A broad category of oxidoreductases that either reduce double bonds or oxidize single bonds between OXYGEN and CARBON in organic compounds.
Enzymes catalyzing the dehydrogenation of or oxidation of compounds containing primary amines.
The simplest saturated hydrocarbon. It is a colorless, flammable gas, slightly soluble in water. It is one of the chief constituents of natural gas and is formed in the decomposition of organic matter. (Grant & Hackh's Chemical Dictionary, 5th ed)
Oxidoreductases with specificity for oxidation or reduction of SULFUR COMPOUNDS.
A subclass of enzymes which includes all dehydrogenases acting on carbon-carbon bonds. This enzyme group includes all the enzymes that introduce double bonds into substrates by direct dehydrogenation of carbon-carbon single bonds.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Enzymes catalyzing the dehydrogenation of secondary amines, introducing a C=N double bond as the primary reaction. In some cases this is later hydrolyzed.
Physiologic methyl radical donor involved in enzymatic transmethylation reactions and present in all living organisms. It possesses anti-inflammatory activity and has been used in treatment of chronic liver disease. (From Merck, 11th ed)
An enzyme that catalyzes the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. Insulin is one of its substrates. EC 1.8.4.2.
Addition of methyl groups. In histo-chemistry methylation is used to esterify carboxyl groups and remove sulfate groups by treating tissue sections with hot methanol in the presence of hydrochloric acid. (From Stedman, 25th ed)
A sulfur-containing essential L-amino acid that is important in many body functions.
Individuals supplying living tissue, organs, cells, blood or blood components for transfer or transplantation to histocompatible recipients.
A ferredoxin-containing enzyme that catalyzes the COENZYME A-dependent oxidative decarboxylation of PYRUVATE to acetyl-COENZYME A and CARBON DIOXIDE.
A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).
Oxidoreductases that are specific for KETONES.
A family of thioltransferases that contain two active site CYSTEINE residues, which either form a disulfide (oxidized form) or a dithiol (reduced form). They function as an electron carrier in the GLUTHIONE-dependent synthesis of deoxyribonucleotides by RIBONUCLEOTIDE REDUCTASES and may play a role in the deglutathionylation of protein thiols. The oxidized forms of glutaredoxins are directly reduced by the GLUTATHIONE.
Non-cadaveric providers of organs for transplant to related or non-related recipients.
Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Hydrogen-donating proteins that participates in a variety of biochemical reactions including ribonucleotide reduction and reduction of PEROXIREDOXINS. Thioredoxin is oxidized from a dithiol to a disulfide when acting as a reducing cofactor. The disulfide form is then reduced by NADPH in a reaction catalyzed by THIOREDOXIN REDUCTASE.
Artificial, single or multilaminar vesicles (made from lecithins or other lipids) that are used for the delivery of a variety of biological molecules or molecular complexes to cells, for example, drug delivery and gene transfer. They are also used to study membranes and membrane proteins.
A technique using antibodies for identifying or quantifying a substance. Usually the substance being studied serves as antigen both in antibody production and in measurement of antibody by the test substance.
Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).
The complex formed by the binding of antigen and antibody molecules. The deposition of large antigen-antibody complexes leading to tissue damage causes IMMUNE COMPLEX DISEASES.
Exclusive legal rights or privileges applied to inventions, plants, etc.
An early local inflammatory reaction to insult or injury that consists of fever, an increase in inflammatory humoral factors, and an increased synthesis by hepatocytes of a number of proteins or glycoproteins usually found in the plasma.
Serum glycoproteins participating in the host defense mechanism of COMPLEMENT ACTIVATION that creates the COMPLEMENT MEMBRANE ATTACK COMPLEX. Included are glycoproteins in the various pathways of complement activation (CLASSICAL COMPLEMENT PATHWAY; ALTERNATIVE COMPLEMENT PATHWAY; and LECTIN COMPLEMENT PATHWAY).
A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)
A family of gram-positive, aerobic actinomycetes found in soil and animal tissue. Some species are the cause of infection in man and animals.
A procedure consisting of a sequence of algebraic formulas and/or logical steps to calculate or determine a given task.
An order of gram-positive, primarily aerobic BACTERIA that tend to form branching filaments.
An order of fungi in the phylum ASCOMYCOTA characterized by stromatic perithecial forms in most species. Notable genera are Magnaporthe and Glomerella, the latter having the anamorph (mitosporic form) COLLETOTRICHUM.
Proteins that are involved in the peptide chain termination reaction (PEPTIDE CHAIN TERMINATION, TRANSLATIONAL) on RIBOSOMES. They include codon-specific class-I release factors, which recognize stop signals (TERMINATOR CODON) in the MESSENGER RNA; and codon-nonspecific class-II release factors.
An autosomal recessive disorder of fatty acid oxidation, and branched chain amino acids (AMINO ACIDS, BRANCHED-CHAIN); LYSINE; and CHOLINE catabolism, that is due to defects in either subunit of ELECTRON TRANSFER FLAVOPROTEIN or its dehydrogenase, electron transfer flavoprotein-ubiquinone oxidoreductase (EC 1.5.5.1).
Flavoproteins that serve as specific electron acceptors for a variety of DEHYDROGENASES. They participate in the transfer of electrons to a variety of redox acceptors that occur in the respiratory chain.
A flavoprotein enzyme that is responsible for the catabolism of LYSINE; HYDROXYLYSINE; and TRYPTOPHAN. It catalyzes the oxidation of GLUTARYL-CoA to crotonoyl-CoA using FAD as a cofactor. Glutaric aciduria type I is an inborn error of metabolism due to the deficiency of glutaryl-CoA dehydrogenase.
Disorders affecting amino acid metabolism. The majority of these disorders are inherited and present in the neonatal period with metabolic disturbances (e.g., ACIDOSIS) and neurologic manifestations. They are present at birth, although they may not become symptomatic until later in life.
Brain disorders resulting from inborn metabolic errors, primarily from enzymatic defects which lead to substrate accumulation, product reduction, or increase in toxic metabolites through alternate pathways. The majority of these conditions are familial, however spontaneous mutation may also occur in utero.
Systematic efforts to assist individuals in selecting an occupation or suitable employment on the basis of aptitude, education, etc.
A enzyme that catalyzes the transfer of acetyl groups from ACETYL CoA to acyl-carrier protein to form COENZYME A and acetyl-acyl-carrier protein.
An NAD-dependent enzyme that catalyzes the oxidation of acyl-[acyl-carrier protein] to trans-2,3-dehydroacyl-[acyl-carrier protein]. It has a preference for acyl groups with a carbon chain length between 4 to 16.
An enzyme that catalyzes the oxidation of acyl-[acyl-carrier protein] to trans-2,3-dehydroacyl-[acyl-carrier protein] in the fatty acid biosynthesis pathway. It has a preference for acyl derivatives with carbon chain length from 4 to 16.
Consists of a polypeptide chain and 4'-phosphopantetheine linked to a serine residue by a phosphodiester bond. Acyl groups are bound as thiol esters to the pantothenyl group. Acyl carrier protein is involved in every step of fatty acid synthesis by the cytoplasmic system.
A 3-oxoacyl reductase that has specificity for ACYL CARRIER PROTEIN-derived FATTY ACIDS.
This enzyme catalyzes the transacylation of malonate from MALONYL CoA to activated holo-ACP, to generate malonyl-(acyl-carrier protein), which is an elongation substrate in FATTY ACIDS biosynthesis. It is an essential enzyme in the biosynthesis of FATTY ACIDS in all BACTERIA.
Congener of CYTARABINE that is metabolized to cytarabine and thereby maintains a more constant antineoplastic action.

