NAD (+) and NADP (+) Dependent Alcohol OxidoreductasesAlcohol Oxidoreductases: 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).Alcohol Drinking: Behaviors associated with the ingesting of alcoholic beverages, including social drinking.Oxidoreductases: 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)Alcohols: Alkyl compounds containing a hydroxyl group. They are classified according to relation of the carbon atom: primary alcohols, R-CH2OH; secondary alcohols, R2-CHOH; tertiary alcohols, R3-COH. (From Grant & Hackh's Chemical Dictionary, 5th ed)Protein Disulfide Reductase (Glutathione): 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.Pyruvate Synthase: A ferredoxin-containing enzyme that catalyzes the COENZYME A-dependent oxidative decarboxylation of PYRUVATE to acetyl-COENZYME A and CARBON DIOXIDE.NADH, NADPH Oxidoreductases: 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.

The alcohol dehydrogenase polymorphism in populations of Drosophila melanogaster. I. Selection in different environments. (1/3212)

The allozyme polymorphism at the alcohol dehydrogenase locus in Drosophila melanogaster was studied in order to obtain experimental evidence about the maintenance of this polymorphism. Populations started with different initial allele frequencies from homozygous F and S lines showed a convergence of frequencies on regular food at 25 degrees, leading to values equal to those in the base populations. These results were interpreted as due to some kind of balancing selection. In populations kept at 29.8 degrees, a lower equilibrium F frequency was attained. Addition of ethanol and some other alcohols to the food gave a rapid increase in F frequency, and high humidity decreased the F frequency slightly. Combination or alternation of ethanol and high humidity had variable effects in the populations tested. For a further analysis of the allele-frequency changes, estimates were obtained for egg-to-adult survival under different conditions and for adult survival on ethanol-supplemented food. On ethanol food (both at regular and high humidity), egg-to-adult survival of SS homozygotes was considerably lower than that of the FF and FS genotypes. Under regular conditions of food, temperature and humidity, a tendency to heterozygote superiority was observed, while at high humidity a relative high survival of SS was noticed in some tests. Adult survival of SS was lower than that of FF, but FS was generally intermediate, though the degree of dominance differed between populations. The results are consistent with the hypothesis of the occurrence of selection at the Adh locus.  (+info)

Separation and properties of two acetylacetoin reductases from Bacillus cereus YUF-4. (2/3212)

The separation and purification of two kinds of acetylacetoin reductases (AACRs) from Bacillus cereus YUF-4 were examined. NADPH-linked AACR (AACR I) and NADH-linked AACR (AACR II) were separated from each other by ammonium sulfate fractionation, DEAE-cellulose chromatography, and hydroxyapatite chromatography. The former was purified 3.4-fold with a yield of 10.0%, and the latter was purified 29-fold with a yield of 15.6%. The two enzymes differ from each other in some enzymic properties such as substrate specificity.  (+info)

Metabolic engineering of poly(3-hydroxyalkanoates): from DNA to plastic. (3/3212)

Poly(3-hydroxyalkanoates) (PHAs) are a class of microbially produced polyesters that have potential applications as conventional plastics, specifically thermoplastic elastomers. A wealth of biological diversity in PHA formation exists, with at least 100 different PHA constituents and at least five different dedicated PHA biosynthetic pathways. This diversity, in combination with classical microbial physiology and modern molecular biology, has now opened up this area for genetic and metabolic engineering to develop optimal PHA-producing organisms. Commercial processes for PHA production were initially developed by W. R. Grace in the 1960s and later developed by Imperial Chemical Industries, Ltd., in the United Kingdom in the 1970s and 1980s. Since the early 1990s, Metabolix Inc. and Monsanto have been the driving forces behind the commercial exploitation of PHA polymers in the United States. The gram-negative bacterium Ralstonia eutropha, formerly known as Alcaligenes eutrophus, has generally been used as the production organism of choice, and intracellular accumulation of PHA of over 90% of the cell dry weight have been reported. The advent of molecular biological techniques and a developing environmental awareness initiated a renewed scientific interest in PHAs, and the biosynthetic machinery for PHA metabolism has been studied in great detail over the last two decades. Because the structure and monomeric composition of PHAs determine the applications for each type of polymer, a variety of polymers have been synthesized by cofeeding of various substrates or by metabolic engineering of the production organism. Classical microbiology and modern molecular bacterial physiology have been brought together to decipher the intricacies of PHA metabolism both for production purposes and for the unraveling of the natural role of PHAs. This review provides an overview of the different PHA biosynthetic systems and their genetic background, followed by a detailed summation of how this natural diversity is being used to develop commercially attractive, recombinant processes for the large-scale production of PHAs.  (+info)

MOT1 can activate basal transcription in vitro by regulating the distribution of TATA binding protein between promoter and nonpromoter sites. (4/3212)

MOT1 is an ATPase which can dissociate TATA binding protein (TBP)-DNA complexes in a reaction requiring ATP hydrolysis. Consistent with this observation, MOT1 can repress basal transcription in vitro. Paradoxically, however, some genes, such as HIS4, appear to require MOT1 as an activator of transcription in vivo. To further investigate the function of MOT1 in basal transcription, we performed in vitro transcription reactions using yeast nuclear extracts depleted of MOT1. Quantitation of MOT1 revealed that it is an abundant protein, with nuclear extracts from wild-type cells containing a molar excess of MOT1 over TBP. Surprisingly, MOT1 can weakly activate basal transcription in vitro. This activation by MOT1 is detectable with amounts of MOT1 that are approximately stoichiometric to TBP. With amounts of MOT1 similar to those present in wild-type nuclear extracts, MOT1 behaves as a weak repressor of basal transcription. These results suggest that MOT1 might activate transcription via an indirect mechanism in which limiting TBP can be liberated from nonpromoter sites for use at promoters. In support of this idea, excess nonpromoter DNA sequesters TBP and represses transcription, but this effect can be reversed by addition of MOT1. These results help to reconcile previous in vitro and in vivo results and expand the repertoire of transcriptional control strategies to include factor-assisted redistribution of TBP between promoter and nonpromoter sites.  (+info)

Characterization of the glucose 6-phosphate dehydrogenase activity in rat liver mitochondria. (5/3212)

Glucose 6-phosphate dehydrogenase activity in rat liver mitochondria can be released by detergent. The released activity is separated by chromatography into two peaks. One peak has the kinetic behaviour and mobility similar to the soluble sex-linked enzyme, whereas the other peak is similar to the microsomal hexose 6-phosphate dehydrogenase. There is no evidence for the existence of a new glucose 6-phosphate dehydrogenase activity in rat liver mitochondria.  (+info)

Identification of the reactive cysteine residue (Cys227) in human carbonyl reductase. (6/3212)

Carbonyl reductase is highly susceptible to inactivation by organomercurials suggesting the presence of a reactive cysteine residue in, or close to, the active site. This residue is also close to a site which binds glutathione. Structurally, carbonyl reductase belongs to the short-chain dehydrogenase/reductase family and contains five cysteine residues, none of which is conserved within the family. In order to identify the reactive residue and investigate its possible role in glutathione binding, alanine was substituted for each cysteine residue of human carbonyl reductase by site-directed mutagenesis. The mutant enzymes were expressed in Escherichia coli and purified to homogeneity. Four of the five mutants (C26A, C122A C150A and C226A) exhibited wild-type-like enzyme activity, although K(m) values of C226A for three structurally different substrates were increased threefold to 10-fold. The fifth mutant, C227A, showed a 10-15-fold decrease in kcat and a threefold to 40-fold increase in K(m), resulting in a 30-500-fold drop in kcat/K(m). NaCl (300 mM) increased the activity of C227A 16-fold, whereas the activity of the wild-type enzyme was only doubled. Substitution of serine rather than alanine for Cys227 similarly affected the kinetic constants with the exception that NaCl did not activate the enzyme. Both C227A and C227S mutants were insensitive to inactivation by 4-hydroxymercuribenzoate. Unlike the parent carbonyl compounds, the glutathione adducts of menadione and prostaglandin A1 were better substrates for the C227A and C227S mutants than the wild-type enzyme. Conversely, the binding of free glutathione to both mutants was reduced. Our findings indicate that Cys227 is the reactive residue and suggest that it is involved in the binding of both substrate and glutathione.  (+info)

Protection of mice against a lethal influenza virus challenge after immunization with yeast-derived secreted influenza virus hemagglutinin. (7/3212)

The A/Victoria/3/75 (H3N2-subtype) hemagglutinin (HA) gene was engineered for expression in Pichia pastoris as a soluble secreted molecule. The HA cDNA lacking the C-terminal transmembrane anchor-coding sequence was fused to the Saccharomyces cerevisiae alpha-mating factor secretion signal and placed under control of the methanol-inducible P. pastoris alcohol oxidase 1 (AOX1) promoter. Growth of transformants on methanol-containing medium resulted in the secretion of recombinant non-cleaved soluble hemagglutinin (HA0s). Remarkably, the pH of the induction medium had an important effect on the expression level, the highest level being obtained at pH 8.0. The gel filtration profile and the reactivity against a panel of different HA-conformation specific monoclonal antibodies indicated that HA0s was monomeric. Analysis of the N-linked glycans revealed a typical P. pastoris type of glycosylation, consisting of glycans with 10-12 glycosyl residues. Mice immunized with purified soluble hemagglutinin (HA0s) showed complete protection against a challenge with 10 LD50 of mouse-adapted homologous virus (X47), whereas all control mice succumbed. Heterologous challenge with X31 virus [A/Aichi/2/68 (H3N2-subtype)], resulted in significantly higher survival rates in the immunized group compared with the control group. These results, together with the safety, reliability and economic potential of P. pastoris, as well as the flexibility and fast adaptation of the expression system may allow development of an effective recombinant influenza vaccine.  (+info)

The choline-converting pathway in Staphylococcus xylosus C2A: genetic and physiological characterization. (8/3212)

A Staphylococcus xylosus C2A gene cluster, which encodes enzymes in the pathway for choline uptake and dehydrogenation (cud), to form the osmoprotectant glycine betaine, was identified. The cud locus comprises four genes, three of which encode proteins with significant similarities to those known to be involved in choline transport and conversion in other organisms. The physiological role of the gene products was confirmed by analysis of cud deletion mutants. The fourth gene possibly codes for a regulator protein. Part of the gene cluster was shown to be transcriptionally regulated by choline and elevated NaCl concentrations as inducers.  (+info)

*Alcohol oxidoreductase

Alcohol oxidoreductases are oxidoreductase enzymes that act upon an alcohol functional group. They are classified under "1.1" ... Alcohol oxidoreductases at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ...

*HSD17B4

It's an alcohol oxidoreductase, specifically 17β-Hydroxysteroid dehydrogenase. It is involved in fatty acid β-oxidation and ...

*Hydroxysteroid dehydrogenase

... s (HSDs) are a group of alcohol oxidoreductases that catalyze the dehydrogenation of ...

*Long-chain-alcohol dehydrogenase

NAD+ oxidoreductase. Other names in common use include long-chain alcohol dehydrogenase, and fatty alcohol oxidoreductase. This ... Lee T (1979). "Characterization of fatty alcohol:NAD+ oxidoreductase from rat liver". J. Biol. Chem. 254 (8): 2892-6. PMID ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, a long-chain-alcohol dehydrogenase (EC 1.1.1.192) is an enzyme that catalyzes the chemical reaction a long-chain ...

