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Dihydroorotate dehydrogenase (DHODH) is a rate-limiting enzyme in the de novo biosynthesis pathway of pyrimidines. Inhibition of this enzyme impedes cancer cell proliferation but the exact mechanisms of action of these inhibitors in cancer cells are poorly understood. In this study, we showed that cancer cells, namely melanoma, myeloma and lymphoma overexpressed DHODH protein and treatment with A771726 and Brequinar sodium resulted in cell cycle arrest at S-phase. Transfection with DHODH shRNA depleted DHODH protein expression and impeded the proliferation of melanoma cells. shRNA knockdown of DHODH in combination with DHODH inhibitors further reduced the cancer cell proliferation, suggesting that knockdown of DHODH had sensitized the cells to DHODH inhibitors. Cell cycle regulatory proteins, c-Myc and its transcriptional target, p21 were found down- and up-regulated, respectively, following treatment with DHODH inhibitors in melanoma, myeloma and lymphoma cells. Interestingly, knockdown of ...

InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.

In enzymology, a bilirubin oxidase (EC 1.3.3.5) is an enzyme that catalyzes the chemical reaction 2 bilirubin + O2 ⇌ {\displaystyle \rightleftharpoons } 2 biliverdin + 2 H2O Thus, the two substrates of this enzyme are bilirubin and O2, whereas its two products are biliverdin and H2O. This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is bilirubin:oxygen oxidoreductase. This enzyme is also called bilirubin oxidase M-1. This enzyme participates in porphyrin and chlorophyll metabolism. Two structures of bilirubin oxidase from the ascomycete Myrothecium verrucaria have been deposited in the Protein Data Bank (accession codes 3abg and 2xll). Murao S; Tanaka N (1981). A new enzyme bilirubin oxidase produced by Myrothecium verrucaria MT-1. Agric. Biol. Chem. 45: 2383-2384. doi:10.1271/bbb1961.45.2383. Tanaka N; Murao S (1985). Reaction of bilirubin oxidase produced by ...

Malaria is one of the most significant causes of childhood mortality, but disease control efforts are threatened by resistance of the Plasmodium parasite to current therapies. Continued progress in combating malaria requires development of new, easy to administer drug combinations with broad-ranging activity against all manifestations of the disease. DSM265, a triazolopyrimidine-based inhibitor of the pyrimidine biosynthetic enzyme dihydroorotate dehydrogenase (DHODH), is the first DHODH inhibitor to reach clinical development for treatment of malaria. We describe studies profiling the biological activity, pharmacological and pharmacokinetic properties, and safety of DSM265, which supported its advancement to human trials. DSM265 is highly selective toward DHODH of the malaria parasite Plasmodium, efficacious against both blood and liver stages of P. falciparum, and active against drug-resistant parasite isolates. Favorable pharmacokinetic properties of DSM265 are predicted to provide ...

Acute myeloid leukemia (AML) is a devastating disease, with the majority of patients dying within a year of diagnosis. For patients with relapsed/refractory AML, the prognosis is particularly poor with currently available treatments. Although genetically heterogeneous, AML subtypes share a common differentiation arrest at hematopoietic progenitor stages. Overcoming this differentiation arrest has the potential to improve the long-term survival of patients, as is the case in acute promyelocytic leukemia (APL), which is characterized by a chromosomal translocation involving the retinoic acid receptor alpha gene. Treatment of APL with all-trans retinoic acid (ATRA) induces terminal differentiation and apoptosis of leukemic promyelocytes, resulting in cure rates of over 80%. Unfortunately, similarly efficacious differentiation therapies have, to date, been lacking outside of APL. Inhibition of dihydroorotate dehydrogenase (DHODH), a key enzyme in the de novo pyrimidine synthesis pathway, was ...