Oxidized derivatives of 7-dehydrocholesterol induce growth retardation in cultured rat embryos: a model for antenatal growth retardation in the Smith-Lemli-Opitz syndrome. (1/834)

7-Dehydrocholesterol accumulates in fetuses affected by the Smith-Lemli-Opitz syndrome as a result of a deficit in the ultimate step of cholesterol synthesis catalyzed by Delta7 reductase. Rat embryos explanted at gestation day 10 and cultured for 48 h in the presence of the Delta7 reductase inhibitor AY 9944 were used as a model to discriminate between the beneficial effect of supplementation with cholesterol and the deleterious effect of supplementation with 7-dehydrocholesterol. Cholesterol supplementation in the form of mixed cholesterol/lecithin liposomes added to serum serving as the culture medium restores the growth of embryos which is markedly decreased in the presence of the inhibitor. 7-Dehydrocholesterol under identical conditions does not restore growth and impairs the beneficial effect of cholesterol added simultaneously. UV-photooxidation of 7-dehydrocholesterol-supplemented culture medium enhances its embryotoxicity, which suggests uptake by the embryo of toxic by-products formed from 7-dehydrocholesterol. By contrast photooxidation of cholesterol-supplemented culture medium does not induce embryotoxicity. alpha-Tocopherol reduces the toxicity of photooxidized 7-dehydrocholesterol supplementing the culture medium. We conclude that 7-dehydrocholesterol does not fulfill the cholesterol requirement of the developing embryos and exerts an additional embryotoxic effect probably via oxidized by-products. This could explain the antenatal growth retardation of SLOS by a blockage of the maternal compensatory cholesterol influx.  (+info)

Evolution of plant defense mechanisms. Relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductases. (2/834)

Pinoresinol-lariciresinol and isoflavone reductase classes are phylogenetically related, as is a third, the so-called "isoflavone reductase homologs." This study establishes the first known catalytic function for the latter, as being able to engender the NADPH-dependent reduction of phenylcoumaran benzylic ethers. Accordingly, all three reductase classes are involved in the biosynthesis of important and related phenylpropanoid-derived plant defense compounds. In this investigation, the phenylcoumaran benzylic ether reductase from the gymnosperm, Pinus taeda, was cloned, with the recombinant protein heterologously expressed in Escherichia coli. The purified enzyme reduces the benzylic ether functionalities of both dehydrodiconiferyl alcohol and dihydrodehydrodiconiferyl alcohol, with a higher affinity for the former, as measured by apparent Km and Vmax values and observed kinetic 3H-isotope effects. It abstracts the 4R-hydride of the required NADPH cofactor in a manner analogous to that of the pinoresinol-lariciresinol reductases and isoflavone reductases. A similar catalytic function was observed for the corresponding recombinant reductase whose gene was cloned from the angiosperm, Populus trichocarpa. Interestingly, both pinoresinol-lariciresinol reductases and isoflavone reductases catalyze enantiospecific conversions, whereas the phenylcoumaran benzylic ether reductase only shows regiospecific discrimination. A possible evolutionary relationship among the three reductase classes is proposed, based on the supposition that phenylcoumaran benzylic ether reductases represent the progenitors of pinoresinol-lariciresinol and isoflavone reductases.  (+info)

BadR, a new MarR family member, regulates anaerobic benzoate degradation by Rhodopseudomonas palustris in concert with AadR, an Fnr family member. (3/834)