*Alcohol dehydrogenase (nicotinoprotein)

Van Ophem, P.W.; Van Beeumen, J.; Duine, J.A. (1993). "Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. ... Alcohol dehydrogenase (nicotinoprotein) (EC 1.1.99.36, NDMA-dependent alcohol dehydrogenase, nicotinoprotein alcohol ... Alcohol dehydrogenase (nicotinoprotein) at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ... Piersma, S.R.; Visser, A.J.; de Vries, S.; Duine, J.A. (1998). "Optical spectroscopy of nicotinoprotein alcohol dehydrogenase ...

*Methanol dehydrogenase (nicotinoprotein)

Van Ophem, P.W.; Van Beeumen, J.; Duine, J.A. (1993). "Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. ... N-dimethyl-4-nitrosoaniline oxidoreductase) is an enzyme with systematic name methanol:acceptor oxidoreductase. This enzyme ... dimethyl-4-nitrosoaniline oxidoreductase from Mycobacterium sp. strain JC1 (DSM 3803)". Microbiology. 156 (Pt 2): 463-471. doi: ... dimethyl-4-nitrosoaniline oxidoreductases from the gram-positive methylotrophic bacteria Amycolatopsis methanolica and ...

*17β-Hydroxysteroid dehydrogenase

... are a group of alcohol oxidoreductases which catalyze the reduction of 17-ketosteroids and the dehydrogenation of 17β- ... Oxidoreductase from the Rat Adrenal Gland]. Hoppe-Seyler's Zeitschrift für Physiologische Chemie (in German). 336: 63-8. doi: ...

*Alcohol oxidase

The systematic name of this enzyme class is alcohol:oxygen oxidoreductase. This enzyme is also called ethanol oxidase. It ... In enzymology, an alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the chemical reaction a primary alcohol + O2 ⇌ {\ ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as ... Suye S (1997). "Purification and properties of alcohol oxidase from Candida methanosorbosa M-2003". Curr. Microbiol. 34 (6): ...

*Coniferyl-alcohol dehydrogenase

The systematic name of this enzyme class is coniferyl-alcohol:NADP+ oxidoreductase. This enzyme is also called CAD. Mansell RL ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, a coniferyl-alcohol dehydrogenase (EC 1.1.1.194) is an enzyme that catalyzes the chemical reaction coniferyl ... the two substrates of this enzyme are coniferyl alcohol and NADP+, whereas its 3 products are coniferyl aldehyde, NADPH, and H+ ...

*Aryl-alcohol dehydrogenase (NADP+)

The systematic name of this enzyme class is aryl-alcohol:NADP+ oxidoreductase. Other names in common use include aryl alcohol ... 2. Purification and properties of aryl-alcohol: NADP-oxidoreductase from Neurospora crassa]". Eur. J. Biochem. (in German). 8 ( ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, an aryl-alcohol dehydrogenase (NADP+) (EC 1.1.1.91) is an enzyme that catalyzes the chemical reaction an ...

*Carbonyl reductase (NADPH)

The systematic name of this enzyme class is secondary-alcohol:NADP+ oxidoreductase. Other names in common use include aldehyde ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ...

*Allyl-alcohol dehydrogenase

The systematic name of this enzyme class is allyl-alcohol:NADP+ oxidoreductase. Otsuka K (1958). "Triphosphopyridine nucleotide ... In enzymology, an allyl-alcohol dehydrogenase (EC 1.1.1.54) is an enzyme that catalyzes the chemical reaction allyl alcohol + ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... NADP+ ⇌ {\displaystyle \rightleftharpoons } acrolein + NADPH + H+ Thus, the two substrates of this enzyme are allyl alcohol and ...

*Perillyl-alcohol dehydrogenase

The systematic name of this enzyme class is perillyl-alcohol:NAD+ oxidoreductase. This enzyme is also called perillyl alcohol ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, a perillyl-alcohol dehydrogenase (EC 1.1.1.144) is an enzyme that catalyzes the chemical reaction perillyl ... Ballal NR, Bhattacharyya PK, Rangachari PN (1966). "Perillyl alcohol dehydrogenase from a soil pseudomonad". Biochem. Biophys. ...

*Cinnamyl-alcohol dehydrogenase

The systematic name of this enzyme class is cinnamyl-alcohol:NADP+ oxidoreductase. Other names in common use include cinnamyl ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, a cinnamyl-alcohol dehydrogenase (EC 1.1.1.195) is an enzyme that catalyzes the chemical reaction cinnamyl ... Sarni F, Grand C, Boudet AM (1984). "Purification and properties of cinnamoyl-CoA reductase and cinnamyl alcohol dehydrogenase ...

*Vanillyl-alcohol oxidase

The systematic name of this enzyme class is vanillyl alcohol:oxygen oxidoreductase. This enzyme is also called 4-hydroxy-2- ... A novel aromatic alcohol oxidase containing covalently bound FAD". Eur. J. Biochem. 208 (3): 651-657. doi:10.1111/j.1432- ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as ... de Jong E, van Berkel WJ, van der Zwan RP, de Bont JA (1992). "Purification and characterization of vanillyl-alcohol oxidase ...

*Aryl-alcohol dehydrogenase

NAD+ oxidoreductase. Other names in common use include p-hydroxybenzyl alcohol dehydrogenase, benzyl alcohol dehydrogenase, and ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, an aryl-alcohol dehydrogenase (EC 1.1.1.90) is an enzyme that catalyzes the chemical reaction an aromatic ... The systematic name of this enzyme class is aryl-alcohol: ... the two substrates of this enzyme are aromatic alcohol and NAD+ ...

*Aryl-alcohol oxidase

... oxygen oxidoreductase. Other names in common use include aryl alcohol oxidase, veratryl alcohol oxidase, and arom. alcohol ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as ... In enzymology, an aryl-alcohol oxidase (EC 1.1.3.7) is an enzyme that catalyzes the chemical reaction an aromatic primary ... FARMER VC, HENDERSON ME, RUSSELL JD (1960). "Aromatic-alcohol-oxidase activity in the growth medium of Polystictus versicolor ...

*3-hydroxybenzyl-alcohol dehydrogenase

NADP+ oxidoreductase. Other names in common use include m-hydroxybenzyl alcohol dehydrogenase, m-hydroxybenzyl alcohol (NADP+) ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, a 3-hydroxybenzyl-alcohol dehydrogenase (EC 1.1.1.97) is an enzyme that catalyzes the chemical reaction 3- ... Forrester PI, Gaucher GM (1972). "m-Hydroxybenzyl alcohol dehydrogenase from Penicillium urticae". Biochemistry. 11 (6): 1108- ...

*8-Hydroxygeraniol dehydrogenase

... acyclic monoterpene primary alcohol:NADP+ oxidoreductase) is an enzyme with systematic name (6E)-8-hydroxygeraniol:NADP+ ... "Purification and characterization of an acyclic monoterpene primary alcohol:NADP+ oxidoreductase from catmint (Nepeta racemosa ... Ikeda, H.; Esaki, N.; Nakai, S.; Hashimoto, K.; Uesato, S.; Soda, K.; Fujita, T. (1991). "Acyclic monoterpene primary alcohol: ... 8-hydroxygeraniol dehydrogenase (EC 1.1.1.324, 8-hydroxygeraniol oxidoreductase, CYP76B10, G10H, CrG10H, SmG10H, ...

*Alcohol dehydrogenase (acceptor)

The systematic name of this enzyme class is alcohol:acceptor oxidoreductase. Other names in common use include primary alcohol ... quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase, and alcohol:(acceptor) oxidoreductase. This enzyme ... Alcohol dehydrogenase Ameyama M; Adachi O (1982). "Alcohol dehydrogenase from acetic acid bacteria, membrane-bound". Methods in ... In enzymology, an alcohol dehydrogenase (acceptor) (EC 1.1.99.8) is an enzyme that catalyzes the chemical reaction a primary ...

*Polyvinyl-alcohol dehydrogenase (acceptor)

... acceptor oxidoreductase. Other names in common use include PVA dehydrogenase, and polyvinyl-alcohol:(acceptor) oxidoreductase. ... oxidized polyvinyl alcohol + reduced acceptor Thus, the two substrates of this enzyme are polyvinyl alcohol and acceptor, ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ... In enzymology, a polyvinyl-alcohol dehydrogenase (acceptor) (EC 1.1.99.23) is an enzyme that catalyzes the chemical reaction ...

*Polyvinyl-alcohol oxidase

The systematic name of this enzyme class is polyvinyl-alcohol:oxygen oxidoreductase. Other names in common use include ... In enzymology, a polyvinyl-alcohol oxidase (EC 1.1.3.30) is an enzyme that catalyzes the chemical reaction polyvinyl alcohol + ... whereas its two products are oxidized polyvinyl alcohol and H2O2. This enzyme belongs to the family of oxidoreductases, ... Shimao M, Nishimura Y, Kato N, Sakazawa C (1985). "Localization of Polyvinyl Alcohol Oxidase Produced by a Bacterial Symbiont, ...

*Atromentin

In addition, there is another adjacent and conserved gene encoding for an alcohol dehydrogenase/oxidoreductase whose function ... and aminotransferase of 23 different atromentin-producing basidiomycetes that was in almost all cases absent from the alcohol ...

*Secondary-alcohol oxidase

... oxygen oxidoreductase. Other names in common use include polyvinyl alcohol oxidase, and secondary alcohol oxidase. Morita M, ... In enzymology, a secondary-alcohol oxidase (EC 1.1.3.18) is an enzyme that catalyzes the chemical reaction a secondary alcohol ... Sakai K, Hamada N, Watanabe Y (1983). "Separation of secondary alcohol oxidase and oxidized poly(vinyl alcohol) hydrolase by ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as ...

*Chlordecone reductase

The systematic name of this enzyme class is chlordecone-alcohol:NADP+ 2-oxidoreductase. This enzyme is also called CDR. As of ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... In enzymology, a chlordecone reductase (EC 1.1.1.225) is an enzyme that catalyzes the chemical reaction chlordecone alcohol + ... the two substrates of this enzyme are chlordecone alcohol and NADP+, whereas its 3 products are chlordecone, NADPH, and H+. ...

