Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:6.2.1.1 (ACS)
78,556 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The amphiphilic behavior of the S-enantiomer of 3(S)-[(2-carboxyethyl)sulfanyl]-3-[2-(8-phenyloctyl)phenyl] propionic acid disodium salt (C26H32O4S.2Na) has been investigated as a function of the ionic strength, mu (buffer and simple electrolyte). The linearity predicted by the Corrin-Harkins relation (J. Am. Chem. Soc. 1947, 69, 683-688) is observed at low buffer concentrations, and it is verified that the nature of the buffer is of less importance than the concentration of the counterion. At high counterion concentrations, the salting-out effect predicted by Mukerjee in 1965 (J. Phys. Chem. 1965, 69, 4038-4040) and 1967 (Adv. Coll. Interf. Sci. 1967, 1, 241-275) manifests itself, and a more complete equation resulting from attaching a salting-out term to the Corrin-Harkins relation, as used recently by Mukerjee and Chan (ACS Abstracts of Papers 1993, 206, COLL 164; Ph.D. Thesis, University of Wisconsin, 1993), gives a better representation of the experimental data. It is shown that the parameter values obtained from this equation are reasonable and predict self-association in the form of micelles rather than as small aggregates.
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PMID:Confirmation of the Mukerjee term in an extended Corrin-Harkins relation using an anionic amphiphilic drug. 868 52

The possibilities of separating monovalent and multivalent ions by electrodialysis (ED) and nanofiltration (NF) are explored. Five synthetic single salt solutions were applied to ED and NF: NaCl, Na(2)SO(4), MgCl(2), MgSO(4) and NaNO(3). Two combinations of anionic and cationic exchange membranes were evaluated for ED (AMV/CMV Selemion membranes and ACS/CMS Tokuyama membranes), and two membranes were evaluated for NF (NTR 7450 and UTC-60). The separation was evaluated using an alternative parameter, the separation efficiency, in order to compare ED and NF. The separation efficiency ranges from 0% (no separation) to 100% (perfect separation). Both NF membranes had a good separation efficiency for the separation of monovalent and divalent anions (ca. 60%); the ED membranes performed worse. For the separation of monovalent and divalent cations, the UTC-60 membrane was the best for the considered separation because of size exclusion effects for the larger divalent ion. The ACS/CMS membranes had a similar separation efficiency (ca. 60%); the NTR 7540 membrane and AMV/CMV ED membranes showed only a small separation.
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PMID:Separation of monovalent and divalent ions from aqueous solution by electrodialysis and nanofiltration. 1497 68

ADP-forming acetyl-CoA synthetase (ACD), the novel enzyme of acetate formation and energy conservation in archaea Acety - CoA + ADP + Pi<==>acetate + ATP CoA), has been studied only in few hyperthermophilic euryarchaea. Here, we report the characterization of two ACDs with unique molecular and catalytic features, from the mesophilic euryarchaeon Haloarcula marismortui and from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum. ACD from H. marismortui was purified and characterized as a salt-dependent, mesophilic ACD of homodimeric structure (166 kDa). The encoding gene was identified in the partially sequenced genome of H. marismortui and functionally expressed in Escherichia coli. The recombinant enzyme was reactivated from inclusion bodies following solubilization and refolding in the presence of salts. The ACD catalyzed the reversible ADP- and Pi-dependent conversion of acetyl-CoA to acetate. In addition to acetate, propionate, butyrate, and branched-chain acids (isobutyrate, isovalerate) were accepted as substrates, rather than the aromatic acids, phenylacetate and indol-3-acetate. In the genome of P. aerophilum, the ORFs PAE3250 and PAE 3249, which code for alpha and beta subunits of an ACD, overlap each other by 1 bp, indicating a novel gene organization among identified ACDs. The two ORFs were separately expressed in E. coli and the recombinant subunits alpha (50 kDa) and beta (28 kDa) were in-vitro reconstituted to an active heterooligomeric protein of high thermostability. The first crenarchaeal ACD showed the broadest substrate spectrum of all known ACDs, catalyzing the conversion of acetyl-CoA, isobutyryl-CoA, and phenylacetyl-CoA at high rates. In contrast, the conversion of phenylacetyl-CoA in euryarchaeota is catalyzed by specific ACD isoenzymes.
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PMID:Unusual ADP-forming acetyl-coenzyme A synthetases from the mesophilic halophilic euryarchaeon Haloarcula marismortui and from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum. 1534 Jul 86

