Relevant bibliographies by topics / OYE Enzymes

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  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
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Academic literature on the topic 'OYE Enzymes'

Author: Grafiati
Published: 4 June 2021
Last updated: 5 February 2022

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Journal articles on the topic "OYE Enzymes"

1

Williams, Richard E., Deborah A. Rathbone, Nigel S. Scrutton, and Neil C. Bruce. "Biotransformation of Explosives by the Old Yellow Enzyme Family of Flavoproteins." Applied and Environmental Microbiology 70, no. 6 (June 2004): 3566–74. http://dx.doi.org/10.1128/aem.70.6.3566-3574.2004.

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ABSTRACT Several independent studies of bacterial degradation of nitrate ester explosives have demonstrated the involvement of flavin-dependent oxidoreductases related to the old yellow enzyme (OYE) of yeast. Some of these enzymes also transform the nitroaromatic explosive 2,4,6-trinitrotoluene (TNT). In this work, catalytic capabilities of five members of the OYE family were compared, with a view to correlating structure and function. The activity profiles of the five enzymes differed substantially; no one compound proved to be a good substrate for all five enzymes. TNT is reduced, albeit slowly, by all five enzymes. The nature of the transformation products differed, with three of the five enzymes yielding products indicative of reduction of the aromatic ring. Our findings suggest two distinct pathways of TNT transformation, with the initial reduction of TNT being the key point of difference between the enzymes. Characterization of an active site mutant of one of the enzymes suggests a structural basis for this difference.
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van Dillewijn, Pieter, Rolf-Michael Wittich, Antonio Caballero, and Juan-Luis Ramos. "Subfunctionality of Hydride Transferases of the Old Yellow Enzyme Family of Flavoproteins of Pseudomonas putida." Applied and Environmental Microbiology 74, no. 21 (September 12, 2008): 6703–8. http://dx.doi.org/10.1128/aem.00386-08.

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ABSTRACT To investigate potential complementary activities of multiple enzymes belonging to the same family within a single microorganism, we chose a set of Old Yellow Enzyme (OYE) homologs of Pseudomonas putida. The physiological function of these enzymes is not well established; however, an activity associated with OYE family members from different microorganisms is their ability to reduce nitroaromatic compounds. Using an in silico approach, we identified six OYE homologs in P. putida KT2440. Each gene was subcloned into an expression vector, and each corresponding gene product was purified to homogeneity prior to in vitro analysis for its catalytic activity against 2,4,6-trinitrotoluene (TNT). One of the enzymes, called XenD, lacked in vitro activity, whereas the other five enzymes demonstrated type I hydride transferase activity and reduced the nitro groups of TNT to hydroxylaminodinitrotoluene derivatives. XenB has the additional ability to reduce the aromatic ring of TNT to produce Meisenheimer complexes, defined as type II hydride transferase activity. The condensations of the primary products of type I and type II hydride transferases react with each other to yield diarylamines and nitrite; the latter can be further reduced to ammonium and serves as a nitrogen source for microorganisms in vivo.
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García-Huertas, Paola, Ana María Mejía-Jaramillo, Carlos Renato Machado, Anna Cláudia Guimarães, and Omar Triana-Chávez. "Prostaglandin F2α synthase in Trypanosoma cruzi plays critical roles in oxidative stress and susceptibility to benznidazole." Royal Society Open Science 4, no. 9 (September 2017): 170773. http://dx.doi.org/10.1098/rsos.170773.

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Nifurtimox (Nfx) and benznidazole (Bz) are the current drugs used for the treatment of Chagas disease. The mechanisms of action and resistance to these drugs in this parasite are poorly known. Prostaglandin F2α synthase or old yellow enzyme (OYE), an NAD(P)H flavin oxidoreductase, has been involved in the activation pathway of other trypanocidal drugs such as Nfx; however, its role in the mechanism of action of Bz is uncertain. In this paper, we performed some experiments of functional genomics in the parasite Trypanosoma cruzi with the aim to test the role of this gene in the resistance to Bz. For this, we overexpressed this gene in sensitive parasites and evaluated the resistance level to the drug and other chemical compounds such as hydrogen peroxide, methyl methanesulfonate and gamma radiation. Interestingly, parasites overexpressing OYE showed alteration of enzymes associated with oxidative stress protection such as superoxide dismutase A and trypanothione reductase. Furthermore, transfected parasites were more sensitive to drugs, genetic damage and oxidative stress. Additionally, transfected parasites were less infective than wild-type parasites and they showed higher alteration in mitochondrial membrane potential and cell cycle after treatment with Bz. These results supply essential information to help further the understanding of the mechanism of action of Bz in T. cruzi .
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Tentori, Francesca, Teodora Bavaro, Elisabetta Brenna, Danilo Colombo, Daniela Monti, Riccardo Semproli, and Daniela Ubiali. "Immobilization of Old Yellow Enzymes via Covalent or Coordination Bonds." Catalysts 10, no. 2 (February 20, 2020): 260. http://dx.doi.org/10.3390/catal10020260.