*Aflatoxin B1

Now an esterase, EstA, catalyzes the hydrolysis of the acetyl, forming the primary alcohol in versiconal. The acetal in ... an oxidoreductase. Then a final recyclization occurs to form aflatoxin B1. Aflatoxin B1 is a potent genotoxic hepatocarcinogen ... Averantin is converted to averufin via a two different enzymes, a hydroxylase and an alcohol dehydrogenase. This will oxygenate ...
HSD17B11; hydroxysteroid (17-beta) dehydrogenase 11; dehydrogenase/reductase (SDR family) member 8 , DHRS8; estradiol 17-beta-dehydrogenase 11; 17 BETA HSD11; 17 BETA HSDXI; PAN1B; retinal short chain dehydrogenase/reductase 2; RetSDR2; SDR16C2; short cha; short chain dehydrogenase/reductase family 16C; member 2; 17-BETA-HSD11; 17-BETA-HSDXI; 17-beta-HSD 11; 17-beta-HSD XI; CTCL tumor antigen HD-CL-03; CTCL-associated antigen HD-CL-03; 17-beta-hydroxysteroid dehydrogenase 11; 17-beta-hydroxysteroid dehydrogenase XI; T-cell lymphoma-associated antigen HD-CL-03; dehydrogenase/reductase SDR family member 8; 17-beta-hydroxysteroid dehydrogenase type XI; dehydrogenase/reductase (SDR family) member 8; retinal short-chain dehydrogenase/reductase 2; cutaneous T-cell lymphoma-associated antigen HD-CL-03; short chain dehydrogenase/reductase family 16C, member 2; DHRS8; 17BHSD11 ...
1. Lee Y, Jeon K, Lee JT, Kim S, Kim VN. MicroRNA maturation: stepwise processing and subcellular localization. Embo J. 2002;21(17):4663-4670 2. Chen K, Rajewsky N. The evolution of gene regulation by transcription factors and microRNAs. Nat Rev Genet. 2007;8(2):93-103 3. Pillai RS, Bhattacharyya SN, Filipowicz W. Repression of protein synthesis by miRNAs: how many mechanisms?. Trends Cell Biol. 2007;17(3):118-126 4. Walker GJ, Indsto JO, Sood R. et al. Deletion mapping suggests that the 1p22 melanoma susceptibility gene is a tumor suppressor localized to a 9-Mb interval. Genes Chromosomes Cancer. 2004;41(1):56-64 5. Bemis LT, Chen R, Amato CM. et al. MicroRNA-137 targets microphthalmia-associated transcription factor in melanoma cell lines. Cancer Res. 2008;68(5):1362-1368 6. Chinnadurai G. The transcriptional corepressor CtBP: a foe of multiple tumor suppressors. Cancer Res. 2009;69(3):731-734 7. Haflidadottir BS, Bergsteinsdottir K, Praetorius C, Steingrimsson E. miR-148 regulates Mitf in ...
Androgen-regulated short-chain dehydrogenase/reductase 1, ARSDR1CGI82, EC 1.1.1.300, HCBP12, HCV core-binding protein HCBP12, MDT1, prostate short-chain dehydrogenase reductase 1, Prostate short-chain dehydrogenase/reductase 1, PSDR1FLJ32633, RALR1, RalR1, Retinal reductase 1, retinol dehydrogenase 11, retinol dehydrogenase 11 (all-trans and 9-cis), retinol dehydrogenase 11 (all-trans/9-cis/11-cis), SCALD, SDR7C1, short chain dehydrogenase/reductase family 7C, member ...
EC 1.1.1, EC 1.1.1.-, FLJ16333, MGC126600, Orphan short-chain dehydrogenase/reductase, RDH-S, RDHSMGC126602, SDR-Oorphan short-chain dehydrogenase / reductase, SDROretinol dehydrogenase similar protein, short-chain dehydrogenase/reductase family 9C member 7, short chain dehydrogenase/reductase family 9C, member ...
Estradiol 17-beta-dehydrogenase 11,1.1.1.62,17-beta-hydroxysteroid dehydrogenase 11,17-beta-HSD 11,17bHSD11,17betaHSD11,17-beta-hydroxysteroid dehydrogenase XI,17-beta-HSD XI,17betaHSDXI,Cutaneous T-cell lymphoma-associated antigen HD-CL-03,CTCL-associated antigen HD-CL-03,Dehydrogenase/reductase SDR family member 8,Retinal short-chain dehydrogenase/reductase 2,retSDR2,Short chain dehydrogenase/reductase family 16C member 2,HSD17B11,DHRS8,PAN1B,SDR16C2,PSEC0029,UNQ207/PRO233,. ...
Corepressor targeting diverse transcription regulators such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation.
BACKGROUND: (R)-[3,5-bis(trifluoromethyl)phenyl] ethanol [(R)-3,5-BTPE] is a valuable chiral intermediate for Aprepitant (Emend) and Fosaprepitant (Ivemend). Biocatalyzed asymmetric reduction is a preferred approach to synthesize highly optically active (R)-3,5-BTPE. However, the product concentration and productivity of reported (R)-3,5-BTPE synthetic processes remain unsatisfied. RESULTS: A NADPH-dependent carbonyl reductase from Lactobacillus kefir (LkCR) was discovered by genome mining for reduction of 3,5-bis(trifluoromethyl) acetophenone (3,5-BTAP) into (R)-3,5-BTPE with excellent enantioselectivity. In order to synthesize (R)-3,5-BTPE efficiently, LkCR was coexpressed with glucose dehydrogenase from Bacillus subtilis (BsGDH) for NADPH regeneration in Escherichia coli BL21 (DE3) cells, and the optimal recombinant strain produced 250.3 g/L (R)-3,5-BTPE with 99.9% ee but an unsatisfied productivity of 5.21 g/(L h). Then, four different linker peptides were used for the fusion expression of ...
The major metabolic pathways involved in synthesis and disposition of carbonyl and hydroxyl group containing compounds are presented, and structural and functional characteristics of the enzyme families involved are discussed. Alcohol and aldehyde dehydrogenases (ADH, ALDH) participate in oxidative pathways, whereas reductive routes are accomplished by members of the aldo-keto reductase (AKR), short-chain dehydrogenases/reductases (SDR) and quinone reductase (QR) superfamilies. A wealth of biochemical, genetic and structural data now establishes these families to constitute important phase I enzymes.
Complete information for SDR42E1 gene (Protein Coding), Short Chain Dehydrogenase/Reductase Family 42E, Member 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Dehydrogenase/reductase (SDR family) member 7 (DHRS7, retSDR4, SDR34C1) is a previously uncharacterized member of the short-chain dehydrogenase/reductase (SDR) superfamily. While human SDR members are known to play an important role in various (patho)biochemical pathways including intermediary metabolism and biotransformation of xenobiotics, only 20% of them are considered to be well characterized. Based on phylogenetic tree and SDR sequence clusters analysis DHRS7 is a close relative to well-known SDR member 11β-hydroxysteroid dehydrogenase 1 (11β-HSD1) that participates in metabolism of endogenous and xenobiotic substances with carbonyl group. The aim of present study is to determine the basic biochemical properties of DHRS7 and its possible involvement in metabolism of substrates with carbonyl group. For the first time the computational predictions of this membrane protein and membrane topology were experimentally confirmed. DHRS7 has been demonstrated to be an integral protein facing the lumen of
Accepted name: L-threonine 3-dehydrogenase. Reaction: L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+. Other name(s): L-threonine dehydrogenase; threonine 3-dehydrogenase; threonine dehydrogenase, THD. Systematic name: L-threonine:NAD+ oxidoreductase. Comments: This enzyme acts in concert with EC 2.3.1.29, glycine C-acetyltransferase, in the degradation of threonine to glycine. This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex [2]. In aqueous solution, the product L-2-amino-3-oxobutanoate can spontaneously decarboxylate to form aminoacetone.. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9067-99-6. References:. 1. Green, M.L. and Elliott, W.H. The enzymic formation of aminoacetone from threonine and its further metabolism. Biochem. J. 92 (1964) 537-549. [PMID: 4284408]. 2. Hartshorne, D. and Greenberg, D.M. Studies on liver threonine dehydrogenase. Arch. Biochem. Biophys. 105 ...
retinol dehydrogenase 8 (all trans) Proteins available through Novus Biologicals. Browse our retinol dehydrogenase 8 (all trans) Protein catalog backed by our Guarantee+.
retinol dehydrogenase 8 (all trans) Proteins available through Novus Biologicals. Browse our retinol dehydrogenase 8 (all trans) Protein catalog backed by our Guarantee+.
592 Drug resistance caused by overexpression of P-glycoprotein (P-gp), the MDR1 gene product, limits the therapeutic outcome in cancer patients. Although modulation of multidrug resistance (MDR) by pharmacological agents, antibodies, antisense oligonucleotides, siRNA, and inhibitors of signal transduction have been reported, clinical benefits have been disappointing. We and others have sought to understand the regulation of MDR1 gene expression as another approach to this problem. CtBP1 (C-terminal-binding protein 1) is a transcriptional co-regulator that plays an important role in oncogenesis. Recently, it was reported that CtBP1 could serve as both a co-activator and co-repressor of transcription. In this study, we determined the effect of CtBP1 on transcription of the MDR1 gene. Chromatin immunoprecipitation (ChIP) experiments demonstrated that CtBP1 bound to the promoter and coding regions of the MDR1 gene, but not to the non-coding regions. Knockdown of CtBP1 expression by siRNA repressed ...
Alcohol Oxidase, 10 mg. Alcohol Oxidase (AOX) is a homooctameric flavoprotein consisting of eight identical subunits of ~74 kD, each containing a flavin adenine dinucleotide molecule (FAD) as a prosthetic group (van der Klei et al.
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Shop Dehydrogenase/reductase SDR family protein ELISA Kit, Recombinant Protein and Dehydrogenase/reductase SDR family protein Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
HSD17B10, hydroxysteroid (17-beta) dehydrogenase 10, is a member of the short-chain dehydrogenase/reductase superfamily. HSD17B10 functions in mitochondrial tRNA maturation and catalyzes the oxidation of a wide variety of fatty acids, alcohols, and steroids. The protein is thought to play a role in the development of Alzheimer's disease. There are several alternatively spliced transcript variants, of which only two have been fully sequenced.
But experimentalists should not get too cocky: the next paper, by Jamie Simpson and collaborators at Monash University, describes some of the things that can go wrong. An STD NMR screen of the antimicrobial target ketopantoate reductase (KPR) using the same Maybridge library of 500 compounds revealed 196 hits! The 47 with the strongest STD signals were then tested in a 1H/15N-HSQC NMR assay, leading to 14 hits, of which 4 gave measurable IC50 values in an enzymatic assay. Unfortunately, follow-up SAR was disappointing, and subsequent experiments revealed that aggregation was to blame: when the biochemical experiments were rerun in the presence of 0.01% Tween-20, only a single fragment gave a measurable IC50 value. The researchers redid their STD-NMR screen in the presence of detergent, resulting in 71 hits, all of which were tested in the biochemical screen. This led to the identification of a new (and fairly potent) hit that had previously been missed. This nicely illustrates the fact that ...
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Complete information for RDH16 gene (Protein Coding), Retinol Dehydrogenase 16 (All-Trans), including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
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RDH5兔多克隆抗体(ab101457)可与人样本反应并经WB, IHC实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
Définitions de 1 3 propanediol dehydrogenase, synonymes, antonymes, dérivés de 1 3 propanediol dehydrogenase, dictionnaire analogique de 1 3 propanediol dehydrogenase (anglais)
cinnamyl alcohol dehydrogenase: NADP-dependent enzyme that catalyzes the reversible conversion of p-hydroxycinnamaldehydes to their corresponding alcohols, leading to the biosynthesis of lignin in plants
This gene encodes a mitochondrial 3-hydroxyisobutyrate dehydrogenase enzyme. The encoded protein plays a critical role in the catabolism of L-valine by catalyzing the oxidation of 3-hydroxyisobutyrate to methylmalonate semialdehyde. [provided by RefSeq, Nov 2011 ...
Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate.
Nicotiana tabacum cDNA encoding a bifunctional protein having catalytic domains for dehydroquinase and shikimate dehydrogenase was cloned and sequenced. Complementation of Escherichia coli aroD and aroE auxotrophs was successful. Amino acid sequencing located the N-terminus of the mature protein. The two catalytic domains exhibited greater amino acid identity with prokaryote homologues than with yeast and fungal homologues. ...