A cluster of genes for the anaerobic degradation of benzoate has been described for the phototrophic bacterium Rhodopseudomonas palustris. Here we provide an initial analysis of the regulation of anaerobic benzoate degradation by examining the contributions of two regulators: a new regulator, BadR, encoded by the benzoate degradation gene cluster, and a previously described regulator, AadR, whose gene lies outside the cluster. Strains with single mutations in either badR or aadR grew slowly on benzoate but were relatively unimpaired in growth on succinate and several intermediates of benzoate degradation. A badR aadR double mutant was completely defective in anaerobic growth on benzoate. Effects of the regulators on transcriptional activation were monitored with an R. palustris strain carrying a chromosomal fusion of 'lacZ to the badE gene of the badDEFG operon. This operon encodes benzoyl-coenzyme A (benzoyl-CoA) reductase, an unusual oxygen-sensitive enzyme that catalyzes the benzene ring reduction reaction that is the rate-limiting step in anaerobic benzoate degradation. Expression of badE::'lacZ was induced 100-fold when cells grown aerobically on succinate were shifted to anaerobic growth on succinate plus benzoate. The aadR gene was required for a 20-fold increase in expression that occurred in response to anaerobiosis, and badR was responsible for a further 5-fold increase in expression that occurred in response to benzoate. Further studies with the badE::'lacZ fusion strain grown with various kinds of aromatic acids indicated that BadR probably responds to benzoyl-CoA acting as an effector molecule. Sequence information indicates that BadR is a member of the MarR family of transcriptional regulators. These studies expand the range of functions regulated by MarR family members to include anaerobic aromatic acid degradation and provide an example of a MarR-type protein that acts as a positive regulator rather than as a negative regulator, as do most MarR family members. AadR resembles the Escherichia coli Fnr regulator in sequence and contains cysteine residues that are spaced appropriately to serve in the capacity of a redox-sensing protein.  (+info)

Site-directed mutagenesis of a possible type 1 copper ligand of bilirubin oxidase; a Met467Gln mutant shows stellacyanin-like properties. (4/834)

In our previous paper, we reported a mutant of recombinant Myrothecium verrucaria bilirubin oxidase, in which the Met467 residue was replaced by Gly [Shimizu, A. et al. (1999) Biochemistry 38, 3034-3042]. This mutant displayed a remarkable reduction in enzymatic activity and an evident decrease in the intensity of the absorption band around 600 nm (type 1 charge transfer transition). In this study, we report the preparation of three Met467 mutants (Met467Gln, Met467His, and Met467Arg) and characterize their enzymatic activities, midpoint potentials, and absorption and ESR spectra. Met467His and Met467Arg show no enzymatic activity and a great reduction in the intensity of the absorption band around 600 nm. Furthermore, their ESR spectra show no type 1 copper signal, but only a type 2 copper signal; however, oxidation by ferricyanide caused the type 1 copper signal to appear. On the other hand, Met467Gln as expressed shows both type 1 and type 2 copper signals in its ESR spectrum, the type 1 copper atom parameters being very different from usual blue copper proteins but very similar to those of stellacyanin. The enzymatic activity of the Met467Gln mutant for bilirubin is quite low (0.3%), but the activity for potassium ferrocyanide is similar (130%) to that of the wild type enzyme. These results indicate that Met467 is important for characterizing the features of the type 1 copper of bilirubin oxidase.  (+info)

Ineffective vitamin D synthesis in cats is reversed by an inhibitor of 7-dehydrocholestrol-delta7-reductase. (5/834)

Changes in plasma 25-hydroxyvitamin D (25-OHD) were used as an index of vitamin D status of cats. Plasma 25-OHD concentration of kittens given a purified vitamin D-free diet and exposed to direct summer sun for 15 h/wk declined at a similar rate as kittens given the same diet kept indoors. Similarly, plasma 25-OHD of kittens exposed to ultraviolet (UV) lamps declined at a similar rate as kittens not exposed, and these kittens developed clinical signs of vitamin D deficiency. Eight weaned kittens were given the vitamin D-free purified diet until their plasma concentrations of 25-OHD were < 5 nmol/L. They then had the hair on their backs clipped at weekly intervals and were paired on the basis of skin color and exposed to UV light for 2 h/d. One member of each pair was given an inhibitor of 7-dehydrocholesterol (5, 7-cholestradien-3beta-ol)-delta7-reductase (EC 1.3.1.21) in the diet. Cats receiving the inhibitor had a progressive increase in 25-OHD concentration of plasma with time to 91 +/- 22 nmol/L (mean +/- SEM), whereas cats not receiving the inhibitor had plasma 25-OHD concentrations that were not detectable (P < 0.001). Biopsy samples of skin from cats receiving the inhibitor had more than five times the concentration of 7-dehydrocholesterol (P < 0.001) than the skin of control cats. Low concentration of 7-dehydrocholesterol (presumably due to high activity of the reductase) in the skin of cats is the major impediment to effective vitamin D synthesis. Analysis of wild caught potential prey of cats indicated that these animals could supply adequate vitamin D to meet the requirement of growing kittens.  (+info)

Identification of peroxisomal proteins by using M13 phage protein VI phage display: molecular evidence that mammalian peroxisomes contain a 2,4-dienoyl-CoA reductase. (6/834)

To elucidate unknown mammalian peroxisomal enzymes and functions, we subjected M13 phage expressing fusions between the gene encoding protein VI and a rat liver cDNA library to an immunoaffinity selection process in vitro (biopanning) with the use of antibodies raised against peroxisomal subfractions. In an initial series of biopanning experiments, four different cDNA clones were obtained. These cDNA species encoded two previously identified peroxisomal enzymes, catalase and urate oxidase, and two novel proteins that contained a C-terminal peroxisomal targeting signal (PTS1). A primary structure analysis of these novel proteins revealed that one, ending in the tripeptide AKL, is homologous to the yeast peroxisomal 2,4-dienoyl-CoA reductase (EC 1.3.1.34; DCR), an enzyme required for the degradation of unsaturated fatty acids, and that the other, ending in the tripeptide SRL, is a putative member of the short-chain dehydrogenase/reductase (SDR) family, with three isoforms. Green fluorescent protein (GFP) fusions encoding GFP-DCR-AKL, GFP-DCR, GFP-SDR-SRL and GFP-SDR were expressed in mammalian cells. The analysis of the subcellular location of the recombinant fusion proteins confirmed the peroxisomal localization of GFP-DCR-AKL and GFP-SDR-SRL, as well as the functionality of the PTS1. That the AKL protein is indeed an NADPH-dependent DCR was demonstrated by showing DCR activity of the bacterially expressed protein. These results demonstrate at the molecular level that mammalian peroxisomes do indeed contain a DCR. In addition, the results presented here indicate that the protein VI display system is suitable for the isolation of rare cDNA clones from cDNA libraries and that this technology facilitates the identification of novel peroxisomal proteins.  (+info)