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Ene-reductases (ERs) belonging to the old yellow enzyme (OYE) family have been thoroughly investigated for the stereospecific reduction of activated prochiral C=C double bonds. In this work, OYE3 was immobilized both by covalent binding on glyoxyl-agarose (OYE3-GA), and by affinity-based adsorption on EziGTM particles (OYE3-EziG). The immobilized OYE3-GA was demonstrated to be active (activity recovery = 52%) and to retain almost 100% of its activity under the enzymatic assay conditions (50 mM phosphate buffer pH 7, 28 °C) for six days, whereas the activity of the non-immobilized enzyme dropped to 50% after two days. In the case of EziGTM, the highest activity recovery (54%) was achieved by using the most hydrophilic carrier (EziGTM Opal) that was selected for the full characterization of this type of enzyme preparation (stability, recycling, re-use, enzyme leakage). OYE3-EziG was slightly less stable than OYE3-GA under the same experimental conditions. OYE3-GA could be recycled and re-used for up to 12 reaction cycles in the bioreduction of α-methyl-trans-cinnamaldehyde; after 12 runs, the highest conversion achieved was 40%. In the case of the co-immobilized OYE3/GDH-EziG, the conversion dropped to 56% after two reaction cycles. No enzyme leakage was detected over 48 h for both OYE3-GA and OYE3/GDH-EziG (50 mM phosphate buffer pH 7, 28 °C). These seed results pave the way for a true optimization of the immobilization of OYE3, as well as for the use of immobilized OYE3 for preparative applications both in batch and continuous flow conditions.
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Hall, Mélanie, Clemens Stueckler, Bernhard Hauer, Rainer Stuermer, Thomas Friedrich, Michael Breuer, Wolfgang Kroutil, and Kurt Faber. "Asymmetric Bioreduction of Activated C=C Bonds UsingZymomonas mobilis NCR Enoate Reductase and Old Yellow Enzymes OYE 1–3 from Yeasts." European Journal of Organic Chemistry 2008, no. 9 (March 2008): 1511–16. http://dx.doi.org/10.1002/ejoc.200701208.

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Odat, Osama, Samer Matta, Hadi Khalil, Sotirios C. Kampranis, Raymond Pfau, Philip N. Tsichlis, and Antonios M. Makris. "Old Yellow Enzymes, Highly Homologous FMN Oxidoreductases with Modulating Roles in Oxidative Stress and Programmed Cell Death in Yeast." Journal of Biological Chemistry 282, no. 49 (September 26, 2007): 36010–23. http://dx.doi.org/10.1074/jbc.m704058200.

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In a genetic screen to identify modifiers of Bax-dependent lethality in yeast, the C terminus of OYE2 was isolated based on its capacity to restore sensitivity to a Bax-resistant yeast mutant strain. Overexpression of full-length OYE2 suppresses Bax lethality in yeast, lowers endogenous reactive oxygen species (ROS), increases resistance to H2O2-induced programmed cell death (PCD), and significantly lowers ROS levels generated by organic prooxidants. Reciprocally, Δoye2 yeast strains are sensitive to prooxidant-induced PCD. Overexpression and knock-out analysis indicate these OYE2 antioxidant activities are opposed by OYE3, a highly homologous heterodimerizing protein, which functions as a prooxidant promoting H2O2-induced PCD in wild type yeast. To exert its effect OYE3 requires the presence of OYE2. Deletion of the 12 C-terminal amino acids and catalytic inactivation of OYE2 by a Y197F mutation enhance significantly survival upon H2O2-induced PCD in wild type cells, but accelerate PCD in Δoye3 cells, implicating the oye2p-oye3p heterodimer for promoting cell death upon oxidative stress. Unexpectedly, a strain with a double knock-out of these genes (Δoye2 oye3) is highly resistant to H2O2-induced PCD, exhibits increased respiratory capacity, and undergoes less cell death during the adaptive response in chronological aging. Simultaneous deletion of OYE2 and other antioxidant genes hyperinduces endogenous levels of ROS, promoting H2O2-induced cell death: in Δoye2 glr1 yeast high levels of oxidized glutathione elicited gross morphological aberrations involving the actin cytoskeleton and defects in organelle partitioning. Altering the ratio of reduced to oxidized glutathione by exogenous addition of GSH fully reversed these alterations. Based on this work, OYE proteins are firmly placed in the signaling network connecting ROS generation, PCD modulation, and cytoskeletal dynamics in yeast.
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Hall, Mélanie, Clemens Stueckler, Bernhard Hauer, Rainer Stuermer, Thomas Friedrich, Michael Breuer, Wolfgang Kroutil, and Kurt Faber. "Asymmetric Bioreduction of Activated C=C Bonds UsingZymomonas mobilis NCR Enoate Reductase and Old Yellow Enzymes OYE 1–3 from Yeasts (Eur. J. Org. Chem. 9/2008)." European Journal of Organic Chemistry 2008, no. 9 (March 2008): 1479. http://dx.doi.org/10.1002/ejoc.200890018.