Carbonyl reduction constitutes a phase I reaction for many xenobiotics and is carried out in mammals mainly by members of two protein families, namely aldo-keto reductases and short-chain dehydrogenases/reductases. In addition to their capacity to reduce xenobiotics, several of the enzymes act on endogenous compounds such as steroids or eicosanoids. One of the major carbonyl reducing enzymes found in humans is carbonyl reductase 1 (CBR1) with a very broad substrate spectrum. A paralog, carbonyl reductase 3 (CBR3) has about 70% sequence identity and has not been sufficiently characterized to date. Screening of a focused xenobiotic compound library revealed that CBR3 has narrower substrate specificity and acts on several orthoquinones, as well as isatin or the anticancer drug oracin. To further investigate structure-activity relationships between these enzymes we crystallized CBR3, performed substrate docking, site-directed mutagenesis and compared its kinetic features to CBR1. Despite high sequence
Pseudomonas aeruginosa ExaE protein: a response regulator of a two-component regulatory system for controling expression quinoprotein ethanol dehydrogenase; isolated from Pseudomonas aeruginosa; amino acid sequence in first source
Accepted name: alcohol dehydrogenase (nicotinoprotein). Reaction: ethanol + acceptor - acetaldehyde + reduced acceptor. Other name(s): nicotinoprotein alcohol dehydrogenase; np-ADH; NDMA-dependent alcohol dehydrogenase; ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase. Systematic name: ethanol:acceptor oxidoreductase. Comments: Contains Zn2+. Nicotinoprotein alcohol dehydrogenases are unique medium-chain dehydrogenases/reductases (MDR) alcohol dehydrogenases that have a tightly bound NAD+/NADH cofactor that does not dissociate during the catalytic process. Instead, the cofactor is regenerated by a second substrate or electron carrier. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, can serve this function in vitro. The enzyme from the Gram-positive bacterium Amycolatopsis methanolica can accept many primary alcohols as substrates, including benzylalcohol [1].. Links to other databases: BRENDA, ...
Accepted name: coniferyl-alcohol dehydrogenase. Reaction: coniferyl alcohol + NADP+ = coniferyl aldehyde + NADPH + H+. Other name(s): CAD. Systematic name: coniferyl-alcohol:NADP+ oxidoreductase. Comments: Specific for coniferyl alcohol; does not act on cinnamyl alcohol, 4-coumaryl alcohol or sinapyl alcohol.. Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 37250-27-4. References:. 1. Mansell, R.L., Babbel, G.R. and Zenk, M.H. Multiple forms and specificity of coniferyl alcohol dehydrogenase from cambial regions of higher plants. Phytochemistry 15 (1976) 1849-1853.. 2. Wyrambik, D. and Grisebach, H. Purification and properties of isoenzymes of cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures. Eur. J. Biochem. 59 (1975) 9-15. [PMID: 1250]. ...
1MGO: Mobility of Fluorobenzyl Alcohols Bound to Liver Alcohol Dehydrogenases as Determined by NMR and X-ray Crystallographic Studies
Similar to Dehydrogenase/reductase SDR family member 4 (EC 1.1.1.184) (NADPH- dependent carbonyl reductase/NADP-retinol dehydrogenase) (CR) (PHCR) (Peroxisomal short-chain alcohol dehydrogenase) (NADPH-dependent retinol dehydrogenase/reductase) (NDRD) (SCAD-SRL) (humNRDR) (PSCD). Splice isoform 2 ...
RDH10 is a specific all-trans retinol dehydrogenase identified in the RPE and now in the Müller cells. 14 We propose that one of the possible physiological functions of RDH10 is to synthesize the all-trans retinal chromophore for RGR and thus to act as a functional partner of RGR in the photic visual cycle. As RGR is known to be expressed in both the RPE and Müller cells, it was necessary to determine whether RDH10 co-expresses with RGR in both the RPE and Müller cells. Western blot analysis demonstrated that RDH10 is expressed at a high level in the RPE and a lower level in the retina (Fig. 2) . The anti-RDH10 antibody stained a cell type in the inner retina. The morphology of the stained cells and their location in the retina are consistent with those of Müller cells. 16 To further confirm the observation, we used rMC-1 cells, a well-established and characterized retinal Müller cell line. 19 RDH10 expression in this cell line was detected at both the mRNA and protein levels (Fig. 4) ...
Reitman and colleagues had a hunch that the genetic mutation seen in cancer might trigger a similar functional change to a closely related enzyme found in yeast and bacteria (homoisocitrate dehydrogenase), which would create the elusive 2-hydroxyadipate dehydrogenase necessary for "green" adipic acid production.. They were right. The functional mutation observed in cancer could be constructively applied to other closely related enzymes, creating a beneficial outcome - in this case the missing link that could enable adipic acid production from cheap sugars. The next step will be to scale up the overall adipic acid production process, which remains a considerable undertaking.. "Its exciting that sequencing cancer genomes can help us to discover new enzyme activities," Reitman said. "Even genetic changes that occur in only a few patients could reveal useful new enzyme functions that were not obvious before.". Yan, a professor in the Department of Pathology and senior author of the study, said the ...
GT:ID BAD57618.1 GT:GENE BAD57618.1 GT:PRODUCT putative short chain dehydrogenase GT:DATABASE GIB00210CH01 GT:ORG nfar0 GB:ACCESSION GIB00210CH01 GB:LOCATION 2940013..2940783 GB:FROM 2940013 GB:TO 2940783 GB:DIRECTION + GB:PRODUCT putative short chain dehydrogenase GB:PROTEIN_ID BAD57618.1 LENGTH 256 SQ:AASEQ MDKDSFRKLFDLSGRTAIVTGGTRGIGLAIAEGFACAGANLVVASRKPEACEQAAARLRELGAQAVGVPTHLGEIDSLRALVDTAVSAFGGIDIVVNNAANALAQPLATMAPEAVDKSFGVNVQGPLFLVQAALPHLRASAHAAVLNLGSVAALQFAPGLSMYAAGKAALLSFTRAMAAEFAADGIRVNAMAPGAVNTDMVRKNPPEFIAAMAQAPLLRRIAEPDEMVGAALLLCSDAGSFITGQTFLVDGGTVAR GT:EXON 1,1-256:0, BL:SWS:NREP 1 BL:SWS:REP 12-,256,DHRS4_RABIT,4e-36,36.8,242/260, PROS 150-,178,PS00061,ADH_SHORT,PDOC00060, SEG 97-,102,nnaana, BL:PDB:NREP 1 BL:PDB:REP 9-,255,1vl8B,1e-34,34.4,247/252, RP:PDB:NREP 1 RP:PDB:REP 10-,256,2ae1A,8e-44,30.6,245/252, RP:PFM:NREP 1 RP:PFM:REP 15-,180,PF00106,2e-21,42.2,166/169,adh_short, HM:PFM:NREP 1 HM:PFM:REP 16-,181,PF00106,2.2e-34,30.9,162/167,adh_short, GO:PFM:NREP 2 GO:PFM ...
GT:ID BAD55466.1 GT:GENE BAD55466.1 GT:PRODUCT putative short chain dehydrogenase GT:DATABASE GIB00210CH01 GT:ORG nfar0 GB:ACCESSION GIB00210CH01 GB:LOCATION 643418..644293 GB:FROM 643418 GB:TO 644293 GB:DIRECTION + GB:PRODUCT putative short chain dehydrogenase GB:PROTEIN_ID BAD55466.1 LENGTH 291 SQ:AASEQ MSRWDTANIPDQSGRTFIVTGANSGLGAVAARALARAGADVVLACRNLTKAEKVAAEIGARATVRELDLADLASVRAFAAGTERVDVLINNAGVMAVPHRTTADGFEMQIGTNHLGHFALTGLLLDKITDRVVTVSSGAHAVGRIDLADLNWERRRYQRWLAYGQSKLANLLFAYELQRRLGAAGSPILSVAAHPGYAATELQSHTETFLDSVMNVGNRILAQTAEMGALPELFAATMPVEPGAFYGPTGLGGMRGYPGRCGSTKASRDERVAGELWALSERLTGVTYSFD GT:EXON 1,1-291:0, BL:SWS:NREP 1 BL:SWS:REP 7-,286,RDH13_MOUSE,2e-38,40.5,269/334, SEG 25-,44,glgavaaralaragadvvla, BL:PDB:NREP 1 BL:PDB:REP 14-,205,2japC,4e-08,39.4,180/246, RP:PDB:NREP 2 RP:PDB:REP 13-,91,2ag5C,1e-05,23.4,77/244, RP:PDB:REP 68-,205,3ce6B,5e-13,8.1,136/485, RP:PFM:NREP 1 RP:PFM:REP 46-,143,PF00106,3e-05,38.8,98/169,adh_short, HM:PFM:NREP 1 HM:PFM:REP ...
Contains NADP+ as a cofactor. This is the first enzyme in the biosynthetic pathway of pseudaminic acid [3], a sialic-acid-like sugar that is unique to bacteria and is used by Helicobacter pylori to modify its flagellin. This enzyme plays a critical role in H. pyloris pathogenesis, being involved in the synthesis of both functional flagella and lipopolysaccharides [1,2]. It is completely inhibited by UDP-alpha-D-galactose. The reaction results in the chirality of the C-5 atom being inverted. It is thought that Lys-133 acts sequentially as a catalytic acid, protonating the C-6 hydroxy group and as a catalytic base, abstracting the C-5 proton, resulting in the elimination of water. This enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes ...
At concentrations of 2mM and above hydroxypyruvate produced no glucose with isolated rat liver cells, although it was rapidly utilized. At a lower concentration of hydroxypyruvate or in the presence of substrates which generate reducing equivalents (ethanol or butyrate), appreciable amounts of glucose were formed from hydroxypyruvate. A possible explanation for this phenomenon is discussed.. ...
Sequence variation of alcohol dehydrogenase (Adh) paralogs in cactophilic Drosophila.: This study focuses on the population genetics of alcohol dehydrogenase (A
ADH4, class II alcohol dehydrogenase 4 pi subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a…
putative quinate/shikimate dehydrogenase [putative shikimate 5-dehydrogenase] ATGGTCAAGGACTCGTATCTCGTCGGGCTGATCGGCGCCGGGATCGGCCCGTCGCTCAGC CCGGCACTGCACGAGCGGGAGGCCGACCGGCAGGGCCTGCGCTATCTGTACCGGCTGATC GACATCGACGCGCTCGGTGTCGGGCCGCAGGCGGTGGGGGACCTCGTACGAGCCGCCCGC GACCTGGGCTTCGACGGGCTGAACATCACGCATCCCTGCAAGCAGCTCGTCATCGGGCAT CTGGACGCGCTCGCCCCGCAGGCCGAGGCGCTCGGCGCGGTGAACACCGTCGTCTTCGAG GGCGGGCGTGCGGTCGGGCACAACACCGATGTCACCGGGTTCGCCGCCTCGTTCGCCCGT GGGCTGCCGGATGCCCCGCTGGAGCGGGTCGTGCAGTTGGGCGCGGGGGGAGCGGGGGCG GCCGTCGCGCATGCCATGCTCACGCTCGGGGCCGGGCACGTCACCGTCGTCGATGCCATG CCGGACCGGTCGGCGGACCTCGCCGCCTCGCTGAACCGGCACTTCGGTGCGGGGCGGGCC GCTGCCGCGGGCCCGGAGCGGCTGGCGGCGCTGCTCGGCGGTGCGGACGGCATCGTGCAT GCCACGCCGACGGGGATGGCCGCTCATCCGGGGCTGCCGCTTCCCGGTGAGTTGCTGCAT CCCGGGTTGTGGGTGGCCGAGGTGGTGTACCGGCCGTTGGAGACCGAGTTGCTGCGTGCC GCTCGGGCGGCGGGGTGTGCGGTTCTCGATGGTGGGGGGATGGCTGTTTTCCAGGCCGCG GACGCGTTTCGGCTGTTCACGGGGCGGGAGCCGGACGCGGTGCGGATGCTTGCGGATATT ...
Compare Alcohol Dehydrogenase ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, and more.
NADP_Rossmann (CL0063) 2-Hacid_dh_C; D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain (PF02826; HMM-score: 180.6) ...
NADP_Rossmann (CL0063) 2-Hacid_dh_C; D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain (PF02826; HMM-score: 173.2) ...
HAO1 antibody, Internal (hydroxyacid oxidase (glycolate oxidase) 1) for WB. Anti-HAO1 pAb (GTX81144) is tested in Human, Mouse samples. 100% Ab-Assurance.
Enzyme-reduced coenzyme binary complexes produce previously unreported shifts in the spectrum of the free coenzyme. These shifts give rise to difference spectra which resemble a general environmental change for reduced diphosphopyridine nucleotide (DPNH) in the glutamic dehydrogenase-DPNH complex, and indicate a more specific enzyme-coenzyme interaction for yeast alcohol dehydrogenase-DPNH, isocitrate dehydrogenase-TPNH, and lactic dehydrogenase-DPNH complexes. ...
tr:A0A0F6BSE2_GEOS0] Alcohol dehydrogenase GroES domain protein; K13953 alcohol dehydrogenase, propanol-preferring [EC:1.1.1.1] ...
vei:Veis_1678 K00111 glycerol-3-phosphate dehydrogenase [EC:1.1.5.3] , (GenBank) FAD dependent oxidoreductase (A) MSEPAFDVAVIGAGVVGCAVARRFVLGGARVLLLEKGADLLSGASKANSAILHTGFDAPG GSLELACMQRGYAEYMQIAQALNLPVLETGALVAAWSDQEFERLAQLHAQASDNGVHDVQ RLDRAEMLAREPHIAPSVRGGLLVPGEHVIDPWSAPLAYLRQAVENGGRAVFDAPLLAGR RVGAQWRLHSARGHFRARCVVNCAGLWGDRVEAMLLGQASFQIKPRKGQFVVFDKSASAL LRSILLPVPGEHSKGIVLTRTVFGNLLVGPTAEEQEDRSRATVERAALQRLIDKAGQLLP ALRTMPVTAVYAGLRPASEKKEYRLHLQADAGYFAVGGIRSTGLTAALGLAAHVFDRLRP CLPDLAPPDRVLCSPVPNLAEHRERDWEKPGDNDIVCHCERVTRREIEAALTGPVPALDL GGLKRRTRVCMGRCQGFHCAARVAELSAGHFHAPLALATLDRHG ...
DHRS2 antibody (dehydrogenase/reductase (SDR family) member 2) for ICC/IF, IHC-P, WB. Anti-DHRS2 pAb (GTX33152) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance.
HSD17B2; hydroxysteroid (17-beta) dehydrogenase 2; estradiol 17-beta-dehydrogenase 2; HSD17; SDR9C2; short chain dehydrogenase/reductase family 9C; member 2; 17 beta HSD 2; 20 alpha HSD; 20 alpha hydroxysteroid dehydrogenase; E2DH; Microsomal 17 beta hydroxysteroid dehydrogenase; Testosterone 17 beta dehydrogenase; 20-alpha-HSD; 17-beta-HSD 2; OTTHUMP00000174979; testosterone 17-beta-dehydrogenase; 20 alpha-hydroxysteroid dehydrogenase; 17-beta-hydroxysteroid dehydrogenase type 2; microsomal 17-beta-hydroxysteroid dehydrogenase; short chain dehydrogenase/reductase family 9C, member 2; EDH17B2 ...
The Report Corticosteroid 11 Beta Dehydrogenase Isozyme 1 (11 Beta Hydroxysteroid Dehydrogenase 1 or Short Chain Dehydrogenase/Reductase Family 26C Member 1 or HSD11B1 or EC 1.1.1.146) - Pipeline Review, H2 2017 provides information on pricing, market analysis, shares, forecast, and company profiles for key industry participants. - MarketResearchReports.biz". Corticosteroid 11 Beta Dehydrogenase Isozyme 1 (11 Beta Hydroxysteroid Dehydrogenase 1 or Short Chain Dehydrogenase/Reductase Family 26C Member 1 or HSD11B1 or EC 1.1.1.146) - 11beta-hydroxysteroid dehydrogenase type 1 is an NADPH-dependent enzyme highly expressed in key metabolic tissues including liver, adipose tissue, and the central nervous system. In these tissues HSD11B1 reduces cortisone to the active hormone cortisol that activates glucocorticoid receptors. This enzyme plays an important role in obesity and insulin resistance.. Corticosteroid 11 Beta Dehydrogenase Isozyme 1 (11 Beta Hydroxysteroid Dehydrogenase 1 or Short Chain ...