article{185982, abstract = {L-Galactono-gamma-lactone dehydrogenase (EC 1.3.2.3; GLDase), an enzyme that catalyzes the final step in the biosynthesis of L-ascorbic acid was purified 1693-fold from a mitochondrial extract of cauliflower (Brassica oleracea, var. botrytis) to apparent homogeneity with an overall yield of 1.1\%, The purification procedure consisted of anion exchange, hydrophobic interaction, gel filtration, and fast protein liquid chromatography, The enzyme had a molecular mass of 56 kDa estimated by gel filtration chromatography and SDS-polyacrylamide gel electrophoresis and showed a pH optimum for activity between pH 8.0 and 8.5, with an apparent K-m of 3.3 mM for L-galactono-gamma-lactone. Based on partial peptide sequence information, polymerase chain reaction fragments were isolated and used to screen a cauliflower cDNA library from which a cDNA encoding GLDase was isolated, The deduced mature GLDase contained 509 amino acid residues with a predicted molecular mass of 57,837 ...

Specifically cleaves olefinic bonds in cyclic enones. Involved in the biosynthesis of jasmonic acid (JA) and perhaps in biosynthesis or metabolism of other oxylipin signaling moleclules. It is required for the spatial and temporal regulation of JA levels during dehiscence of anthers, promoting the stomium degeneration program (By similarity). In vitro, reduces 9S,13S-12-oxophytodienoic acid (9S,13S-OPDA) and 9R,13R-OPDA to 9S,13S-OPC-8:0 and 9R,13R-OPC-8:0, respectively.

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1ICS: X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE.

This gene encodes an enzyme that belongs to the family of dihydrodiol dehydrogenases, which exist in multiple forms in mammalian tissues and are involved in the metabolism of xenobiotics and sugars. These enzymes catalyze the NADP1-linked oxidation of transdihydrodiols of aromatic hydrocarbons to corresponding catechols. This enzyme is a dimeric dihydrodiol dehydrogenase, and it differs from monomeric dihydrodiol dehydrogenases in its high substrate specificity for trans-dihydrodiols of aromatic hydrocarbons in the oxidative direction. [provided by RefSeq, Jul 2008 ...

1RM6: Structure of a Xanthine Oxidase-Related 4-Hydroxybenzoyl-CoA Reductase with an Additional [4Fe-4S] Cluster and an Inverted Electron Flow

Investigation of the chlorophyll synthesis in plastid membranes:. The initial enzyme to start the synthesis of chlorophyll in light is NADPH-protochlorophyllide oxidoreductase (EC 1.3.1.33, POR). The group has studied the aggregation state of the POR, its localization in the lipid phase of the membranes and the enzyme conformational changes after irradiation, by energy transfer from tryptophan residues of membrane proteins to the fluorescence probes 1-aniline-8-naphthalene sulfonate (ANS) and pyrene. The membranes investigated were those accumulated in dark-grown wheat leaves - prolamellar bodies (PLBs) and prothylakoids (PTs). Changes in protein - probe interactions of the PLBs after irradiation has shown that POR is localized close to the membrane surface, most probably on the level of lipid polar heads. This supports the idea that the enzyme is not an integral membrane protein and is most probably localized on the membrane surface.. Photodynamic effect of pigment precursor in plants:. Some ...

A molybdenum-flavin-iron-sulfur protein that is involved in the anaerobic pathway of phenol metabolism in bacteria. A ferredoxin with two [4Fe-4S] clusters functions as t

Postdoctoral Position for a Plant Molecular Biologist / Biochemist A postdoctoral position is available for research on the light-dependent NADPH-protochlorophyllide oxidoreductase (POR), a key enzyme of chlorophyll synthesis in higher plants (see for example Proc. Natl. Acad. Sci. 92: 3254-3258; Plant J. 9: 513-523; Plant Cell 8: 763-769). The aim of the project is to optimize conditions for the overproduction of POR A and POR B in heterologous systems e.g. E. coli and/or yeast, and the reconstitution of the active enzymes. Once these conditions have been established, a detailed spectroscopic and biochemical analysis of the two proteins will be possible. This project represents part of a larger collaboration programme between the ETH and industrial partners. Although expertise in various laboratory methods is available both within and outside the ETH, the successful candidate should have a strong background and interest in molecular genetics and/or biochemistry. The position is initially ...