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Nizam, Shadab, Rajesh Kumar Gazara, Sandhya Verma, Kunal Singh, and Praveen Kumar Verma. "Comparative Structural Modeling of Six Old Yellow Enzymes (OYEs) from the Necrotrophic Fungus Ascochyta rabiei : Insight into Novel OYE Classes with Differences in Cofactor Binding, Organization of Active Site Residues and Stereopreferences." PLoS ONE 9, no. 4 (April 28, 2014): e95989. http://dx.doi.org/10.1371/journal.pone.0095989.

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Memon, Safyan Aman, Kinaan Aamir Khan, and Hammad Naveed. "HECNet: a hierarchical approach to enzyme function classification using a Siamese Triplet Network." Bioinformatics 36, no. 17 (May 25, 2020): 4583–89. http://dx.doi.org/10.1093/bioinformatics/btaa536.

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Abstract Motivation Understanding an enzyme’s function is one of the most crucial problem domains in computational biology. Enzymes are a key component in all organisms and many industrial processes as they help in fighting diseases and speed up essential chemical reactions. They have wide applications and therefore, the discovery of new enzymatic proteins can accelerate biological research and commercial productivity. Biological experiments, to determine an enzyme’s function, are time-consuming and resource expensive. Results In this study, we propose a novel computational approach to predict an enzyme’s function up to the fourth level of the Enzyme Commission (EC) Number. Many studies have attempted to predict an enzyme’s function. Yet, no approach has properly tackled the fourth and final level of the EC number. The fourth level holds great significance as it gives us the most specific information of how an enzyme performs its function. Our method uses innovative deep learning approaches along with an efficient hierarchical classification scheme to predict an enzyme’s precise function. On a dataset of 11 353 enzymes and 402 classes, we achieved a hierarchical accuracy and Macro-F1 score of 91.2% and 81.9%, respectively, on the 4th level. Moreover, our method can be used to predict the function of enzyme isoforms with considerable success. This methodology is broadly applicable for genome-wide prediction that can subsequently lead to automated annotation of enzyme databases and the identification of better/cheaper enzymes for commercial activities. Availability and implementation The web-server can be freely accessed at http://hecnet.cbrlab.org/. Supplementary information Supplementary data are available at Bioinformatics online.
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Cieśla, Joanna. "Metabolic enzymes that bind RNA: yet another level of cellular regulatory network?" Acta Biochimica Polonica 53, no. 1 (January 12, 2006): 11–32. http://dx.doi.org/10.18388/abp.2006_3360.

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Several enzymes that were originally characterized to have one defined function in intermediatory metabolism are now shown to participate in a number of other cellular processes. Multifunctional proteins may be crucial for building of the highly complex networks that maintain the function and structure in the eukaryotic cell possessing a relatively low number of protein-encoding genes. One facet of this phenomenon, on which I will focus in this review, is the interaction of metabolic enzymes with RNA. The list of such enzymes known to be associated with RNA is constantly expanding, but the most intriguing question remains unanswered: are the metabolic enzyme-RNA interactions relevant in the regulation of cell metabolism? It has been proposed that metabolic RNA-binding enzymes participate in general regulatory circuits linking a metabolic function to a regulatory mechanism, similar to the situation of the metabolic enzyme aconitase, which also functions as iron-responsive RNA-binding regulatory element. However, some authors have cautioned that some of such enzymes may merely represent "molecular fossils" of the transition from an RNA to a protein world and that the RNA-binding properties may not have a functional significance. Here I will describe enzymes that have been shown to interact with RNA (in several cases a newly discovered RNA-binding protein has been identified as a well-known metabolic enzyme) and particularly point out those whose ability to interact with RNA seems to have a proven physiological significance. I will also try to depict the molecular switch between an enzyme's metabolic and regulatory functions in cases where such a mechanism has been elucidated. For most of these enzymes relations between their enzymatic functions and RNA metabolism are unclear or seem not to exist. All these enzymes are ancient, as judged by their wide distribution, and participate in fundamental biochemical pathways.
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Dissertations / Theses on the topic "OYE Enzymes"

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Geddes, Alexander. "A study of H-transfer kinetics and catalytic protein dynamics in ene-reductase enzymes of the OYE family." Thesis, University of Manchester, 2017. https://www.research.manchester.ac.uk/portal/en/theses/a-study-of-htransfer-kinetics-and-catalytic-protein-dynamics-in-enereductase-enzymesof-the-oye-family(b9a8338b-7917-4197-9870-261d90228495).html.