SPR Deficiency is caused by mutations in the SPR gene. The SPR gene provides instructions for making the enzyme sepiapterin reductase. Specifically, sepiapterin reductase is responsible for the last step in the production of tetrahydrobiopterin. Most SPR gene mutations result in an enzyme with little or no function.. A nonfunctional sepiapterin reductase gene leads to a lack of tetrahydrobiopterin which causes a disruption in neurotransmitter metabolism. SPR Deficiency is due to an autosomal recessive inheritance. In this type of inheritance pattern there are two mutated copies of the gene that causes the disorder. A person with SPR deficiency usually has unaffected parents (no symptoms) who each carry a single copy of the mutated gene and are referred to as carriers.. Autosomal recessive disorders are typically not seen in every generation of an affected family. When two people who are carriers of an autosomal recessive condition have a child, there is a 25% (1 in 4) chance that the child will ...
N-Hydroxy-N-isopropyloxamate (IpOHA) is known to inhibit extremely tightly (Ki of 22 pM) the bacterial acetohydroxy acid isomeroreductase (EC 1.1.1.86) [Aulabaugh and Schloss (1990) Biochemistry 29, 2824-2830], the second enzyme of the branched-chain
This report describes the microinjection of a purified peroxisomal protein, alcohol oxidase, from Pichia pastoris into mammalian tissue culture cells and the subsequent transport of this protein into vesicular structures. Transport was into membrane-enclosed vesicles as judged by digitonin-permeabilization experiments. The transport was time and temperature dependent. Vesicles containing alcohol oxidase could be detected as long as 6 d after injection. Coinjection of synthetic peptides containing a consensus carboxyterminal tripeptide peroxisomal targeting signal resulted in abolition of alcohol oxidase transport into vesicles in all cell lines examined. Double-label experiments indicated that, although some of the alcohol oxidase was transported into vesicles that contained other peroxisomal proteins, the bulk of the alcohol oxidase did not appear to be transported to preexisting peroxisomes. While the inhibition of transport of alcohol oxidase by peptides containing the peroxisomal targeting ...
Compare aldo-keto reductase family 1, member D1 (delta 4-3-ketosteroid-5-beta-reductase) ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, and more.
A number of Gram-negative bacteria utilize a class of dehydrogenases known as quinoproteins, which are distinct from the flavin- and nicotinamide-dependent enzymes, to catalyze the oxidation of alcohols or aldoses. The reaction is the first step in an electron transport chain that generates a proton motive force that is used to produce ATP. Several quinoproteins contain the noncovalently bound quinoid cofactor pyrroloquinoline quinone (PQQ), the role of which as a potential vitamin in mammals is currently under debate. The first of these papers describes the characterisation of the PQQ radical in Quinoprotein Ethanol Dehydrogenase, by advanced EPR & density functional theory. Although the structure of these proteins has been elucidated by X-ray crystallography until now the location of the alcohol substate could not be determined. In the second of these papers we established the position of the substrate in the binding pocket using the same experimental and theoretical methods.. ...
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Previous studies have observed that carboxyl-terminal binding protein 1 (CtBP1) is highly expressed in several malignant tumors, such as breast, glioma and prostate tumors, and it was found to play a role in cancer development (5,6,9,10). However, the expression pattern and biological functions of CtBP1 in lung adenocarcinoma remain largely unknown. The present study aimed to address this by examining the expression patterns of CtBP1 in lung adenocarcinoma tissues, its correlation to clinicopathological features, and its effects on the malignant behavior of lung cancer cells. As such, it represents the first investigation of the clinical significance of CtBP1 expression in lung adenocarcinoma patients. Using IHC, we found that CtBP1 was upregulated in lung adenocarcinoma patients with lymph node metastasis. Moreover, CtBP1 expression was strongly associated with tumor differentiation, size and with poor overall survival of lung adenocarcinoma patients. These data suggest that CtBP1 may act as an ...
Fatty acid synthase (FAS) is a multifunctional protein, whose primary role is the NADPH-mediated synthesis of palmitate from acetyl-CoA and malonyl-CoA, into long-chain saturated fatty acids. The protein consists of two identical, multifunctional 272 kDa polypeptides. FAS is expressed at high levels in liver, brain, breast, and lung. Studies have reported the in-frame fusion of FAS with estrogen receptor alpha in some cancer cell lines, and FAS expression is upregulated in breast cancer. FAS is also known as OA-519, SDR27X1, and short chain dehydrogenase/reductase family 27X, member 1.. ...
Fatty acid synthase (FAS) is a multifunctional protein, whose primary role is the NADPH-mediated synthesis of palmitate from acetyl-CoA and malonyl-CoA, into long-chain saturated fatty acids. The protein consists of two identical, multifunctional 272 kDa polypeptides. FAS is expressed at high levels in liver, brain, breast, and lung. Studies have reported the in-frame fusion of FAS with estrogen receptor alpha in some cancer cell lines, and FAS expression is upregulated in breast cancer. FAS is also known as OA-519, SDR27X1, and short chain dehydrogenase/reductase family 27X, member 1.. ...
Shop Aryl-alcohol dehydrogenase ELISA Kit, Recombinant Protein and Aryl-alcohol dehydrogenase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Oksidoreduktase aril-alkohol:NADP+ (bahasa Inggris: aryl-alcohol:NADP+ oxidoreductase, aryl-alcohol dehydrogenase (NADP+), aryl alcohol dehydrogenase (nicotinamide adenine dinucleotide phosphate); coniferyl alcohol dehydrogenase; NADPH-linked benzaldehyde reductase; aryl-alcohol dehydrogenase (NADP), EC 1.1.1.91) adalah enzim oksidoreduktase yang bekerja pada alkohol aromatik, alifatik dan sinamil.[1] Reaksi yang dikatalis,[2] ...
Humbert et al. (2006) studied a 24-year-old Moroccan patient with typical fundus albipunctatus, born of first-cousin parents. He carried a 7.36-kb homozygous deletion encompassing the last 3 exons of RLBP1 (7, 8, and 9) and part of the intergenic region between RLBP1 and ABHD2, which lies downstream of RLBP1.. Dessalces et al. (2013) performed clinical and molecular investigations in patients with retinitis punctata albescens (RPA) at various ages, from November 2003, through June 2012, with no planned patient follow-up. The study included 11 patients with RPA (mean age, 24 [range, 3-39] years) from seven families and 11 control subjects undergoing evaluation. All patients had night blindness (before age 6 years in 10). The dotlike deposits were generally dense but could be rare, appearing in adaptive optics as elongated structures with variable orientation and no foveal involvement. There was no specific refractive error, and visual acuity varied widely from normal (1.2) to counting fingers. ...
The SCOP classification for the Methanol dehydrogenase subunit superfamily including the families contained in it. Additional information provided includes InterPro annotation (if available), Functional annotation, and SUPERFAMILY links to genome assignments, alignments, domain combinations, taxonomic visualisation and hidden Markov model information.
Sigma-Aldrich offers abstracts and full-text articles by [Kottawattage S A Kottawatta, Kam-Hei So, Suranga P Kodithuwakku, Ernest H Y Ng, William S B Yeung, Kai-Fai Lee].
BioAssay record AID 704302 submitted by ChEMBL: Activity of human recombinant His6-tagged carbonyl reductase 1 expressed in Escherichia coli BL21(DE3) using menadione as substrate by Michaelis-Menten plot analysis.
The dihydroflavonol-4-reductase sequence from carnation is inserted in a sense/ antisense orientation. The transcription product results in the formation of a dsDFR which suppress the expression of the endogenous DFR gene, thus allowing dominant expression of the introduced petunia Dihydroflavonol-4-reductase thus leading to the synthesis of delphinidin imparting a violet/mauve colour to the carnation ...
CTBP2 Corepressor targeting diverse transcription regulators. Functions in brown adipose tissue (BAT) differentiation. Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB ...
According to our results, a normal E. coli cell extract has a dodecanol-1 dehydrogenase activity of 9.64e-12 kat/mg (0.58 mU/mg); whereas our recombinant strain 018A has an activity of 2.93e-11 kat/mg (1.76 mU/mg). According to our analysis, the enzymatic activities of both strains are statistically different at confidence level of 0.95, which means that the part BBa_K398018 increases 2 times the alcohol dehydrogenase activity in the cell extract. We can conclude from our data that the parts BBa_K398005 and BBa_K398018 have biological activity; particularly when we used BBa_K398018 the enzyme activity of E. coli cell extracts became equivalent to 3% of the in vitro activity of the positive control (Pseudomonas putida). A comparison of both activities maybe it is not interesting from the functional point of view, since those differences could be related to substrate affinity or discrepancies in the optimal pH. However, we think that from this comparison of both in vitro activities we can suggest ...
According to our results, a normal E. coli cell extract has a dodecanol-1 dehydrogenase activity of 9.64e-12 kat/mg (0.58 mU/mg); whereas our recombinant strain 018A has an activity of 2.93e-11 kat/mg (1.76 mU/mg). According to our analysis, the enzymatic activities of both strains are statistically different at confidence level of 0.95, which means that the part BBa_K398018 increases 2 times the alcohol dehydrogenase activity in the cell extract. We can conclude from our data that the parts BBa_K398005 and BBa_K398018 have biological activity; particularly when we used BBa_K398018 the enzyme activity of E. coli cell extracts became equivalent to 3% of the in vitro activity of the positive control (Pseudomonas putida). A comparison of both activities maybe it is not interesting from the functional point of view, since those differences could be related to substrate affinity or discrepancies in the optimal pH. However, we think that from this comparison of both in vitro activities we can suggest ...
1yve: The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 A resolution.
Alcohol use that begins during adolescence affects the development of alcohol use disorders during adulthood. A new study looks at the effects of interplay between peer drinking and the functional variant rs1229984 in the alcohol dehydrogenase 1B gene (ADH1B) among adolescents. Peer drinking reduces the protective effects of this ADH1B variant.
Mammalian alcohol dehydrogenase (ADH) constitutes a complex system with different forms and extensive multiplicity (ADH1-ADH6) that catalyze the oxidation and reduction of a wide variety of alcohols...
Alcohol dehydrogenase derived from yeast is a metalloenzyme containing four tightly bound zinc atoms per molecule (Vallee and Hoch, Proc. Natl. Acad. Sci. USA, 41, 327, 1955). The optimum pH for the enzymatic oxidation of ethanol is 8.6-9.0 and is closer to 7.0 for the reduction of acetaldehyde.. ...
NAD-dependent (R,R)-butanediol dehydrogenase, catalyzes oxidation of (R,R)-2,3-butanediol to (3R)-acetoin, oxidation of meso-butanediol to (3S)-acetoin, and reduction of ...
Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase SMc04462 (SmGhrB) from Sinorhizobium meliloti in complex with NADPH and ...
Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase SMc04462 (SmGhrB) from Sinorhizobium meliloti in complex with ...
1a05: Structure of 3-isopropylmalate dehydrogenase in complex with 3-isopropylmalate at 2.0 A resolution: the role of Glu88 in the unique substrate-recognition mechanism.