A functional 4-hydroxysalicylate/hydroxyquinol degradative pathway gene cluster is linked to the initial dibenzo-p-dioxin pathway genes in Sphingomonas sp. strain RW1. (7/834)

The bacterium Sphingomonas sp. strain RW1 is able to use dibenzo-p-dioxin, dibenzofuran, and several hydroxylated derivatives as sole sources of carbon and energy. We have determined and analyzed the nucleic acid sequence of a 9,997-bp HindIII fragment downstream of cistrons dxnA1A2, which encode the dioxygenase component of the initial dioxygenase system of the corresponding catabolic pathways. This fragment contains 10 colinear open reading frames (ORFs), apparently organized in one compact operon. The enzymatic activities of some proteins encoded by these genes were analyzed in the strain RW1 and, after hyperexpression, in Escherichia coli. The first three ORFs of the locus, designated dxnC, ORF2, and fdx3, specify a protein with a low homology to bacterial siderophore receptors, a polypeptide representing no significant homology to known proteins, and a putative ferredoxin, respectively. dxnD encodes a 69-kDa phenol monooxygenase-like protein with activity for the turnover of 4-hydroxysalicylate, and dxnE codes for a 37-kDa protein whose sequence and activity are similar to those of known maleylacetate reductases. The following gene, dxnF, encodes a 33-kDa intradiol dioxygenase which efficiently cleaves hydroxyquinol, yielding maleylacetate, the ketoform of 3-hydroxy-cis,cis-muconate. The heteromeric protein encoded by dxnGH is a 3-oxoadipate succinyl coenzyme A (succinyl-CoA) transferase, whereas dxnI specifies a protein exhibiting marked homology to acetyl-CoA acetyltransferases (thiolases). The last ORF of the sequenced fragment codes for a putative transposase. DxnD, DxnF, DxnE, DxnGH, and DxnI (the activities of most of them have also been detected in strain RW1) thus form a complete 4-hydroxysalicylate/hydroxyquinol degradative pathway. A route for the mineralization of the growth substrates 3-hydroxydibenzofuran and 2-hydroxydibenzo-p-dioxin in Sphingomonas sp. strain RW1 thus suggests itself.  (+info)

Characterization of a novel cis-benzene dihydrodiol dehydrogenase from Pseudomonas putida ML2. (8/834)

A second and novel cis-benzene dihydrodiol dehydrogenase which is able to dehydrogenate a range of cis-dihydrodiols and other vicinal alcohols has been purified from Pseudomonas putida ML2. The enzyme is a tetramer of a polypeptide of 39 kDa in molecular mass and has a pH optimum of 9.0. Despite having a primary structure that has significant similarity to glycerol dehydrogenases, the kcat/Km value of the enzyme for cis-benzene dihydrodiol is 4300-fold higher compared to glycerol. The apparent Km values of the enzyme for cis-benzene dihydrodiol and glycerol are 0.01 mM and 46 mM, respectively, and 0.22 mM for NAD+.  (+info)