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Dynamic structural fluctuations occurring over a broad range of timescales are now known to facilitate the catalytic function of enzymes, but there is less comprehensive experimental evidence linking fast-timescale, high frequency motions to the reaction coordinate. Interest in the role of such motions has recently surged and been the subject of intensive experimental efforts, in part due to the identification of enzymatic hydride tunnelling reactions. This mechanism involves transiently degenerate product and reactant states, which enable H-transfer to occur instantaneously without the need to surmount the activation barrier associated with traditional transition-state based models of enzyme catalysis. The primary gauge of tunnelling in enzyme-catalysed reactions is the identification of temperature dependent kinetic isotope effects (KIEs), i.e. the relative rates of a reaction where the transferred atom is substituted for an alternate isotope. The identification of temperature-, and also pressure-, dependent KIEs has resulted in the emergence of new models of describing enzymatic H-transfer. These invoke a role for fast-timescale protein motions that 'promote' transfer via tunnelling. A popular model system for studying enzymatic H-tunnelling reactions is Pentaerythritol tetranitrate reductase, which belongs to the Old Yellow Enzyme (OYE) family of ene-reductases. These nicotinamide coenzyme dependent oxidoreductases catalyse the stereospecific reduction of alpha/β-unsaturated alkene containing substrates. Here, the importance of donor-acceptor distances in determining the observed rate of PETNR reduction with NAD(P)H is probed via a detailed structural and kinetic analysis of site-directed variants. In addition, an investigation of distance-dependent Nuclear Overhauser effects via Nuclear Magnetic Resonance (NMR) spectroscopy is undertaken to assess active site organisation and measure donor-acceptor distances in PETNR-substrate complexes. A variable pressure NMR study reveals how NOE build- up is perturbed in high-energy conformers favoured as a result of the application of increased hydrostatic pressures. Recently there has been interest in exploiting the stereoselective properties of reactions catalysed by ene-reductase enzymes for use in biocatalytic reactions to produce industrially valuable compounds from renewable sources. The reactions of PETNR and additional OYE enzymes, Thermophilic old yellow enzyme and Xenobiotic reductase A, with both natural coenzymes and a set of synthetic Nicotinamide Coenzyme Biomimetics (NCBs) are also characterised. The NCBs represent affordable and fast-reacting alternatives to the physiological coenzymes. Reactions with NCBS are also shown to proceed via a tunnelling mechanism and furthermore, that enhanced donor-acceptor sampling correlates with the faster reactivity seen with these compounds.
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Bamaga, Majid Abdullah. "Identification and characterisation of an Old Yellow Enzyme (OYE) - NamA - from Listeria monocytogenes." Thesis, Edinburgh Napier University, 2014. http://researchrepository.napier.ac.uk/Output/9831.

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The food-borne pathogene Listeria monocytogenes has been considered a significant threat to human health worldwide. It mainly infects individuals suffering insuffecint immunity such as pregnant women. During pregnancy, L. monocytogenes is capable of causing a serious damage to the mother and the fetus. It can spread to different organs including the placenta via adaptation to interacellular lifestyle. To maintain pregnancy, the levels of the hormones progesterone and β-estradiol increase and reduction in hormone levels was proposed to be associated with fetal death and abortion. The objectives of this project therefore were to investigate the role of pregnancy hormones on the growth and virulence of L. monocytogenes, and to identify bacterial genes with possible roles in binding to pregnancy hormones. It was obsereved that the growth of L. monocytogenes in the presence of progesterone under anaerobic condition was affected by the action of the hormone and the effect was dose/time-dependent of exposure as increasing concentrations showed greater effect on the bacterial growth. Interestingly, bacterial growth was restored within 24 h of exposure to the hormone. In parallel, a Tn917-LTV3 insertion library was constructed and a number of mutants isolated that had reduced growth in the presence of β-estradiol were identified. However, reduction in growth was not microbiologically significant. Furthermore, bioinformatics analysis was performed to identify listerial genes with possible role in hormones degradation. It was observed that L. monocytogenes encodes for a protein that is possibly involved in steroid degradation; therefore, gene expression and a clear-deletion mutant were performed to test this hypothesis. This revealed no significant role of this protein in the growth restoration observed in the presence of progesterone. Also, the deleted gene was investigated of its ability to reduce NADPH in the presence of a possible substrate (progesterone, β-estradiol). This showed that this gene could possess an enzymatic activity toward pregnancy hormones. An attempt to purify this protein for further investigation was performed and protein expression in a soluble form was unsuccessful. The findings presented in this thesis represent an important view when considering the relation between pregnancy hormones and L. monocytogenes; however, further investigations of hormone-degrading proteins from L. monocytogenes are needed. This knowledge may form the basis of a therapy to protect pregnant individuals.
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Chakrabarti, Ajoy Chuni Carleton University Dissertation Biology. "One-step conversion of cellulose to fructose using co-immobilized cellulase, B-glucosidase and glucose isomerase." Ottawa, 1988.

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au, s. averis@murdoch edu, and Susana M. E. Severgnini. "Isolation and characterisation of two chitinase and one novel glucanase genes for engineering plant defence against fungal pathogens." Murdoch University, 2006. http://wwwlib.murdoch.edu.au/adt/browse/view/adt-MU20071213.105659.