huCtBP1 has been shown to interact with the histone de‐acetylase HDAC1 both in vitro and in vivo (Sundqvist et al., 1998). We have strengthened the connection by showing that the de‐acetylase inhibitor TSA decreases the inhibitory activities of mCtBP1 and Net CID. These results raise the possibility that Net and mCtBP1 might recruit one of the recently described multi‐protein complexes that contain HDACs (Alland et al., 1997; Hassig et al., 1997; Laherty et al., 1997; Nagy et al., 1997; Zhang et al., 1997). The composition and number of complexes are not well defined, but they contain uncharacterized subunits in addition to HDAC1, HDAC2, NCoR, SMRT, Sin3, RbAp46, RbAp48 and SAP30 (Ashraf and Ip, 1998; Davie, 1998; Kuo and Allis, 1998; Laherty et al., 1998; Luger and Richmond, 1998; Torchia et al., 1998; Zhang et al., 1998). Net interacts with the N‐terminal region of mCtBP1 that is so far unique to CtBP family members. The conserved central domain of CtBP might be involved in ...
Alfa Aesar™ tert-Butyl glycolate, 94% 250mg Alfa Aesar™ tert-Butyl glycolate, 94% T1 to Tetradeca -Organics
Looking for SPECTRUM Cinnamyl Acetate,25ml (26WR97)? Graingers got your back. Price:$36.20. Easy ordering & convenient delivery. Log-in or register for your pricing.
View mouse Aldh7a1 Chr18:56509687-56572951 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
tr:Q0VQG6_ALCBS] succinate-semialdehyde dehydrogenase [NAD(P)+]; K00135 succinate-semialdehyde dehydrogenase / glutarate-semialdehyde dehydrogenase [EC:1.2.1.16 1.2.1.79 1.2.1.20] ...
Semi-rational and evolutionary development of carbonyl reductase from Candida parapsilosis (CPCR) for asymmetric synthesis in organic-aqueous biphasic ...
Holzer, H. & Holldorf, A. (1957). „Isolation of a D-glycerate dehydrogenase, its properties, and its use for the optical determination of hydroxypyruvate in the presence of pyruvate". Biochem. Z. 329: 292-312. PMID 13522707 ...
The treatment for methanol poisoning involves removing and neutralizing any methanol that is still in the persons stomach and...
Learn more about oxazole-5-methanol. We enable science by offering product choice, services, process excellence and our people make it happen.
α-Hydroxy ketones and vicinal diols constitute well-known building blocks in organic synthesis. Here we describe one enzyme that enables the enantioselective synthesis of both building blocks starting from diketones. The enzyme 2,3-butanediol dehydrogenase (BudC) from S. marcescens CECT 977 belongs to the NA 2017 Catalysis, Science and Technology Hot Articles
Home » Butadienes » Butanoic acid » Butanol-extractable iodine » Butanol butyl alcohol » Butanol dehydrogenase. Butanol dehydrogenase (Science: enzyme) From clostridium acetobutylicum; reduces butyraldehyde to butanol; has higher activity on longer chain (c5,c6 or c7) aldehydes registry number: EC 1.1.1.- Synonym: NADH-dependent butanol dehydrogenase ...
Four additional variants of alcohol and aldehyde dehydrogenases have been purified and functionally characterized, and their primary structures have been determined. The results allow conclusions about the structural and evolutionary relationships within the large family of MDR alcohol dehydrogenases from characterizations of the pigeon (Columba livia) and dogfish (Scyliorhinus canicula) major liver alcohol dehydrogenases. The pigeon enzyme turns out to be of class I type and the dogfish enzyme of class III type. This result gives a third type of evidence, based on purifications and enzyme characterization in lower vertebrates, that the classical liver alcohol dehydrogenase originated by a gene duplication early in the evolution of vertebrates. It is discernable as the major liver form at about the level in-between cartilaginous and osseous fish. The results also show early divergence within the avian orders. Structures were determined by Edman degradations, making it appropriate to acknowledge ...
Shikimic acid, the sole chemical building block for the antiviral drug oseltamivir (Tamiflu®), is one of the potent pharmaceutical intermediates with three chiral centers. Here we report a metabolically engineered recombinant Bacillus megaterium strain with aroE (shikimate dehydrogenase) overexpression for the production of shikimic acid. In a 7 L bioreactor, 4.2 g/L shikimic acid was obtained using the recombinant strain over 0.53 g/L with the wild type. The enhancement of total shikimate dehydrogenase activity was 2.13-fold higher than the wild type. Maximum yield of shikimic acid (12.54 g/L) was obtained with fructose as carbon source. It was isolated from the fermentation broth using amberlite IRA-400 resin and 89 % purity of the product was achieved. This will add up a new organism in the armory for the fermentation based production which is better over plant based extraction and chemical synthesis of shikimic acid.
Alcohol dehydrogenase 4 is an enzyme that in humans is encoded by the ADH4 gene. This gene encodes class II alcohol dehydrogenase 4 pi subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. Class II alcohol dehydrogenase is a homodimer composed of 2 pi subunits. It exhibits a high activity for oxidation of long-chain aliphatic alcohols and aromatic alcohols and is less sensitive to pyrazole. This gene is localized to chromosome 4 in the cluster of alcohol dehydrogenase genes. GRCh38: Ensembl release 89: ENSG00000198099 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000037797 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". "Entrez Gene: ADH4 alcohol dehydrogenase 4 (class II), pi polypeptide". Human ADH4 genome location and ADH4 gene details page in the UCSC Genome Browser. ...
La tropinone reduttasi è un enzima appartenente alla classe delle ossidoreduttasi, che catalizza la seguente reazione: pseudotropina + NADP+ ⇄ tropinone + NADPH + H+ Questo enzima, come la tropina deidrogenasi (o TR-I), agisce ad un punto chiave del metabolismo dei tropano alcaloidi. La tropina (prodotto della TR-I) è incorporata nella isociamina e nella scopolamina, mentre la pseudotropina (prodotto di questo enzima) è il primo metabolita specifico del pathway delle calistegine. I due enzimi sono sempre presenti insieme in tutte le specie che producono tropano-alcaloidi, hanno un substrato comune (il tropinone) e sono strettamente stereospecifici. Dräger, B., Tropinone reductases, enzymes at the branch point of tropane alkaloid metabolism, in Phytochemistry, vol. 67, 2006, pp. 327-337, Entrez PubMed 16426652. Nakajima, K., Hashimoto, T. and Yamada, Y., Two tropinone reductases with different stereospecificities are short-chain dehydrogenases evolved from a common ancestor, in Proc. Natl. ...
Aldo-Keto Reductases and Toxicant Metabolism provides an overview of the rapidly growing Aldo-Keto Reductase (AKR) superfamily and its role in the metabolism of endogenous and exogenous toxicants. This book discusses the ability of AKRs to metabolize endogenous toxicants including: sugar aldehydes, advanced glycosylation end products, and lipid aldehydes (products of lipid peroxidation decomposition).
In the present study, we determined the expression and localization of porcine AKR1C1 in the ovary and uterine endometrium through RT-PCR, real-time PCR, northern blotting, and immunohistochemistry during the estrous cycle and pregnancy. Analysis of the nucleotide sequence by using the GenBank database revealed that porcine AKR1C1 cDNA belongs to the AKR family. Both nucleotide and amino acid sequences of the porcine AKR1C1 cloned in this study showed high homology with those of bovine (86/82%), goat (80/78%), rat (76/66), mouse (76/68%), and human (81/76%) 20α-HSD. Based on the results of 3-RACE, we detected a stop codon in a different site from that of porcine AKR1C1 reported previously [7]. Several conserved sequence patterns were found in the porcine AKR1C1 cloned in the present study. A catalytic tetrad, such as that consisting of Asp 50, Tyr 55, Lys 84, and His 117, is a common feature of the AKR family [1]. Other amino acids such as Gly 22, Gly 45, Asp 112, Pro 119, Gly 164, Asn 167, ...
TY - JOUR. T1 - A Catalytic Role of XoxF1 as La3+-Dependent Methanol Dehydrogenase in Methylobacterium extorquens Strain AM1. AU - Nakagawa, Tomoyuki. AU - Mitsui, Ryoji. AU - Tani, Akio. AU - Sasa, Kentaro. AU - Tashiro, Shinya. AU - Iwama, Tomonori. AU - Hayakawa, Takashi. AU - Kawai, Keiichi. PY - 2012/11/27. Y1 - 2012/11/27. N2 - In the methylotrophic bacterium Methylobacterium extorquens strain AM1, MxaF, a Ca2+-dependent methanol dehydrogenase (MDH), is the main enzyme catalyzing methanol oxidation during growth on methanol. The genome of strain AM1 contains another MDH gene homologue, xoxF1, whose function in methanol metabolism has remained unclear. In this work, we show that XoxF1 also functions as an MDH and is La3+-dependent. Despite the absence of Ca2+ in the medium strain AM1 was able to grow on methanol in the presence of La3+. Addition of La3+ increased MDH activity but the addition had no effect on mxaF or xoxF1 expression level. We purified MDH from strain AM1 grown on methanol ...
Looking for online definition of -acetoacetyl coenzyme A thiolase in the Medical Dictionary? -acetoacetyl coenzyme A thiolase explanation free. What is -acetoacetyl coenzyme A thiolase? Meaning of -acetoacetyl coenzyme A thiolase medical term. What does -acetoacetyl coenzyme A thiolase mean?
Low concentrations of hexachlorophene (HCP) inhibit a number of pyridine nucleotide-linked dehydrogenase enzymes. The I₅₀ HCP concentrations were 105 μM for pig heart isocitrate dehydrogenase (ICD), 65 μM for horse liver alcohol dehydrogenase, 39 μM for torula yeast glucose-6-phosphate dehydrogenase (G6PD), 6.0 μM for beef heart malate dehydrogenase, and 1.6 μM for bovine liver glutamate dehydrogenase (GDH) at the enzyme concentrations tested. HCP exhibited cooperative inhibition of these enzymes since the observed maximum interaction coefficient, n, between HCP binding sites ranged between 1.62 and 3.33 but it was not an allosteric effector as evidenced by Hill coefficients for the substrates of approximately 1.0 both in the absence and the presence of HCP. More detailed kinetic analysis showed that HCP in most cases exhibited mixed kinetics, giving average K[subscript i] values with G6PD of 16.6 μM for NADP⁺ and 18.2 μM for glucose -6- phosphate; with ICD of 171 µM for NADP⁺ ...
Looking for online definition of polyol dehydrogenases in the Medical Dictionary? polyol dehydrogenases explanation free. What is polyol dehydrogenases? Meaning of polyol dehydrogenases medical term. What does polyol dehydrogenases mean?
Previously we have developed a butanol tolerant mutant of Clostridium acetobutylicum Rh8, from the wild type strain DSM 1731. Strain Rh8 can tolerate up to 19 g/L butanol, with solvent titer improved accordingly, thus exhibiting industrial application potential. To test if strain Rh8 can be used for production of high level mixed alcohols, a single secondary alcohol dehydrogenase from Clostridium beijerinckii NRRL B593 was overexpressed in strain Rh8 under the control of thl promoter. The heterogenous gene sADH was functionally expressed in C. acetobutylicum Rh8. This simple, one-step engineering approach switched the traditional ABE (acetone-butanol-ethanol) fermentation to IBE (isopropanol-butanol-ethanol) fermentation. The total alcohol titer reached 23.88 g/l (7.6 g/l isopropanol, 15 g/l butanol, and 1.28 g/l ethanol) with a yield to glucose of 31.42%. The acid (butyrate and acetate) assimilation rate in isopropanol producing strain Rh8(psADH) was increased. The improved butanol tolerance and the
The metabolic pathway of phenylpropanoids involves a number of enzymes. The shikimate pathway is a seven step metabolic route used by bacteria, fungi, and plants for the biosythesis of aromatic amino acids (phenylalanine, tyrosine, and tryptophan). In plants, the biosynthesis of all phenylpropanoids begins with the amino acids phenylalanine and tyrosine. Phenylalanine ammonia-lyase (PAL, a.k.a. phenylalanine/tyrosine ammonia-lyase) is an enzyme responsible for the transformation of L-phenylalanine or tyrosine into trans-cinnamic acid or p-coumaric acid respectively and ammonia. Trans-cinnamate 4-monooxygenase (cinnamate 4-hydroxylase) is the enzyme responsible for the transformation of trans-cinnamate into 4-hydroxycinnamate (p-coumaric acid). 4-Coumarate-CoA ligase is the enzyme responsible for the transformation of 4-coumarate (p-coumaric acid) into 4-coumaroyl-CoA. Cinnamyl-alcohol dehydrogenase (CAD), an enzyme responsible for the transformation of cinnamyl alcohol into cinnamaldehyde ...