Uncharacterized protein; Essential protein required during embryogenesis (PubMed-24097264). Exhibits holdase chaperone activity involved in the stabilization of NADPH-protochlorophyllide oxidoreductase (POR) proteins against photooxidative stress during POR proteins import into chloroplasts. Required for chloroplast biogenesis and development (PubMed-24151298, PubMed-25901327). When expressed in yeast, triggers mitochondria-mediated cell death associated with the loss of mitochondrial membrane potential (PubMed-16192270) (258 aa ...

Proper nucleosides availability is crucial for the proliferation of living entities (eukaryotic cells, parasites, bacteria, and virus). Accordingly, the uses of inhibitors of the de novo nucleosides biosynthetic pathways have been investigated in the past. In the following we have focused on dihydroorotate dehydrogenase (DHODH), the fourth enzyme in the de novo pyrimidine nucleosides biosynthetic pathway. We first described the different types of enzyme in terms of sequence, structure, and biochemistry, including the reported bioassays. In a second part, the series of inhibitors of this enzyme along with a description of their potential or actual uses were reviewed. These inhibitors are indeed used in medicine to treat autoimmune diseases such as rheumatoid arthritis or multiple sclerosis (leflunomide and teriflunomide) and have been investigated in treatments of cancer, virus, and parasite infections (i.e., malaria) as well as in crop science.

Candidate: Brequinar. Type: Orally available, potent, and selective small molecule dihydroorotate dehydrogenase (DHODH) inhibitor designed to block host cell de novo pyrimidine biosynthesis.. Status: Clear Creek said September 1 it received FDA clearance on an IND application to study its lead drug candidate brequinar as a COVID-19 treatment, and has dosed the first patient in the Phase Ia CRISIS trial (NCT04425252).. The randomized, open label, multi-center study will enroll up to 24 patients hospitalized with COVID-19, with the aim of assessing the preliminary efficacy, safety, and tolerability of brequinar. The study will assign participants 1:2 to standard of care or standard of care plus five once-daily oral doses of 100 mg brequinar. The primary endpoint is safety/tolerability measured by rates of post randomization adverse events and hematology/chemistry safety labs. The trial was recruiting at four sites in Hartford, CT; Jacksonville, FL; Philadelphia; and Tampa, FL.. Clear Creek cited ...

Author: Muessig, C. et al.; Genre: Journal Article; Published in Print: 2006; Keywords: Arabidopsis/genetics/*physiology|br/|Arabidopsis Proteins/genetics/physiology|br/|*Gene Expression Regulation, Plant|br/|Oxidoreductases Acting on CH-CH Group Donors/genetics/physiology|br/|Plant Growth Regulators/genetics/*physiology|br/|Steroids/*physiology; Title: Molecular analysis of brassinosteroid action

DIHYDROOROTATE DEHYDROGENASE(2z)-2-Cyano-3-Hydroxy-N-[4-(Trifluoromethyl)phenyl]but-2-EnamideAcetate IonAntiproliferative Agent A771726Flavin MononucleotideOrotic Acid

The DHODH, or dihydroorotate dehydrogenase, gene encodes a 43-kDa enzymatic protein localized to the inner mitochondrial membrane, where it interacts with the mitochondrial respiratory chain and acts as a rate-limiting step in de novo pyrimidine biosynthesis (51-53). Mutations within DHODH have been linked with Miller Syndrome, a recessive disorder characterized by malformations of the limbs and eyes, among other symptoms (54-57). DHODH has also been investigated for a role in cancer, including melanoma (58) and acute myeloid leukemia (59), and decreased expression of DHODH was associated with breast cancer risk (60). Several other studies have examined the utility of DHODH inhibitors in cancer by inducing cell-cycle arrest and apoptosis in cancer cells (59, 61-66). Although DHODH has not been previously associated with lung cancer risk, the abundance of biological evidence for its pleiotropic role in cancer gives credibility to the association.. We identified significant associations on ...