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Hydrolytic enzymes such as chitinases and glucanases are implicated in plant defense responses against fungal pathogens. These enzymes are responsible for the breakdown of chitin and glucan, two major components of the fungal cell walls. Genes encoding these enzymes have been used to genetically engineer plants to enhance their protection against fungal pathogens. Western Australia has over 4000 endemic plant species and a largely unknown fungal biota. Given that fungi possessing chitinases and glucanases with novel activities have been isolated in other parts of the world, we propose that fungi from Western Australian soils may possess novel biochemical/enzymatic activities. The aims of this research project were to isolate chitinolytic and glucanolytic fungi from soil and to clone the genes encoding for chitinase and glucanase enzymes. To achieve these aims, fungi with activity against chitin and glucan were isolated, the activity quantified by colorimetric and inhibition assays and gene fragments with homology to known chitinase and glucanase genes were isolated and their sequences determined. Soil fungi were isolated from five locations in and around the Perth Metropolitan area of Western Australia with the use of a medium containing Rose Bengal that eliminates all actinomycetes and most bacteria and reduces the growth of fast growing mold colonies. Forty-one isolates were obtained by this method. Twenty four chitinolytic and glucanolytic fungal isolates were identified by growing them on chitin-containing media to select for those species that utilised chitin/glucan as a carbon source. These were assayed for production of exo- and endochitinolytic and glucanolytic enzymes. Enzyme activity was compared between crude and dialysed supernatants. Exochitinase activity was determined in the supernatants of 4-day old fungal cultures by the release of p-nitrophenol from p-nitrophenyl-N-acetyl-â-D glucosaminide. The supernatants were measured for endochitinase activity determined by the reduction of turbidity of suspensions of colloidal chitin. Glucanase activity was determined by release of reducing sugar (glucose) from laminarin. Supernatants from eleven of the twenty four isolates showed significant levels of enzyme activity. Eleven isolates were assayed for activity against purified cell walls of phytopathogenic fungi. Activity was determined by measuring reducing sugars in the fungal supernatants against cell wall preparations of six economically important plant pathogens. Chitinolytic activity was detected in seven isolates against cell wall preparations of Botrytis cinerea and Rhizoctonia solani, in four isolates against Fusarium solani and Sclerotinia sclerotium; in five isolates against Ascochyta faba and in six isolates against Leptosphaeria maculans. Similarly glucanolytic activity was detected in eight isolates against B. cinerea, in seven against R. solani, in two against F. solani, in three against S. sclerotium and A. faba and in one against L. maculans. The supernatants derived from the isolates were used in a bioassay to determine growth inhibition against live B. cinerea spores by measuring turbidity reduction. Growth inhibition was measured against a control (B. cinerea, grown in medium with no added supernatant). Boiled supernatant did not inhibit the growth of B. cinerea spores but there was 100% inhibition by the crude supernatant from ten of the twenty four isolates. Similarly, supernatants were used to assess growth inhibition against live mycelia cultures of F. solani and S. sclerotium. Growth inhibition of F solani ranged from 9- 59%, boiled and crude supernatants respectively whilst growth inhibition of S. sclerotium ranged from 46-75%, boiled and crude supernatants respectively. Two partial chitinase genes from the soil filamentous ungus Trichoderma asperellum,(ChiA and ChiB) and a novel glucanase gene from the filamentous fungus Aspergillus (Glu1) were cloned. ChiA, was 639 bp long, encoding 191 amino acids with identity to other chitinase genes. Two highly conserved regions, characteristic of glycosyl hydrolases from family 18, were present. ChiB, was 887 bp long and encoded a 293 amino acid sequence that was closely related to an endochitinase gene from the filamentous fungus Trichoderma asperellum. The two highly conserved regions corresponding to the substrate binding and active sites that characterise the glycosyl hydrolases from family 18, also found in ChiA, were found in this gene. Glu1 was 2844 bp long and encoded a 948 amino acid sequence that shared high identity with a â-1, 3-glucanase from the filamentous fungus Aspergillus oryzae. The sequence contained conserved regions found in glycosyl hydrolases from family 17 that encode for substrate binding, N-terminal sequences and putative asparagine linked glycosylation sites. The partial putative sequence ChiA is probably a pseudogene because it has two inframe stop codons. However, once the entire sequence of ChiB is known, both ChiB and the novel glucanase gene Glu1 could be useful contenders for engineering resistance in crop plants.
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Chen, Xianwen. "PROFILING THE SUBSTRATE SPECIFICITY OF PROTEIN TYROSINE PHOSPHATASES BY COMBINATORIAL LIBRARY SCREENING." The Ohio State University, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=osu1315341322.

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Schümperli, Michael. "The system of biotransformations : multi-enzyme reaction engineering for one-pot synthesis of vicinal diols /." Zürich : ETH, 2008. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=17692.

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Sinelnikova, Natalia. "Synthesis of new inhibitors of human homogentisate 1,2-dioxygenase, one of the enzymes, involved in tyrosine metabolic pathway in humans." Thesis, Université Laval, 2006. http://www.theses.ulaval.ca/2006/23593/23593.pdf.