Ethylene biosynthesis in higher plants is regulated developmentally and environmentally. To investigate the regulation of ACC synthase gene expression, the promoters of Arabidopsis ACS genes, AtACS4, AtACS5, and AtACS7, were fused to a GUS reporter gene, and the recombinant transgenes were introduced into Arabidopsis to produce three groups of AtACS::GUS transgenic plants. Histochemic and fluorometric study of these transgenic plants revealed that promoters of AtACS4, AtACS, and AtACS7 are all active in dark-germinated seedlings. AtACS5 has the highest promoter activity in leaves of 2-week-old light-grown seedlings among the three AtACS genes studied. In the mature leaves, AtACS4 and AtACS7 genes are expressed in both veins and areoles, whereas AtACS5 is expressed at a higher level in the areoles and epidermal cells surrounding trichomes. The promoter activities of all these AtACS genes are found in the reproductive organs. AtACS5 and AtACS7 are highly expressed in petals, sepals, carpels, stamens, cauline leaves, inflorescence stems, and siliques, while AtACS4 expression is undetectable in the petals of open flowers. All three AtACS genes are expressed in root tissue. In the 2-week-old light-grown Arabidopsis, the AtACS4 promoter is responsive to the plant hormones IAA, ethylene, and ABA, and to darkness and wounding; the AtACS5 promoter to IAA, ABA, salt, high temperature, and wounding; and the AtACS7 promoter to GA3, ethylene, and ABA, and to darkness and salt. Low-temperature treatment abolishes the darkness-induced AtACS7 gene expression, but not that of AtACS4. Each AtACS gene has a unique expression profile during growth and development. It appears that at any developmental stage or any growth period of Arabidopsis, there is always a member of AtACS multigene family that is actively expressed.
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PMID:The GUS reporter-aided analysis of the promoter activities of Arabidopsis ACC synthase genes AtACS4, AtACS5, and AtACS7 induced by hormones and stresses. 1569 63

Halophilic archaea activate acetate via an (acetate)-inducible AMP-forming acetyl-CoA synthetase (ACS), (Acetate+ATP+CoA --> Acetyl-CoA+AMP+PP(i)). The enzyme from Haloarcula marismortui was purified to homogeneity. It constitutes a 72-kDa monomer and exhibited a temperature optimum of 41 degrees C and a pH optimum of 7.5. For optimal activity, concentrations between 1 M and 1.5 M KCl were required, whereas NaCl had no effect. The enzyme was specific for acetate (100%) additionally accepting only propionate (30%) as substrate. The kinetic constants were determined in both directions of the reaction at 37 degrees C. Using the N-terminal amino acid sequence an open reading frame - coding for a 74 kDa protein - was identified in the partially sequenced genome of H. marismortui. The function of the ORF as acs gene was proven by functional overexpression in Escherichia coli. The recombinant enzyme was reactivated from inclusion bodies, following solubilization in urea and refolding in the presence of salts, reduced and oxidized glutathione and substrates. Refolding was dependent on salt concentrations of at least 2 M KCl. The recombinant enzyme showed almost identical molecular and catalytic properties as the native enzyme. Sequence comparison of the Haloarcula ACS indicate high similarity to characterized ACSs from bacteria and eukarya and the archaeon Methanosaeta. Phylogenetic analysis of ACS sequences from all three domains revealed a distinct archaeal cluster suggesting monophyletic origin of archaeal ACS.
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PMID:AMP-forming acetyl-CoA synthetase from the extremely halophilic archaeon Haloarcula marismortui: purification, identification and expression of the encoding gene, and phylogenetic affiliation. 1594 65