Complete genome sequence of Thermosphaera aggregans type strain (M11TLT)Complete genome sequence of Thermosphaera aggregans type strain (M11TLT)

B) MBX-related ferredoxin-NADPH oxidoreductases. C) MBX-related ferredoxin-NADPH oxidoreductases. The reference operon of ... Genes of two different types of alcohol dehydrogenases were identified, a zinc binding (Tagg_0918) and an iron containing ... 2-oxoglutarate-ferredoxin oxidoreductase (Tagg_0390-0393), 2-oxoisovalerate-ferredoxin oxidoreductase (Tagg_0826-0829) and ... MBX-related ferredoxin-NADPH oxidoreductase. In presence of elemental sulfur the ferredoxin-oxidizing, H2-evolving MBH complex ...
more infohttp://standardsingenomics.org/content/2/3/245/

Alcohol oxidoreductase - WikipediaAlcohol oxidoreductase - Wikipedia

Alcohol oxidoreductases are oxidoreductase enzymes that act upon an alcohol functional group.[1][2] ... Alcohol+oxidoreductases at the US National Library of Medicine Medical Subject Headings (MeSH) ... This oxidoreductase article is a stub. You can help Wikipedia by expanding it.. *v ... Functional group of an alcohol molecule. The carbon atom is attached to other carbon or hydrogen atoms. ...
more infohttp://www.let.rug.nl/~gosse/termpedia2/termpedia.php?language=dutch_general&density=7&link_color=000000&termpedia_system=perl_db&url=http%3A%2F%2Fen.wikipedia.org%2Fwiki%2FAlcohol_oxidoreductase

Alcohol oxidoreductase - WikipediaAlcohol oxidoreductase - Wikipedia

Alcohol oxidoreductases are oxidoreductase enzymes that act upon an alcohol functional group. They are classified under "1.1" ... Alcohol oxidoreductases at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ...
more infohttps://en.wikipedia.org/wiki/Alcohol_oxidoreductase

N-dimethyl-4-nitrosoaniline oxidoreductase alcohol - N
     Summary Report | CureHunterN'-dimethyl-4-nitrosoaniline oxidoreductase alcohol - N Summary Report | CureHunter

... a group III alcohol oxidoreductase from Rhodococcus sp, Amycolatopsis methanolica and Mycobacterium gastri; amino acid sequence ... Oxidoreductases: 9264*Alcohol Oxidoreductases: 1*N-dimethyl-4-nitrosoaniline oxidoreductase alcohol - N ... dimethyl-4-nitrosoaniline oxidoreductase alcohol - N. Subscribe to New Research on N-dimethyl-4-nitrosoaniline oxidoreductase ... a group III alcohol oxidoreductase from Rhodococcus sp, Amycolatopsis methanolica and Mycobacterium gastri; amino acid sequence ...
more infohttp://www.curehunter.com/public/keywordSummaryC095705-N--dimethyl-4-nitrosoaniline-oxidoreductase-alcohol---N.do

An unbiased cell morphology-based screen for new, biologically active small molecules.An unbiased cell morphology-based screen for new, biologically active small molecules.