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Chang, Xiangning. "Short term sublethal studies in rats exposed to nickel subsulfide and nickel ore : effects on oxidative damage, antioxidant and detoxicating enzymes /." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp03/MQ55491.pdf.

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Anderson, Mattias. "Amine Transaminases in Multi-Step One-Pot Reactions." Doctoral thesis, KTH, Industriell bioteknologi, 2017. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-199646.

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Amine transaminases are enzymes that catalyze the mild and selective formation of primary amines, which are useful building blocks for biologically active compounds and natural products. In order to make the production of these kinds of compounds more efficient from both a practical and an environmental point of view, amine transaminases were incorporated into multi-step one-pot reactions. With this kind of methodology there is no need for isolation of intermediates, and thus unnecessary work-up steps can be omitted and formation of waste is prevented. Amine transaminases were successfully combined with other enzymes for multi-step synthesis of valuable products: With ketoreductases all four diastereomers of a 1,3-amino alcohol could be obtained, and the use of a lipase allowed for the synthesis of natural products in the form of capsaicinoids. Amine transaminases were also successfully combined with metal catalysts based on palladium or copper. This methodology allowed for the amination of alcohols and the synthesis of chiral amines such as the pharmaceutical compound Rivastigmine. These examples show that the use of amine transaminases in multi-step one-pot reactions is possible, and hopefully this concept can be further developed and applied to make industrial processes more sustainable and efficient in the future.

QC 20170113

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Döbber, Johannes [Verfasser], Martina [Gutachter] Pohl, and Vlada B. [Gutachter] Urlacher. "Fusion tag-based immobilization methods for the one-step purification and immobilization of enzymes / Johannes Döbber ; Gutachter: Martina Pohl, Vlada B. Urlacher." Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2018. http://d-nb.info/1163449865/34.

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Books on the topic "OYE Enzymes"

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Kelley, William Donald. One answer to cancer: Reviewed after 32 years, 1967-1999 : with cancer cure suppressed. Winfield, Kan: College of Metabolic Medicine, 1998.

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One answer to cancer: Reviewed after 30 years, 1967-1997 : the metabolic approach to the successful resolution of malignancy. Mineral Wells, TX: Cancer Coalition, 1997.

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Busacca, Maurizio, and Roberto Paladini. Collaboration Age. Venice: Fondazione Università Ca’ Foscari, 2020. http://dx.doi.org/10.30687/978-88-6969-424-0.

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Recently, public policies of urban regeneration have intensified and multiplied. They are being promoted with the aim to start social and economic dynamics within the local context which is subject to intervention. From the empirical analysis, we realise that such activities are mainly implemented by three subjects or by mixed coalitions (public institutions, actors of the third sector and companies). Within them, each player is moved by a multiplicity of interests and goals that go beyond their own nature – public interest, market and mutualism – and tend to redefine themselves, thus becoming hybrid forms of production of value (social, economic, cultural). By studying a number Italian and Catalan cases, this essay deals with the theory that, under specific conditions and configurations, a collaborative direction – of organization, production and design – would give life to successful procedures, even without the identification of a one-best-way. The collaboration is not simply a choice of operation, but a real production method which mobilises social resources to create hybrid solutions – between state, market and society – to complex issues that could not be faced solely with the use of the rationale of action of one among the three actors. In this framework, the systems of relations and interactions between players and shared capital become an essential condition for the success of every initiative of urban redevelopment, or failure thereof. Such initiatives are brought to life by the strategic role of individuals who foster connections as well as the dissemination of non-redundant information between social networks, and collective and individual actors which would otherwise be separated and barely able to communicate and collaborate with each other. In addition to the functions carried out by knowledge brokers, that have been extensively described in organisational studies and economic sociology, the aforementioned figures act as real social enzymes, that is to say, they handle the available information and function as catalysts of social processes of production of knowledge. Moreover, they increase the reaction speed, working on mechanisms which control the spontaneity.
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Deegan, Patrick. Porphyria. Edited by Patrick Davey and David Sprigings. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199568741.003.0179.

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This chapter discusses six diseases caused by inborn errors of metabolism affecting the biosynthesis of haem. Haem is a tetracyclic metal-binding compound involved in oxygen transport (in haemoglobin and myoglobin) and redox reactions (e.g. in the cytochrome P450 system). Each of these conditions is caused by a single gene defect in one of the enzymes involved in the biosynthesis of haem. Inheritance is usually autosomal dominant with incomplete penetrance. The enzyme defect results in disease, not as a result of deficiency of the reaction product, but as a result of accumulation of precursors. Early, soluble precursors, 5-aminolaevulinic acid, and porphobilinogen (not porphyrins as such) are neurotoxic and, when present in great excess, as occurs when flux through the haem synthetic pathway is increased in response to particular medications or hormones, lead to acute neurovisceral crises. Later cyclical precursors (porphyrins) in the pathway are also water soluble and excreted in urine, but are susceptible to activation by electromagnetic radiation in the visible spectrum and are converted to free-radical metabolites that cause pain, inflammation, and tissue damage in the skin. The final haem precursors (also porphyrins) are hydrophobic and excreted in the bile and faeces and are also activated by light to toxic metabolites.
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A, Ali Elvis, ed. Natural remedies & supplements: The all-in-one guide to herbs, vitamins, minerals, enzymes, amino acids, fats, herbs ... Niagara Falls, NY: AGES Publications, 2000.