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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
Gentaur molecular products has all kinds of products like :search , Zyagen \ DHODH Antibody \ BIN-001723-M01 for more molecular products just contact us
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 ...
Monoklonale und polyklonale Biliverdin Reductase Antikörper für viele Methoden. Ausgesuchte Qualitäts-Hersteller für Biliverdin Reductase Antikörper. Hier bestellen.
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 ...
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 ...
This enzyme belongs to oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The ... Mondovi B, Costa MT, Agro AF, Rotilio G (1967). "Pyridoxal phosphate as a prosthetic group of pig kidney diamine oxidase". Arch ... urea cycle and metabolism of amino groups, glycine, serine and threonine metabolism, histidine metabolism, tyrosine metabolism ... systematic name of this enzyme class is amine:oxygen oxidoreductase (deaminating) (copper-containing). This enzyme participates ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other ... The systematic name of this enzyme class is all-trans-13,14-dihydroretinol:acceptor 13,14-oxidoreductase. Other names in common ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other ... The systematic name of this enzyme class is L-pipecolate:acceptor 1,6-oxidoreductase. This enzyme is also called L-pipecolate:( ... acceptor) 1,6-oxidoreductase. This enzyme participates in lysine degradation. Baginsky ML, Rodwell VW (1967). "Metabolism of ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with other ... The systematic name of this enzyme class is taurine:acceptor oxidoreductase (deaminating). This enzyme is also called taurine:( ... acceptor) oxidoreductase (deaminating). This enzyme participates in nitrogen metabolism. Kondo H, Kagotani K, Oshima M, ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other ... The systematic name of this enzyme class is coproporphyrinogen-III:S-adenosyl-L-methionine oxidoreductase (decarboxylating). ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... The systematic name of this enzyme class is D-glucose:acceptor 1-oxidoreductase. Other names in common use include glucose ... dehydrogenase (Aspergillus), glucose dehydrogenase (decarboxylating), and D-glucose:(acceptor) 1-oxidoreductase. This enzyme ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... The systematic name of this enzyme class is choline:acceptor 1-oxidoreductase. Other names in common use include choline ... oxidase, choline-cytochrome c reductase, choline:(acceptor) oxidoreductase, and choline:(acceptor) 1-oxidoreductase. This ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donor with other ... Instead, the demethylation of the N-methyl group on sarcosine occurs directly. The reduced FADH− from the first step then is ... Sarcosine dehydrogenase contains a covalently bound FAD group " linked via the 8 alpha position of the isoalloxazine ring to an ... The systematic name of this enzyme class is sarcosine:acceptor oxidoreductase (demethylating). Other names in common use ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... The systematic name of this enzyme class is 2-dehydro-D-gluconate:acceptor 2-oxidoreductase. Other names in common use include ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... The systematic name of this enzyme class is D-fructose:acceptor 5-oxidoreductase. Other names in common use include fructose 5- ... dehydrogenase (acceptor), D-fructose dehydrogenase, and D-fructose:(acceptor) 5-oxidoreductase. Ameyama M; Adachi O (1982). "[ ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... The systematic name of this enzyme class is polyvinyl-alcohol:acceptor oxidoreductase. Other names in common use include PVA ... dehydrogenase, and polyvinyl-alcohol:(acceptor) oxidoreductase. It employs one cofactor, PQQ. Shimao M, Ninomiya K, Kuno O, ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other ... The systematic name of this enzyme class is 5-methyltetrahydromethanopterin:coenzyme-F420 oxidoreductase. Other names in common ... coenzyme-F420 oxidoreductase. This enzyme participates in folate biosynthesis. As of late 2007, only one structure has been ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... The systematic name of this enzyme class is 3-hydroxycyclohexanone:acceptor 1-oxidoreductase. Dangel W, Tschech A, Fuchs G ( ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... The systematic name of this enzyme class is alkan-1-ol:acceptor oxidoreductase. Other names in common use include polyethylene ... 1985). "Identification of the prosthetic group and further characterization of a novel enzyme, polyethylene-glycol ... glycol dehydrogenase, and alkan-1-ol:(acceptor) oxidoreductase. This enzyme participates in fatty acid metabolism. It employs ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... hexopyranoside-cytochrome c oxidoreductase, and D-aldohexoside:(acceptor) 3-oxidoreductase. Hayano K, Fukui S (August 1967). " ... The systematic name of this enzyme class is D-aldohexoside:acceptor 3-oxidoreductase. Other names in common use include D- ... glucoside 3-dehydrogenase, D-aldohexopyranoside dehydrogenase, D-aldohexoside:cytochrome c oxidoreductase, D-glucoside 3- ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other ... prosthetic groups, electron donor, and genes of a member of the molybdenum-flavin-iron-sulfur proteins". Eur. J. Biochem. 251 ( ... The systematic name of this enzyme class is benzoyl-CoA:acceptor oxidoreductase. Other names in common use include: 4- ... hydroxybenzoyl-CoA reductase (dehydroxylating), and 4-hydroxybenzoyl-CoA:(acceptor) oxidoreductase. Glockler R, Tschech A, ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... The systematic name of this enzyme class is (S)-lactate:oxaloacetate oxidoreductase. This enzyme is also called malate-lactate ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with other ... The systematic name of this enzyme class is glycine:acceptor oxidoreductase (hydrogen-cyanide-forming). Other names in common ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... The systematic name of this enzyme class is pyridoxine:acceptor 5-oxidoreductase. Other names in common use include pyridoxal-5 ... 5-oxidoreductase. This enzyme participates in vitamin B6 metabolism. It has 2 cofactors: FAD, and PQQ. Sundaram TK, Snell EE ( ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... The systematic name of this enzyme class is (S)-3-hydroxybutanoate:2-oxoglutarate oxidoreductase. This enzyme is also called ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... The systematic name of this enzyme class is (R)-2-hydroxy-acid:acceptor 2-oxidoreductase. Other names in common use include D-2 ... acid dehydrogenase, and (R)-2-hydroxy-acid:(acceptor) 2-oxidoreductase. It has 2 cofactors: FAD, and Zinc. Gregolin C, Singer ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... The systematic name of this enzyme class is D-gluconate:acceptor 2-oxidoreductase. Other names in common use include gluconate ... 