Gateways to Clinical Trials is a guide to the most recent clinical trials in current literature and congresses. The data in the following tables have been retrieved from the Clinical Trials Knowledge Area of Prous Science Integrity, the drug discovery and development portal, http://integrity.prous.com. This issue focuses on the following selection of drugs: Abiraterone acetate, acyline, adalimumab, adenosine triphosphate, AEE-788, AIDSVAX gp120 B/B, AK-602, alefacept, alemtuzumab, alendronic acid sodium salt, alicaforsen sodium, alprazolam, amdoxovir, AMG-162, aminolevulinic acid hydrochloride, aminolevulinic acid methyl ester, aminophylline hydrate, anakinra, anecortave acetate, anti-CTLA-4 MAb, APC-8015, aripiprazole, aspirin, atazanavir sulfate, atomoxetine hydrochloride, atorvastatin calcium, atrasentan, AVE-5883, AZD-2171; Betamethasone dipropionate, bevacizumab, bimatoprost, biphasic human insulin (prb), bortezomib, BR-A-657, BRL-55730, budesonide, busulfan; Calcipotriol, calcipotriol/betamethasone dipropionate, calcium folinate, capecitabine, capravirine, carmustine, caspofungin acetate, cefdinir, certolizumab pegol, CG-53135, chlorambucil, ciclesonide, ciclosporin, cisplatin, clofarabine, clopidogrel hydrogensulfate, clozapine, co-trimoxazole, CP-122721, creatine, CY-2301, cyclophosphamide, cypher, cytarabine, cytolin; D0401, darbepoetin alfa, darifenacin hydrobromide, DASB, desipramine hydrochloride, desloratadine, desvenlafaxine succinate, dexamethasone, didanosine, diquafosol tetrasodium, docetaxel, doxorubicin hydrochloride, drotrecogin alfa (activated), duloxetine hydrochloride, dutasteride; Ecallantide, efalizumab, efavirenz, eletriptan, emtricitabine, enfuvirtide, enoxaparin sodium, estramustine phosphate sodium, etanercept, ethinylestradiol, etonogestrel, etonogestrel/ethinylestradiol, etoposide, exenatide; Famciclovir, fampridine, febuxostat, filgrastim, fludarabine phosphate, fluocinolone acetonide, fluorouracil, fluticasone propionate, fluvastatin sodium, fondaparinux sodium; Gaboxadol, gamma-hydroxybutyrate sodium, gefitinib, gelclair, gemcitabine, gemfibrozil, glibenclamide, glyminox; Haloperidol, heparin sodium, HPV 16/HPV 18 vaccine, human insulin, human insulin; Icatibant, imatinib mesylate, indium 111 (111In) ibritumomab tiuxetan, infliximab, INKP-100, iodine (I131) tositumomab, IoGen, ipratropium bromide, ixabepilone; L-870810, lamivudine, lapatinib, laquinimod, latanoprost, levonorgestrel, licochalcone a, liposomal doxorubicin, lopinavir, lopinavir/ritonavir, lorazepam, lovastatin; Maraviroc, maribavir, matuzumab, MDL-100907, melphalan, methotrexate, methylprednisolone, mitomycin, mitoxantrone hydrochloride, MK-0431, MN-001, MRKAd5 HIV-1 gag/pol/nef, MRKAd5gag, MVA.HIVA, MVA-BN Nef, MVA-Muc1-IL-2, mycophenolate mofetil; Nelfinavir mesilate, nesiritide, NSC-330507; Olanzapine, olmesartan medoxomil, omalizumab, oral insulin, osanetant; PA-457, paclitaxel, paroxetine, paroxetine hydrochloride, PCK-3145, PEG-filgrastim, peginterferon alfa-2a, peginterferon alfa-2b, perillyl alcohol, pexelizumab, pimecrolimus, pitavastatin calcium, porfiromycin, prasterone, prasugrel, pravastatin sodium, prednisone, pregabalin, prinomastat, PRO-2000, propofol, prostate cancer vaccine; Rasagiline mesilate, rhBMP-2/ACS, rhBMP-2/BCP, rhC1, ribavirin, rilpivirine, ritonavir, rituximab, Ro-26-9228, rosuvastatin calcium, rosuvastatin sodium, rubitecan; Selodenoson, simvastatin, sirolimus, sitaxsentan sodium, sorafenib, SS(dsFv)-PE38, St. John's Wort extract, stavudine; Tacrolimus, tadalafil, tafenoquine succinate, talaglumetad, tanomastat, taxus, tegaserod maleate, telithromycin, tempol, tenofovir, tenofovir disoproxil fumarate, testosterone enanthate, TH-9507, thalidomide, tigecycline, timolol maleate, tiotropium bromide, tipifarnib, torcetrapib, trabectedin, travoprost, travoprost/timolol, treprostinil sodium; Valdecoxib, vardenafil hydrochloride hydrate, varenicline, VEGF-2 gene therapy, venlafaxine hydrochloride, vildagliptin, vincristine sulfate, voriconazole, VRX-496, VX-385; Warfarin sodium; Ximelagatran; Yttrium 90 (90Y) ibritumomab tiuxetan; Zanolimumab, zidovudine.
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PMID:Gateways to clinical trials. 1608 22