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Waldek, Stephen. Fabry disease. Edited by Neil Turner. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199592548.003.0335_update_001.

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Fabry disease is a rare X-linked disorder of glycosphingolipid metabolism caused by a deficiency of the lysosomal acid hydrolase enzyme, alpha-galactosidase A. The resulting accumulation of substrate, mostly globotriaosylceramide, leads to a progressive, multiorgan disease affecting predominantly the kidneys, skin, heart, and nervous system. It is one of over 50 lysosomal storage diseases. It is typically diagnosed in young men after many years of ‘acral pain’ syndrome, when the diagnosis is made through identification of characteristic abnormalities of skin, kidney or heart, or of other organs. Renal failure has been a common outcome. Females may also develop manifestations, usually later in life. Renal biopsy shows vacuoles/deposits in podocytes and other renal cell types with progressive scarring. The diagnosis can be made by measuring enzyme levels in men, or by genetic testing. This latter is the more reliable test in women. Fabry disease can now be treated where affordable by regular (every 2 weeks) intravenous infusions of recombinant preparations of the deficient enzyme. These are burdensome and expensive, but are transforming the outlook for the condition.
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Dierdorf, Stephen F. Porphyria. Edited by Matthew D. McEvoy and Cory M. Furse. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780190226459.003.0026.

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Heme, and iron containing compound that forms the nonprotein portion of hemoglobin, is essential to life. Heme synthesis requires eight enzymatic steps, and a deficiency in any one of the eight enzymes can lead to the accumulation of potentially toxic intermediates. Some forms of porphyria may be asymptomatic until the patient receives a triggering agent, and acute porphyrias can also be difficult to diagnose because of the nonspecific clinical features. The most serious of the clinical manifestations is severe neurologic dysfunction. An attack can be triggered by medications administered during the perioperative period, and failure to act promptly can result in mortality rates as high as 5%.
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Hendriksz, Christian J., and Francois Karstens. Mucopolysaccharidosis in Adults. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0054.

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There are 8 different types of diseases of the mucopolysaccharides, each caused by a deficiency in one of 10 different enzymes involved in the degradation of glycosaminoglycans (GAGs). Partially degraded GAGs accumulate within the lysosomes of many different cell types and lead to clinical symptoms and excretion of large amounts of GAGs in the urine. Heritability is autosomal recessive except for MPS type II, which is X-linked. The disorders are chronic and progressive and, although the specific types all have their individual features, they share an abundance of clinical similarities. All involve the musculoskeletal, the cardiovascular, the pulmonary and the central nervous system.
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Poll-The, Bwee Tien, Ronald J. A. Wanders, and Hans R. Waterham. Peroxisomal Disorders. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0062.

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Peroxisomal disorders represent a group of disorders in which there is an impairment in one or more peroxisomal functions. Clinically, a dysfunction of peroxisomes results in most cases in neurologic symptoms of varying extent ranging from severe neurologic symptoms in children to late-onset disease in adults. In most peroxisomal disorders there is ocular and hearing involvement in combination with a multitude of other clinical manifestations. The peroxisomal disorders are subdivided into two major groups: (1) the peroxisome biogenesis disorders (PBDs), and (2) the single peroxisome enzyme deficiencies. The PBD group comprises the Zellweger spectrum disorders (ZSDs) and rhizomelic chondrodysplasia punctate type 1 (RCDP1) whereas the single peroxisomal enzyme deficiency group contains several different disorders including X-linked adrenoleukodystrophy as the most frequent disorder. Laboratory diagnosis of a peroxisomal disorder involves a variety of different biochemical assays in blood and urine, and should be followed up by detailed biochemical and celbiological studies in cultured fibroblasts including complementation analysis. Prenatal diagnosis is possible either by biochemical testing or by molecular analysis.
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Geracioti, Thomas D., Jeffrey R. Strawn, and Matthew D. Wortman. Mechanisms of Action in the Pharmacology of PTSD. Edited by Israel Liberzon and Kerry J. Ressler. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190215422.003.0020.