2-oxidoreductase. This enzyme participates in pentose phosphate pathway. It employs one cofactor, FAD. Matsushita K, Shinagawa ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other ... The systematic name of this enzyme class is cyclohexanone:acceptor 2-oxidoreductase. This enzyme is also called cyclohexanone:( ... acceptor) 2-oxidoreductase. Dangel W, Tschech A, Fuchs G (1989). "Enzyme-reactions involved in anaerobic cyclohexanol ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other ... The systematic name of this enzyme class is 5,10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase. Other names in ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... The systematic name of this enzyme class is (S)-2-hydroxy-2-phenylacetate:acceptor 2-oxidoreductase. This enzyme transfers the ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other ... The systematic name of this enzyme class is 2-methylbutanoyl-CoA:acceptor oxidoreductase. Other names in common use include ... oxidoreductase. This enzyme participates in valine, leucine and isoleucine degradation. Ikeda Y, Dabrowski C, Tanaka K (1983 ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other ... It was created by a group containing K.A.Tiffany, D.L.Roberts, M.Wang, R.Paschke, A.-W.A.Mohsen, J.Vockley, and J.J.P.Kim. The ... The systematic name of this enzyme class is 3-methylbutanoyl-CoA:acceptor oxidoreductase. Other names in common use include ... isovaleryl-coenzyme A dehydrogenase, isovaleroyl-coenzyme A dehydrogenase, and 3-methylbutanoyl-CoA:(acceptor) oxidoreductase. ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... The systematic name of this enzyme class is glycolate:acceptor 2-oxidoreductase. Other names in common use include glycolate ... Lord JM (May 1972). "Glycolate oxidoreductase in Escherichia coli". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 267 (2 ... oxidoreductase, glycolic acid dehydrogenase, and glycolate:(acceptor) 2-oxidoreductase. This enzyme participates in glyoxylate ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other ... The systematic name of this enzyme class is N-methyl-L-glutamate:acceptor oxidoreductase (demethylating). Other names in common ... use include N-methylglutamate dehydrogenase, and N-methyl-L-glutamate:(acceptor) oxidoreductase (demethylating). This enzyme ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other ... 1-en-oxido-reductase, Delta1-steroid reductase, and 3-oxosteroid:(acceptor) Delta1-oxidoreductase. LEVY HR, TALALAY P (1959). " ... The systematic name of this enzyme class is 3-oxosteroid:acceptor Delta1-oxidoreductase. Other names in common use include 3- ...
The Gene Ontology (GO) project is a collaborative effort to address the need for consistent descriptions of gene products across databases. You can use this browser to view terms, definitions, and term relationships in a hierarchical display. Links to summary annotated gene data at MGI are provided in Term Detail reports.
... protochlorophyllide oxidoreductase is observed. Within the first 5 min of continuous light approximately 90% of the enzyme ... Oxidoreductases / metabolism * Oxidoreductases / radiation effects* * Oxidoreductases Acting on CH-CH Group Donors* ... During the illumination of etiolated barley plants a rapid decline of the NADPH: protochlorophyllide oxidoreductase is observed ... protochlorophyllide oxidoreductase Eur J Biochem. 1981 Nov;120(1):95-103. doi: 10.1111/j.1432-1033.1981.tb05674.x. ...
A homogeneous phase reaction occurs with the antibody and complement acting to release the enzyme if an immunospecific antigen- ... 1. Oxidoreductases. 1.1 Acting on the CH--OH group of donors. 1.1.1 With NAD or NADP as acceptor ... 5. A liposome in accordance with claim 1 wherein said enzyme is selected from the group consisting of oxidoreductases, ... Foremost amongst these are: amino groups derived from phosphatidyl ethanolamine, hydroxyl groups provided by phosphatidyl ...
... protochlorophyllide oxidoreductase (POR), a nuclear-encoded plastid-localized enzyme, catalyzes the photoreduction of ... Oxidoreductases / genetics * Oxidoreductases / metabolism* * Oxidoreductases Acting on CH-CH Group Donors* * Phytochrome / ... Distinct roles for light-dependent NADPH:protochlorophyllide oxidoreductases (POR) A and B during greening in higher plants ... Light-dependent NADPH:protochlorophyllide oxidoreductase (POR), a nuclear-encoded plastid-localized enzyme, catalyzes the ...
oxidoreductase activity, acting on the CH-CH group of donors Source: InterPro ... OxidoreductaseUniRule annotation. ,p>Information which has been generated by the UniProtKB automatic annotation system, without ... FAD-dependent oxidoreductaseImported. ,p>Information which has been imported from another database using automatic procedures ... It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.,p>,a href=/help ...
GO:0016491 (oxidoreductase activity). GO:0016627 (oxidoreductase activity, acting on the CH-CH group of donors). GO:0050660 ( ...
Oxidoreductases;. Acting on the CH-OH group of donors;. With NAD+ or NADP+ as acceptor. BRITE hierarchy. ... The enzyme oxidizes a hydroxyl group on ring A, converting it to an oxo group.. ... 3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide-a:NAD+ oxidoreductase (bacteriochlorophyllide a-forming). ...
Oxidoreductases;. Acting on the CH-CH group of donors;. With NAD+ or NADP+ as acceptor. BRITE hierarchy. ...
Oxidoreductases Acting on CH-CH Group Donors); EC 1.3.1.38 (trans-2-enoyl-CoA reductase (NADPH)); EC 2.3.1.- ( ... Oxirredutases atuantes sobre Doadores de Grupo CH-CH/gen tica. Oxirredutases atuantes sobre Doadores de Grupo CH-CH/metabolismo ... Although several groups have reported butyrate production under oxygen-limited conditions by a native producer, Clostridium ... 107-92-6 (Butyric Acid); 8PJ61P6TS3 (1-Butanol); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.36 (acetoacetyl-CoA reductase); ...
oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor Source: InterPro ... OxidoreductaseARBA annotation. ,p>Information which has been generated by the UniProtKB automatic annotation system, without ... It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.,p>,a href=/help ... Phytochromobilin:ferredoxin oxidoreductase, chloroplasticImported. Automatic assertion inferred from database entriesi ...
Oxidoreductases EC 1.3.- Oxidoreductases Acting on CH-CH Group Donors EC 1.3.1.21 7-dehydrocholesterol reductase IM Am J (...) ... Animals Cholesterol metabolism Humans Morphogenesis Oxidoreductases genetics Oxidoreductases Acting on CH-CH Group Donors Smith ... group A, n = 9; group B, n = 10; group C, n = 9) were ... group C1). To determine whether the changes in CH metabolism ... Dutch Advisory Group on Growth Hormone. (PubMed). Carbohydrate metabolism during long-term growth hormone (GH) treatment and ...