Compare 2,4-dienoyl-CoA reductase 2, peroxisomal ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, and more.

2,4-Dienoyl-CoA reductase (EC 1.3.1.34) participates in beta-oxidation of (poly)unsaturated enoyl-CoAs and it appears in mammalian mitochondria as two isoforms with molecular masses of 120 and 60 kDa [Hakkola and Hiltunen (1993) Eur. J. Biochem. 215, 199-204]. The 120 kDa isomer is a homotetrameric enzyme, and here we report cDNA cloning of its subunit from human. cDNA clones were isolated by reverse transcriptase-PCR from a fibrosarcoma cell line and by screening from a human liver lambda gt11 cDNA library. The 1128 bp clone contained an open reading frame of 1008 bp encoding a polypeptide of 335 amino acid residues with a predicted molecular mass of 36066 Da. This polypeptide represents the immature monomer of the 120 kDa enzyme, and it contains a predicted N-terminal mitochondrial targeting signal. The amino acid (nucleotide) sequence of human 2,4-dienoyl-CoA reductase shows 82.7% (81.7%) similarity (identity) to the corresponding sequence from the rat. Northern-blot analysis gave a single ...

Broad-spectrum antiviral drugs targeting host processes could potentially treat a wide range of viruses while reducing the likelihood of emergent resistance. Despite great promise as therapeutics, such drugs remain largely elusive. Here we used parallel genome-wide high-coverage short hairpin RNA (shRNA) and clustered regularly interspaced short palindromic repeats (CRISPR)-Cas9 screens to identify the cellular target and mechanism of action of GSK983, a potent broad-spectrum antiviral with unexplained cytotoxicity. We found that GSK983 blocked cell proliferation and dengue virus replication by inhibiting the pyrimidine biosynthesis enzyme dihydroorotate dehydrogenase (DHODH). Guided by mechanistic insights from both genomic screens, we found that exogenous deoxycytidine markedly reduced GSK983 cytotoxicity but not antiviral activity, providing an attractive new approach to improve the therapeutic window of DHODH inhibitors against RNA viruses. Our results highlight the distinct advantages and ...

BRD9185 is a Dihydroorotate dehydrogenase (DHODH) inhibitor, with an EC50 of 16 nM against multidrug-resistant blood-stage parasites in vitro and is curative after just three doses in a P. berghei mouse model ...

This presentation outlines work as part of MMV to develop a new class of antimalarials targeting dihydroorotate dehydrogenase (DHODH). The triazolopyrimidines were identified as lead compounds; information is provided on their mode of action, and their efficacy and pharmacokinetics in animal models. ...

DUBLIN - The most solid conclusion that can be drawn from Immunic Inc.s phase II trial of IMU-838 in hospitalized COVID-19 patients is that a reduction in the need for invasive ventilation is no longer a useful endpoint for studies of COVID-19 drugs. The study randomized 233 hospitalized patients with moderate disease to receive either a twice daily dose of IMU-838 (vidofludimus calcium), an oral dihydroorotate dehydrogenase (DHOD) inhibitor, or placebo, over a 14-day treatment period. The primary endpoint was the proportion of patients without . . .