The aim was to understand how interaction of the central carbon and the secondary carnitine metabolisms is affected under salt stress and its effect on the production of L-carnitine by Escherichia coli. The biotransformation of crotonobetaine into L-carnitine by resting cells of E. coli O44 K74 was improved by salt stress, a yield of nearly twofold that for the control being obtained with 0.5 M NaCl. Crotonobetaine and the L-carnitine formed acted as an osmoprotectant during cell growth and biotransformation in the presence of NaCl. The enzyme activities involved in the biotransformation process (crotonobetaine hydration reaction and crotonobetaine reduction reaction), in the synthesis of acetyl-CoA/acetate (pyruvate dehydrogenase, acetyl-CoA synthetase [ACS] and ATP/acetate phosphotransferase) and in the distribution of metabolites for the tricarboxylic acid cycle (isocitrate dehydrogenase [ICDH]) and glyoxylate shunt (isocitrate lyase [ICL]) were followed in batch with resting cells both in the presence and absence of NaCl and in perturbation experiments performed on growing cells in a high density cell recycle membrane reactor. Further, the levels of carnitine, crotonobetaine, gamma-butyrobetaine and ATP and the NADH/NAD(+) ratio were measured in order to know how the metabolic state was modified and coenzyme pools redistributed as a result of NaCl's effect on the energy content of the cell. The results provided the first experimental evidence of the important role played by salt stress during resting and growing cell biotransformation (0.5 M NaCl increased the L-carnitine production in nearly 85%), and the need for high levels of ATP to maintain metabolite transport and biotransformation. Moreover, the main metabolic pathways and carbon flow operating during cell biotransformation was that controlled by the ICDH/ICL ratio, which decreased from 8.0 to 2.5, and the phosphotransferase/ACS ratio, which increased from 2.1 to 5.2, after a NaCl pulse fivefold the steady-state level. Resting E. coli cells were seen to be made up of heterogeneous populations consisting of several types of subpopulation (intact, depolarized, and permeabilized cells) differing in viability and metabolic activity as biotransformation run-time and the NaCl concentration increased. The results are discussed in relation with the general stress response of E. coli, which alters the NADH/NAD(+) ratio, ATP content, and central carbon enzyme activities.
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PMID:Salt stress effects on the central and carnitine metabolisms of Escherichia coli. 1689 34

Intensification of the synthesis of the microbial exopolysaccharide ethapolan by Acinetobacter sp. B-7005 was shown to occur on a mixture of energy-deficient growth substrates (acetate + glucose). When the bacterium grew on the substrate mixture, both substrates were utilized simultaneously; acetate was taken up by means of active transport at the expense of the energy of the proton-motive force. When acetate was present in the form of a sodium salt, the activities of acetyl-CoA synthetase and phosphoenolpyruvate synthetase (the key enzyme of gluconeogenesis) were tenfold higher than in the presence of potassium acetate, and the indexes of ethapolan synthesis were two times higher. The positive effect of Na+ on ethapolan synthesis is supposed to consist in the creation of ion gradients on the membrane, necessary for the generation of the proton-motive force. Simultaneous functioning of the glyoxylate cycle and pyruvate carboxylase reaction, as well as an increase in the activity of isocitrate lyase, malate synthase, and phosphoenolpyruvate synthetase, provide evidence of increased gluconeogenesis in the presence of the acetate + glucose mixture (as compared to gluconeogenesis on the corresponding monosubstrates).
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PMID:[Synthesis of the exopolysaccharide ethapolan on a mixture of energy-deficient growth substrates]. 1741 Aug 72

This work focuses on synthetic methods to produce monodisperse Ni colloidal nanoparticles (NPs), in the 4-16 nm size range, and their structural characterization. Narrow size distribution nanoparticles were obtained by high-temperature reduction of a nickel salt and the production of tunable sizes of the Ni NPs was improved compared to other methods previously described. The as-synthesized nanoparticles exhibited spherical shape and highly disordered structure, as it could be assigned by X-ray diffraction (XRD) and high resolution transmission electron microscopy (HRTEM). Annealing at high temperature in organic solvent resulted in an increase of nanoparticle atomic ordering; in this case, the XRD pattern showed an fcc-like structure. Complementary data obtained by X-ray absorption spectroscopy confirmed the complex structure of these nanoparticles. Temperature dependence of the magnetic susceptibility of these highly disordered Ni NPs showed the magnetic behavior cannot be described by the conventional superparamagnetic theory, claiming the importance of the internal structure in the magnetic behavior of such nanomaterials.
ACS Nano 2008 Jun
PMID:Chemical synthesis and structural characterization of highly disordered N colloidal nanoparticles. 1920 50

Luminescent silicon quantum dots (Si QDs) have great potential for use in biological imaging and diagnostic applications. To exploit this potential, they must remain luminescent and stably dispersed in water and biological fluids over a wide range of pH and salt concentration. There have been many challenges in creating such stable water-dispersible Si QDs, including instability of photoluminescence due their fast oxidation in aqueous environments and the difficulty of attaching hydrophilic molecules to Si QD surfaces. In this paper, we report the preparation of highly stable aqueous suspensions of Si QDs using phospholipid micelles, in which the optical properties of Si nanocrystals are retained. These luminescent micelle-encapsulated Si QDs were used as luminescent labels for pancreatic cancer cells. This paves the way for silicon quantum dots to be a valuable optical probe in biomedical diagnostics.
ACS Nano 2008 May
PMID:Biocompatible luminescent silicon quantum dots for imaging of cancer cells. 1920 83


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