C12N9/001-Oxidoreductases (1.) acting on the CH-CH group of donors (1.3) ... A suitable HFC is 1,1-difluoroethane (CH3CHF2), commercially available as Dymel 152A from Dupont. The concentration of Dymel ... The acid can be selected from the group consisting of sodium bisulfate, citric acid, acetic acid, nitrous acid, hydrocyanic ... Bleaching activators can be compounds with O- or N-bounded acetyl groups that react with the strongly nucleophilic hydroperoxy ...
Extrapolation of clinical trial results comparing warfarin and direct-acting oral anticoagulant (DOAC) users experiencing major ... Oxidoreductases Acting On Ch-ch Group Donors. A subclass of enzymes which includes all dehydrogenases acting on carbon-carbon ... This enzyme group includes all the enzymes that introduce double bonds into substrates by direct dehydrogenation of carbon- ... It is a direct-acting smooth muscle relaxant used in the treatment of impotence and as a vasodilator, especially for cerebral ...
Oxidoreductases Acting on CH-NH Group Donors*. Polycystic Kidney Diseases / pathology. Prenatal Diagnosis. ... Oxidoreductases Acting on CH-NH Group Donors; EC 1.5.5.1/electron-transferring-flavoprotein dehydrogenase ... The childs 3-day extrauterine life was ch ...
Oxidoreductases: 9264*Oxidoreductases Acting on CH-CH Group Donors*B-Specific) Enoyl-(Acyl-Carrier Protein) Reductase (NADPH*S ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... The systematic name of this enzyme class is carnitine:NAD+ 3-oxidoreductase. ...
GO:0016638 oxidoreductase activity, acting on the CH-NH2 group of donors ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ ... The systematic name of this enzyme class is n-alkanal:NAD(P)+ 2-oxidoreductase. Other names in common use include NAD(P)H- ... dependent alkenal/one oxidoreductase, and NADPH:2-alkenal alpha,beta-hydrogenase. Structural studies[edit]. As of late 2007, ... 2002). "The NADPH:quinone oxidoreductase P1-zeta-crystallin in Arabidopsis catalyzes the alpha,beta-hydrogenation of 2-alkenals ...
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor IBA. CGD:CAL0000189861, PANTHER: ... oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (IBA). ... oxidoreductase activity IBA. PANTHER:PTN000041225, SGD:S000003125. 2290270. (PMID:21873635). GO_Central. PMID:21873635. ...
The amino groups may be introduced into the polymer by reduction of nitrile groups with lithium aluminum hydride in an inert ... or covalent bonding to a micro-porous water-insoluble acrylonitrile polymer containing from 20 μM to 1000 μM of amino groups ... C12N9/0006-Oxidoreductases (1.) acting on CH-OH groups as donors (1.1) ... especially chlorine atom groups, to substitute chlorine atom groups with free amino groups. Alternatively, an acrylonitrile ...
1. Oxidoreductases. 1.1 Acting on the CH-OH group of donors. 1.1.1 With NAD+ or NADP+ as acceptor. 1.1.1.110 aromatic 2-oxoacid ... Oxidoreductases;. Acting on the CH-OH group of donors;. With NAD+ or NADP+ as acceptor. BRITE hierarchy. ... indolelactate:NAD+ oxidoreductase;. indolelactate dehydrogenase;. fldH (gene name);. (indol-3-yl)lactate:NAD+ oxidoreductase. ...
GO:0016491 [oxidoreductase activity]. GO:0016627 [oxidoreductase activity, acting on the CH-CH group of donors]. GO:0016787 [ ... GO:0016491 [oxidoreductase activity]. GO:0016627 [oxidoreductase activity, acting on the CH-CH group of donors]. GO:0016787 [ ... GO:0016627 [oxidoreductase activity, acting on the CH-CH group of donors]. GO:0050660 [flavin adenine dinucleotide binding]. GO ... For each group, a list of included tissues is accessed by clicking on group name, group symbol, RNA bar, or protein bar. ...
GO:0016491 [oxidoreductase activity]. GO:0016614 [oxidoreductase activity, acting on CH-OH group of donors]. GO:0016740 [ ... GO:0016491 [oxidoreductase activity]. GO:0016614 [oxidoreductase activity, acting on CH-OH group of donors]. GO:0016740 [ ... For each group, a list of included tissues is accessed by clicking on group name, group symbol, RNA bar, or protein bar. ... Color-coding is based on tissue groups, each consisting of tissues with functional features in common. To access sample data, ...
oxidoreductase activity, acting on the CH-CH group of donors. IEA. --. GO:0050660. flavin adenine dinucleotide binding. IEA. -- ...
oxidoreductase activity, acting on the ch-oh group of donors, nad or nadp as acceptor. ... oxidoreductase activity, acting on ch-oh group of donors. oxidoreductase activity. Molecular Function. ...
Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor. ... oxidoreductase activity, acting on the ch-oh group of donors, nad or nadp as acceptor. ... oxidoreductase activity, acting on ch-oh group of donors. oxidoreductase activity. Molecular Function. ...
oxidoreductase activity, acting on the ch-oh group of donors, nad or nadp as acceptor. ... oxidoreductase activity, acting on ch-oh group of donors. oxidoreductase activity. Molecular Function. ...
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 1. DR ... KW FAD {ECO:0000256,PIRSR:PIRSR000137-2}; KW Flavoprotein {ECO:0000256,PIRSR:PIRSR000137-2}; KW Oxidoreductase {ECO:0000313, ...
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor IEA Inferred from Electronic Annotation. ... Cysteine is synthesized from serine through different pathways in different organism groups. In bacteria and plants, cysteine ... Cysteine is synthesized from serine through different pathways in different organism groups. In bacteria and plants, cysteine ...
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro. DR Gene3D; 1.10.540.10; -; 1. ...
  • A homogeneous phase reaction occurs with the antibody and complement acting to release the enzyme if an immunospecific antigen-antibody. (google.com)
  • 5. A liposome in accordance with claim 1 wherein said enzyme is selected from the group consisting of oxidoreductases, hydrolases and mixtures thereof. (google.com)
  • The enzyme oxidizes a hydroxyl group on ring A, converting it to an oxo group. (genome.jp)
  • This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. (wikipedia.org)
  • The systematic name of this enzyme class is (R)-2-hydroxy-acid:acceptor 2-oxidoreductase. (wikipedia.org)
  • This protein is a cytosolic enzyme encoded by a housekeeping X-linked gene whose main function is to produce NADPH, a key electron donor in the defense against oxidizing agents and in reductive biosynthetic reactions. (genecards.org)
  • The systematic name of this enzyme class is n-alkanal:NAD(P)+ 2-oxidoreductase . (wikipedia.org)
  • Several new major enzyme categories include: DNA Repair Enzymes, Metalloexopeptidases, Oxidoreductases Acting on CH-CH Group Donors, Proprotein Convertases, and Ubiquitin-Protein Ligase Complexes. (nih.gov)
  • The systematic name of this enzyme class is amine:oxygen oxidoreductase (deaminating) (copper-containing). (wikipedia.org)