Complete information for DHCR24-DT gene (RNA Gene), DHCR24 Divergent Transcript, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium

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TY - JOUR. T1 - Candida tropicalis Etr1p and Saccharomyces cerevisiae Ybr026p (Mrf1p), 2-enoyl thioester reductases essential for mitochondrial respiratory competence. AU - Torkko, Juha. AU - Koivuranta, Kari. AU - Miinalainen, Ilkka. AU - Yagi, Ahmed. AU - Schmitz, Werner. AU - Kastaniotis, Alexander. AU - Airenne, Tomi. AU - Gurvitz, Aner. AU - Hiltunen, Kalervo. PY - 2001. Y1 - 2001. N2 - We report here on the identification and characterization of novel 2-enoyl thioester reductases of fatty acid metabolism, Etr1p from Candida tropicalis and its homolog Ybr026p (Mrf1′p) from Saccharomyces cerevisiae. Overexpression of these proteins in S. cerevisiae led to the development of significantly enlarged mitochondria, whereas deletion of the S. cerevisiae YBR026c gene resulted in rudimentary mitochondria with decreased contents of cytochromes and a respiration-deficient phenotype. Immunolocalization and in vivo targeting experiments showed these proteins to be predominantly mitochondrial. ...

Biliverdin reductase (BVR) is an enzyme (EC 1.3.1.24) found in all tissues under normal conditions, but especially in reticulo-macrophages of the liver and spleen. BVR facilitates the conversion of biliverdin to bilirubin via the reduction of a double-bond between the second and third pyrrole ring into a single-bond. There are two isozymes, in humans, each encoded by its own gene, biliverdin reductase A (BLVRA) and biliverdin reductase B (BLVRB). BVR acts on biliverdin by reducing its double-bond between the pyrrole rings into a single-bond. It accomplishes this using NADPH + H+ as an electron donor, forming bilirubin and NADP+ as products. BVR catalyzes this reaction through an overlapping binding site including Lys18, Lys22, Lys179, Arg183, and Arg185 as key residues. This binding site attaches to biliverdin, and causes its dissociation from heme oxygenase (HO) (which catalyzes reaction of ferric heme --> biliverdin), causing the subsequent reduction to bilirubin. BVR is composed of two ...

NADPH: protochlorophyllide oxidoreductase (POR) catalyses the light-dependent reduction of protochlorophyllide to chlorophyllide, a key regulatory reaction in the chlorophyll biosynthetic pathway. Sequence comparisons have revealed that POR is a member of the short-chain alcohol dehydrogenase family of enzymes. A tyrosine and a lysine residue are conserved throughout all members of this family, and are proposed to be within the active site. This present study describes how site-directed mutagenesis has been used to change Tyr-189 to Phe and Lys-193 to Arg in the Synechocystis POR enzyme. The mutant enzymes were produced with a His tag in Escherichia coli and subsequently purified on a Ni2+-affinity column. The two mutations resulted in inactive enzymes, indicating that both residues are crucial for activity. The Kd value for NADPH binding to the K193R mutant was significantly higher than for the wild-type enzyme, suggesting that the affinity for NADPH has also been reduced. ...

A procedure for the purification of the enzyme NADPH:protochlorophyllide oxidoreductase is described. This involves fractionation of sonicated oat etioplast membranes by discontinuous-sucrose-density-gradient centrifugation, which gives membranes in which the enzyme is present at a high specific activity. The enzyme is solubilized from the membranes with Triton X-100, followed by gel filtration of the extract; enzyme activity is eluted in fractions corresponding to a mol.wt of approx. 35000. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of the enzyme-containing fractions from gel filtration shows two peptides, of mol.wts. approx. 35000 and 37000. ...

EL HAMOURI B, OLIVER RP & GRIFFITHS WT (1983) Complexes of NADPH: protochlorophyllide oxidoreductase. Photobiochemistry Photobiophysics 6 305- ...

Protoporphyrinogen oxidase (Protox), an enzyme that catalyzes the common step of chlorophyll and heme biosynthetic pathways, was purified from spinach chloroplasts. The molecular weight of purified protein was estimated to be approximately 60,000 by SDS-PAGE. Protox activity was stimulated by addition of FAD, suggesting that chloroplast Protox requires FAD as a cofactor. Furthermore, the Protox-inhibiting herbicide, S23142, specifically inhibited the purified Protox activity at an IC50 value of 1 nM.. ...