Alcohol Oxidoreductases / chemistry. Apoptosis. Cell Line. Cell Line, Tumor. Cell Physiological Phenomena*. Cells / cytology*. ... Asher G,Lotem J,Cohen B,Sachs L,Shaul Y. Regulation of p53 stability and p53-dependent apoptosis by NADH quinone oxidoreductase ... This pathway was not known to be dependent on the oxidoreductase CBR1, thus validating that the compounds discovered in such ... To initially validate that the oxidoreductase CBR1 was indeed inhibited by hydroxy-PP, we measured CBR1 catalytic activity in ...
more infohttp://www.biomedsearch.com/nih/unbiased-cell-morphology-based-screen/15799708.html

TNO Repository search for: subject:bacterial metabolismTNO Repository search for: subject:'bacterial metabolism'

Chemicals/CAS: 2,6-Dichloroindophenol, 956-48-9; Alcohol Oxidoreductases, EC 1.1.-; carveol dehydrogenase, EC 1.1.1.243; ... Alcohol Oxidoreductases · Anaerobiosis · Biodegradation, Environmental · Cyclohexenes · Hydrolases · Isomerases · Monoterpenes ... Oxidoreductase · Oxygenase · Unclassified drug · Bacterial metabolism · Controlled study · Enzyme activity · Nonhuman · ...
more infohttps://repository.tudelft.nl/search/tno/?q=subject%3A%22bacterial%20metabolism%22

TNO Repository search for: subject:OxygenaseTNO Repository search for: subject:'Oxygenase'

Chemicals/CAS: 2,6-Dichloroindophenol, 956-48-9; Alcohol Oxidoreductases, EC 1.1.-; carveol dehydrogenase, EC 1.1.1.243; ... Alcohol Oxidoreductases · Anaerobiosis · Biodegradation, Environmental · Cyclohexenes · Hydrolases · Isomerases · Monoterpenes ... Oxidoreductases · Rats · Rats, Wistar · RNA, Messenger · Steroid Hydroxylases · Support, Non-U.S. Govt · Taurocholic Acid · ... cinnamyl alcohol · collagen type 16 · disulfiram · dodecyl sulfate sodium · eugenol · ferritin · ferrochelatase · glucose 6 ...
more infohttps://repository.tudelft.nl/search/tno/?q=subject%3A%22Oxygenase%22

cinnamyl alcohol dehydrogenase
     Summary Report | CureHuntercinnamyl alcohol dehydrogenase Summary Report | CureHunter

cinnamyl alcohol dehydrogenase: NADP-dependent enzyme that catalyzes the reversible conversion of p-hydroxycinnamaldehydes to ... cinnamyl alcohol dehydrogenase. Subscribe to New Research on cinnamyl alcohol dehydrogenase NADP-dependent enzyme that ... 12/01/2014 - "Lignin and lignans in plant defence: insight from expression profiling of cinnamyl alcohol dehydrogenase genes ... 09/01/1999 - "Molecular characterisation and expression of a wound-inducible cDNA encoding a novel cinnamyl-alcohol ...
more infohttp://www.curehunter.com/public/keywordSummaryC018656-cinnamyl-alcohol-dehydrogenase.do

Sugar Alcohol Dehydrogenases - Semantic ScholarSugar Alcohol Dehydrogenases - Semantic Scholar

Known as: Sugar Alcohol Dehydrogenases [Chemical/Ingredient], Oxidoreductases, Sugar Alcohol, Sugar Alcohol Oxidoreductases ( ...
more infohttps://www.semanticscholar.org/topic/Sugar-Alcohol-Dehydrogenases/1531527

adult acute myeloid leukemia cellular diagnosis 2005:2010[pubdate] *count=100 - BioMedLib™ search engineadult acute myeloid leukemia cellular diagnosis 2005:2010[pubdate] *count=100 - BioMedLib™ search engine

Alcohol Oxidoreductases / antagonists & inhibitors. Alcohol Oxidoreductases / genetics. Alcohol Oxidoreductases / metabolism. ... Alcohol Oxidoreductases; EC 1.1.1.184 / CBR1 protein, human; YDU8YIP30L / daunorubicinol; ZS7284E0ZP / Daunorubicin ...
more infohttp://www.bmlsearch.com/?kwr=adult+acute+myeloid+leukemia+cellular+diagnosis+2005:2010%5Bpubdate%5D&cxts=100&stmp=b0

Structure of human CBR3.Panel A: The substrate binding  | Open-iStructure of human CBR3.Panel A: The substrate binding | Open-i

Alcohol Oxidoreductases/chemistry*. Minor. *Aldehyde Reductase. *Antineoplastic Agents/pharmacology. *Cloning, Molecular. * ...
more infohttps://openi.nlm.nih.gov/detailedresult.php?img=PMC2741203_pone.0007113.g002&req=4

Kinetics and reaction mechanism of yeast alcohol dehydrogenase with long-chain primary alcohols. | BioGRIDKinetics and reaction mechanism of yeast alcohol dehydrogenase with long-chain primary alcohols. | BioGRID

Hexanol Or Decanol As Substrates Invariably Result In Non-linear Lineweaver-Burk Plots If The Alcohol Is The Variable Substrate ... Kinetic Studies Of Yeast Alcohol Dehydrogenase With NAD+ And Ethanol, ... Albumins, Alcohol Oxidoreductases, Alcohols, Ethanol, Glutathione, Hexanols, Kinetics, NAD, Saccharomyces cerevisiae. Biochem. ... Kinetics and reaction mechanism of yeast alcohol dehydrogenase with long-chain primary alcohols.. Schoepp W, Aurich H ...
more infohttps://thebiogrid.org/22061/publication/kinetics-and-reaction-mechanism-of-yeast-alcohol-dehydrogenase-with-long-chain-primary-alcohols.html

HSD17B4 - WikipediaHSD17B4 - Wikipedia

Its an alcohol oxidoreductase, specifically 17β-Hydroxysteroid dehydrogenase. It is involved in fatty acid β-oxidation and ...
more infohttps://en.wikipedia.org/wiki/HSD17B4

Heat Stress Affects Prostaglandin Synthesis in Bovine Endometrial Cells - PubMedHeat Stress Affects Prostaglandin Synthesis in Bovine Endometrial Cells - PubMed

Alcohol Oxidoreductases / genetics Actions. * Search in PubMed * Search in MeSH * Add to Search ...
more infohttps://pubmed.ncbi.nlm.nih.gov/29710018/

Alcohol Dehydrogenase (acceptor), 978-613-9-96853-4, 6139968534 ,9786139968534Alcohol Dehydrogenase (acceptor), 978-613-9-96853-4, 6139968534 ,9786139968534

The systematic name of this enzyme class is alcohol:acceptor oxidoreductase. Other names in common use include primary alcohol ... quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase, and alcohol:(acceptor) oxidoreductase. ... In enzymology, an alcohol dehydrogenase (acceptor) (EC 1.1.99.8) is an enzyme that catalyzes the chemical reaction a primary ... This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other ...
more infohttps://www.morebooks.de/store/es/book/alcohol-dehydrogenase-acceptor/isbn/978-613-9-96853-4?currency=SGD

Joseph P Neglia - Research Output
     - Experts@MinnesotaJoseph P Neglia - Research Output - [email protected]

Mulrooney, D. A., Dover, D. C., Li, S., Yasui, Y., Ness, K. K., Mertens, A. C., Neglia, J. P., Sklar, C. A., Robison, L. L., Davies, S. M., Hudson, M., Armstrong, G., Perkins, J., OLeary, M., Friedman, D., Pendergrass, T., Greffe, B., Odom, L., Ruccione, K., Mulvihill, J. & 30 others, Ginsberg, J., Meadows, A., Tersak, J., Ritchey, A. K., Blatt, J., Reaman, G., Packer, R., Davies, S., Bhatia, S., Qualman, S., Hammond, S., Termuhlen, A., Ruymann, F., Diller, L., Grier, H., Li, F., Meacham, L., Mertens, A., Leisenring, W., Potter, J., Greenberg, M., Nathan, P. C., Boice, J., Rodriguez, V., Smithson, W. A., Gilchrist, G., Oeffinger, K., Finklestein, J., Anderson, B. & Inskip, P., May 1 2008, In : Cancer. 112, 9, p. 2071-2079 9 p.. Research output: Contribution to journal › Article ...
more infohttps://experts.umn.edu/en/persons/joseph-p-neglia/publications/?type=%2Fdk%2Fatira%2Fpure%2Fresearchoutput%2Fresearchoutputtypes%2Fcontributiontojournal%2Farticle&page=1

Panagiotis Z Anastasiadis, PhD - Research Output
     - Mayo ClinicPanagiotis Z Anastasiadis, PhD - Research Output - Mayo Clinic

Kim, M., Ma, D. J., Calligaris, D., Zhang, S., Feathers, R. W., Vaubel, R. A., Meaux, I., Mladek, A. C., Parrish, K. E., Jin, F., Barriere, C., Debussche, L., Watters, J., Tian, S., Decker, P. A., Eckel-Passow, J. E., Kitange, G. J., Johnson, A. J., Parney, I. F., Anastasiadis, P. Z. & 3 others, Agar, N. Y. R., Elmquist, W. F. & Sarkaria, J. N., Sep 1 2018, In : Molecular Cancer Therapeutics. 17, 9, p. 1893-1901 9 p.. Research output: Contribution to journal › Article ...
more infohttps://mayoclinic.pure.elsevier.com/en/persons/panagiotis-z-anastasiadis/publications/?ordering=title&descending=false

Protein - Other functions | Britannica.comProtein - Other functions | Britannica.com

alcohol: NAD oxidoreductase. alcohol dehydrogenase. alcohol + NAD → acetaldehyde NADH. alcoholic fermentation. 1.1.1.27. L- ... Oxidoreductases and transferases account for about 50 percent of the approximately 1,000 enzymes recognized thus far. The table ... Enzymes that catalyze reactions in which hydrogen is transferred belong to the group known as oxidoreductases; those that ... The numbering system is as follows: the first number places the enzyme in one of six general groups-1, oxidoreductases; 2, ...
more infohttps://www.britannica.com/science/protein/Other-functions

Henne A[au] - PubMed - NCBIHenne A[au] - PubMed - NCBI

... generation of a gene bank for genes conferring alcohol oxidoreductase activity on Escherichia coli. ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed?cmd=search&term=Henne+A%5Bau%5D&dispmax=50

Metabolic studies on the development of ethanol-induced fatty liver in KK-Ay mice | MetaMetabolic studies on the development of ethanol-induced fatty liver in KK-Ay mice | Meta

... accelerated lipogenesis and increased utilization of the dietary fats may be possible causal factors in the alcoholic fatty ... Mechanisms involved in the development of the alcoholic fatty liver in KK-Ay mice were investigated. Incorporation studies ... Alcohol Oxidoreductases. Related Papers. *. An analysis of the relationships among obesity, plasma insulin and hepatic ... Hepatic lipogenesis and mobilization of peripheral fats in the formation of alcoholic fatty liver. Japanese Journal of ...
more infohttps://www.meta.org/papers/metabolic-studies-on-the-development-of-ethanol-in/477

Mahmoud Ahmed, PhD, MS - Publications
     - UTMB Health Research Expert ProfilesMahmoud Ahmed, PhD, MS - Publications - UTMB Health Research Expert Profiles

Ahmed, M., Aleksunes, L. M., Boeuf, P., Chung, M. K., Daoud, G., Desoye, G., Díaz, P., Golos, T. G., Illsley, N. P., Kikuchi, K., Komatsu, R., Lao, T., Morales-Prieto, D. M., Nanovskaya, T., Nobuzane, T., Roberts, C. T., Saffery, R., Tamura, I., Tamura, K., Than, N. G. & 8 others, Tomi, M., Umbers, A., Wang, B., Weedon-Fekjaer, M. S., Yamada, S., Yamazaki, K., Yoshie, M. & Lash, G. E., 2013, In : Placenta. 34, SUPPL. Research output: Contribution to journal › Article ...
more infohttps://researchexperts.utmb.edu/en/persons/mahmoud-ahmed/publications/?type=%2Fdk%2Fatira%2Fpure%2Fresearchoutput%2Fresearchoutputtypes%2Fcontributiontojournal%2Farticle