroxylase Fe(II) in Complex with Tetrahydrobiopterin...
1J8U: High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin.
*  Dr Michael J. Morris - Profiles - Staff - Chemistry - The University of Sheffield
My group is presently conducting research in several areas of synthetic organometallic and inorganic chemistry. Our main interest at present lies in the chemistry of complexes containing dithiolene (1,2-enedithiolate) ligands. These are important in biological inorganic chemistry where they are involved in the active sites of molybdenum and tungsten enzymes, and are also of interest because of the redox activity of the ligand. We have recently started a research program aimed at introducing additional redox-active substituents into dithiolene ligands in order to establish whether communication between them is possible in complexes containing two or more such ligands. We have already shown that this is the case in dinuclear bis(dithiolene) complexes and we are now expanding our research into mononuclear complexes. We are also interested in reactions involving the transfer of dithiolene ligands from one complex to another as a route to new and otherwise inaccessible dithiolene complexes.. In ...
*  3,4-Dihydroxystyrene - Wikipedia
3,4-Dihydroxystyrene (DHS) is a centrally-acting inhibitor of the enzyme phenylalanine hydroxylase (PH). It is likely that DHS and other PH inhibitors will never have clinical applications on account of their capacity for inducing hyperphenylalaninemia and phenylketonuria. Phenylalanine hydroxylase Koizumi S; Matsushima Y; Nagatsu T; Iinuma H; Takeuchi T; Umezawa H (September 1984). "3,4-dihydroxystyrene, a novel microbial inhibitor for phenylalanine hydroxylase and other pteridine-dependent monooxygenases". Biochimica et Biophysica Acta. 789 (2): 111-8. doi:10.1016/0167-4838(84)90194-8. PMID 6148105 ...
*  Science of Synthesis Knowledge Updates 2012 Vol. 2 - beck-shop.de
Content of this volume: Acylsilanes, Asymmetric Lithiation, 1,2,3-Trithioles, Their Benzo Derivatives, Selenium and Tellurium Analogues, 1,2,4-Triazolium Salts, Dithiadiazolium Salts and Dithiadiazolyl-Containing Compounds, 1,4-Dithiins, Pyridopyridazines, Pteridines and Related Structures, Pteridines and Related Structures, 1,2,3-Triazines and Phosphorus Analogues, 1,2,3-Triazines and Phosphorus Analogues, 1,2,4-Triazines, 1,3,5-Triazines and Phosphorus Analogues, Synthesis by Substitution of Hydrogen.. ...
*  PAH - SNPedia
Mutations in the phenylalanine hydroxylase (PAH) gene which result in lower activities of the enzyme will cause the metabolic disease phenylketonuria. SNPs in this gene include: ...
*  Awesomenauts - the 2D moba on Steam
Use your power, show your might! Play this Multiplayer Online Battle Arena (MOBA) game for FREE now! AWESOMENAUTS combines 2D platforming with team-based strategy and hero based action. Whether you are a new recruit or an intergalactic legend, play AWESOMENAUTS!