AS07 227, HemY antibody, NP_681164, Anti-HemY | protoporphyrinogen oxidase antibodyHemY is an uncharacterized enzyme of heme biosynthesis. Immunogen: Overexpressed Thermosynechococcus elongatus HemY

Purchase Recombinant Bacillus thuringiensis Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit. It is produced in Yeast. High purity. Good price.

Complete information for DHCR7 gene (Protein Coding), 7-Dehydrocholesterol Reductase, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium

en] Protochlorophyllide (Pchlide) reductases are key enzymes in the process of chlorophyll biosynthesis. In this review, current knowledge on the molecular organization, substrate specificity and assembly of the light-dependent reduced nicotinamide adenine dinucleotide phosphate:Pchlide oxidoreductases are discussed. Characteristics of light-independent enzymes are also described briefly, and the possible reasons for the selection of light-dependent enzymes during the course of evolution are discussed ...

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InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.

|p|Despite the clinical success of Androgen Receptor (AR)-targeted therapies, reactivation of AR signalling remains the main driver of castration-r...

The tracing, of course, cannot be sent into the shop for the workmen to use, as it would soon become soiled and in time destroyed, so that it is necessary to have some cheap and rapid means of making ...

The link for light-induced protochlorophyllide reductase takes me to the blog for major histocompatability complex.. ReplyDelete ...

MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersChlorophyll and bacteriochlorphylllight-dependent protochlorophyllide reductase (TIGR01289; EC 1.3.1.33; HMM-score: 13.3) ...

PPOX antibody [N3C3] (protoporphyrinogen oxidase) for WB. Anti-PPOX pAb (GTX106163) is tested in Human samples. 100% Ab-Assurance.

Sasarman A, Letowski J, Czaika G, Ramirez V, Nead MA, Jacobs JM, Morais R. Nucleotide sequence of the hemG gene involved in the protoporphyrinogen oxidase activity of Escherichia coli K12. Canadian journal of microbiology.. 1993 Dec 0; 39(12):1155-61. ...

DE MORI, RENAN M.... Structural basis for the function and inhibition of dihydroorotate dehydrogenase from Schistosoma mansoni. FEBS Journal 288 n.3 p. JUN 2020. Journal article.

A maize gene encoding an NADPH binding enzyme highly homologous to isoflavone reductases is activated in response to sulfur starvation ...

This innovative concept consists of hull and core where are held all 8 bteps of the work-flow which make the concept functional. The core has several gears and turbines which are responsible for these 8 steps (5 of them are dedicated to the turbo stages). The first step is fuel compression, followed by 2 cold turbo levels. The fourth step is where the fuel starts burning - combustion stage, which creates thrust for the next, 5th step - thrust step, which provides power to the planetary gears and turbines and moves the system. This step is followed by two hot turbo steps and the circle is enclosed by the final 8th step - bigger turbine. All this motion in a retrodynamic circumstance effect, wich is plus higher RPM speed of self reaction motion, because is like when something go to a something is coming. Its a Rotary-Turbo-InFlow Technique principle ...

Human DHCR7 full-length ORF ( NP_001351.1, 1 a.a. - 475 a.a.) recombinant protein with GST-tag at N-terminal. (H00001717-P01) - Products - Abnova

This protein is identical to GenBank accession AAD18267 (genome position accession AE001598). This methylase is thought to promote the oxidation of protoporphyrinogen. (May have DNA methylating activity ...

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J:58465 Donoviel DB, Hadjantonakis AK, Ikeda M, Zheng H, Hyslop PS, Bernstein A, Mice lacking both presenilin genes exhibit early embryonic patterning defects. Genes Dev. 1999 Nov 1;13(21):2801-10 ...