  • This enzyme participates in 8 metabolic pathways: urea cycle and metabolism of amino groups, glycine, serine and threonine metabolism, histidine metabolism, tyrosine metabolism, phenylalanine metabolism, tryptophan metabolism, beta-alanine metabolism, and alkaloid biosynthesis ii. (wikipedia.org)
  • The systematic name of this enzyme class is all-trans-13,14-dihydroretinol:acceptor 13,14-oxidoreductase. (wikipedia.org)
  • The systematic name of this enzyme class is 5-methyltetrahydrofolate:ferredoxin oxidoreductase . (primidi.com)
  • The systematic name of this enzyme class is dTDP-D-galactose:NADP+ 6-oxidoreductase. (creative-enzymes.com)
  • Other names in common use include D-2-hydroxy acid dehydrogenase, and (R)-2-hydroxy-acid:(acceptor) 2-oxidoreductase. (wikipedia.org)
  • With a nitrogenous group as acceptor. (expasy.org)
  • Other names in common use include primary alcohol dehydrogenase, MDH, quinohemoprotein alcohol dehydrogenase, quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase, and alcohol:(acceptor) oxidoreductase. (morebooks.de)
  • During the illumination of etiolated barley plants a rapid decline of the NADPH: protochlorophyllide oxidoreductase is observed. (nih.gov)
  • In contrast to previous concepts of chlorophyll biosynthesis in higher plants, our results present evidence that the NADPH: protochlorophyllide oxidoreductase functions only for a short time period after the onset of light. (nih.gov)
  • Other names in common use include NAD(P)H-dependent alkenal/one oxidoreductase , and NADPH:2-alkenal alpha,beta-hydrogenase . (wikipedia.org)
  • Genetic variations in POR, encoding NADPH-cytochrome P450 oxidoreductase (CYPOR), can diminish the function of numerous cytochromes P450, and also have the potential to block degradation of heme by heme oxygenase-1 (HO-1). (nih.gov)
  • Instead, our data implicate other pathways, particularly cell cycle, metabolism and neurotransmitter pathways, acting in combination to generate tissue-specific patterns of instability. (biomedcentral.com)
  • A flavoprotein oxidoreductase that has specificity for short-chain fatty acids. (umassmed.edu)
  • Antioxidative function and substrate specificity of NAD(P)H-dependent alkenal/one oxidoreductase. (wikipedia.org)
  • 5.2) is the member of quinoproteins group that use the redox cofactor pyrroloquinoline quinoine, calcium ions and glucose as substrate for its activity. (scielo.br)
  • Fluoxetine may be acting on several different molecular pathways to reduce anxiety-related behaviors in wild-derived zebrafish. (biomedcentral.com)
  • 3. The microorganism according to claim 2, wherein said efflux system is selected from the group consisting of monocarboxylate efflux systems, formate efflux systems, lactate efflux systems, malate efflux systems, succinate efflux systems, aromatic carboxylic acid efflux systems, functional variants thereof, and any combination thereof. (patents.com)
  • 5. The microorganism according claim 2, wherein said efflux system is selected from the group consisting of: monocarboxylate efflux systems of amino acid sequence SEQ ID NO:1, lactate efflux systems of amino acid sequence SEQ ID NO:23, lactate efflux systems of amino acid sequence SEQ ID NO:25, functional variants thereof having at least 80% sequence identity to said amino acid sequences, and any combination thereof. (patents.com)
  • 22 22 Enantioselectivity Origins Aromatic group prefers to rely in quadrant IV Stoltz B. M. et al. (slideplayer.com)
  • The purpose of this study is to determine whether or not there exists nonrandom grouping of cis-regulatory elements within gene promoters that can be perceived independent of gene expression data and whether or not there is any correlation between this grouping and the biological function of the gene. (biomedcentral.com)
  • Partitional clustering of the transcription factor binding site composition within these promoter segments reveals a small number of gene groups that are selectively enriched for gene ontology terms consistent with distinct aspects of cellular function. (biomedcentral.com)
  • Although several groups have reported butyrate production under oxygen-limited conditions by a native producer, Clostridium tyrobutylicum, and by a metabolically engineered Escherichia coli, efforts to produce butyrate under aerobic growth conditions have met limited success. (bireme.br)
  • This condition belongs to a group of disorders known as fatty acid oxidation disorders (FOD). (malacards.org)
  • Significance ranking of the class-determining transcription factor binding sites within these clusters show substantial overlap between the gene ontology terms of the transcriptions factors associated with the binding sites and the gene ontology terms of the regulated genes within each group. (biomedcentral.com)
  • The aim was to establish a possible relationship between these five candidate genes and clinical left ventricular hypertrophy (LVH) in a genetically homogenous group. (cdc.gov)
  • Stimulator of IFN genes (STING) are a group of transmembrane proteins that are involved in the induction of type I interferon that is important in the innate immune response. (meta.org)
  • clinical trial results comparing warfarin and direct-acting oral anticoagulant (DOAC) users experiencing major hemorrhage to clinical care is challenging due to differences seen among non-randomized oral anticoagulant users, bleed location, and etiology. (bioportfolio.com)
  • The brown algae (Phaeophyceae) are photosynthetic organisms, derived from a secondary endosymbiosis [ 1 ], that have evolved complex multicellularity independently of other major groups such as animals, green plants, fungi, and red algae. (biomedcentral.com)
  • Current guidelines recommend caution in prescribing concomitant use of direct-acting oral anticoagulants (DOACs) and antiepileptic drugs due to drug-drug interactions leading to potential risk of DOAC. (bioportfolio.com)
  • Direct oral anticoagulants (DOAC) are a new drug group that has been approved for chronic anticoagulation of patients in atrial fibrillation or suffering acute thrombosis, between others. (bioportfolio.com)
  • Equivalent inpatient mortality among direct-acting oral anticoagulant and warfarin users presenting with major hemorrhage. (bioportfolio.com)
  • The old descriptor ANIMALS will be changed to ANIMAL POPULATION GROUPS. (nih.gov)
  • Of the five candidate gene markers studied, no significant differences in the genotype distribution of the MTHFR, PON 1 and 2 or ACE markers were found between the LVH and non-LVH groups. (cdc.gov)
  • Enzymes that catalyse the removal of methyl groups from LYSINE or ARGININE residues found on HISTONES. (wakehealth.edu)
  • Rhodobacter sphaeroides mutants overexpressing chlorophyllide a oxidoreductase of Blastochloris viridis elucidate functions of enzymes in late bacteriochlorophyll biosynthetic pathways. (ebi.ac.uk)