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This chapter reviews medications currently available for PTSD in the context of their mechanisms of action, pathophysiological relevance, and clinical efficacy data. It systematically reviews aminergic mechanisms in PTSD pharmacology, including commonly used serotonin and norepinephrine agents, selective reuptake inhibitors and receptors drugs, as well as dopaminergic agents and psychostimulants. It also discusses the use of anticonvusants and antianxiety agents that modulate GABAergic and glutamatergic signaling, such as carbamazepine, VPA, benzodiazepines, gabapentine, and others. It also reviews other clinically available agents as well as HPA axis-modulating compounds, both for treatment and secondary prevention of PTSD. It concludes with the suggestion that clinical selection of one or more of these medications for PTSD should be based on individual patient considerations, including target symptoms, PTSD subtype, post-traumatic interval, comorbidities, genotypes for CYP450 enzymes, and genetic polymorphisms of clinical relevance.
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Book chapters on the topic "OYE Enzymes"

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Varfolomeev, Sergey, Bella Grigorenko, Sofya Lushchekina, Patrick Masson, Galina Mahaeva, and Alexander Nemuchin. "Human cholinesterases." In ORGANOPHOSPHORUS NEUROTOXINS, 69–126. ru: Publishing Center RIOR, 2020. http://dx.doi.org/10.29039/21_069-126.

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The work is devoted to modeling the elementary stages of the hydrolysis reaction in the active site of enzymes belonging to the class of cholinesterases — acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). The study allowed to describe at the molecular level the effect of the polymorphic modification of BChE, causing serious physiolog ical consequences. Cholinesterase plays a crucial role in the human body. AChE is one of the key enzymes of the central nervous system, and BChE performs protective functions in the body. According to the results of calculations using the combined method of quantum and molecular mechanics (KM/MM), the mechanism of the hydrolysis of the native acetylcholine substrate in the AChE active center was detailed. For a series of ester substrates, a method for estimation of dependence of the enzyme reactivity on the structure of the substrate has been developed. The mechanism of hydrolysis of the muscle relaxant of succininylcholine BChE and the effect of the Asp70Gly polymorph on it were studied. Using various computer simulation methods, the stability of the enzyme-substrate complex of two enzyme variants with succinylcholine was studied.
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Varfolomeev, Sergey, Bella Grigorenko, Sofya Lushchekina, and Alexander Nemuchin. "Human cholinesterases." In Organophosphorous Neurotoxins, 63–120. ru: Publishing Center RIOR, 2020. http://dx.doi.org/10.29039/chapter_5e4132b5f22366.15634219.

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The work is devoted to modeling the elementary stages of the hydrolysis reaction in the active site of enzymes belonging to the class of cholinesterases — acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). The study allowed to describe at the molecular level the effect of the polymorphic modification of BChE, causing serious physiolog ical consequences. Cholinesterase plays a crucial role in the human body. AChE is one of the key enzymes of the central nervous system, and BChE performs protective functions in the body. According to the results of calculations using the combined method of quantum and molecular mechanics (KM/MM), the mechanism of the hydrolysis of the native acetylcholine substrate in the AChE active center was detailed. For a series of ester substrates, a method for estimation of dependence of the enzyme reactivity on the structure of the substrate has been developed. The mechanism of hydrolysis of the muscle relaxant of succininylcholine BChE and the effect of the Asp70Gly polymorph on it were studied. Using various computer simulation methods, the stability of the enzyme-substrate complex of two enzyme variants with succinylcholine was studied.
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Efremenko, Elena, Il'ya Lyagin, and Aslanli Aslanli. "Enzyme-based nanocomplexes and their construction for detoxification of organophosphorus compounds." In ORGANOPHOSPHORUS NEUROTOXINS, 361–79. ru: Publishing Center RIOR, 2020. http://dx.doi.org/10.29039/53_361-379.

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Organophosphorus compounds (OPC) pose a serious threat, as they can have a neurotoxic effect on the human body, even death. In this regard, the main challenge of our times is the search for effective ways of degradation of OPC. In this case, preference is given to biological methods of OPC detoxification, which do not require the use of harsh chemical methods of degradation and are suitable for in vivo use. One of such methods is the use of biocatalysts — enzymes capable of hydrolyzing OPC. To stabilize the activity of enzymes, as well as leveling a possible immune response from the body when used in vivo, various modification methods are used, such as nanocapsulation, the formation of enzymepolyelectrolyte complexes, immobilization of the enzyme on various functionalized carriers, etc. The chapter contains the information on examples of such biocatalysts, discussion of their advantages and disadvantages.
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Hausmann, Rudolf. "One Gene — One Enzyme." In To Grasp the Essence of Life, 44–55. Dordrecht: Springer Netherlands, 2002. http://dx.doi.org/10.1007/978-94-017-3540-7_3.

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Schomburg, Dietmar, and Dörte Stephan. "3alpha-Hydroxy-5beta-androstan-17-one 3alpha-dehydrogenase." In Enzyme Handbook 10, 6–8. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-57756-7_3.

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Schomburg, Dietmar, and Dörte Stephan. "2,4-Dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucosyltransferase." In Enzyme Handbook 12, 909–11. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61117-9_202.

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Naegeli, Hanspeter. "Molecular Recognition Strategies I: One Enzyme-One Substrate Motifs." In Mechanisms of DNA Damage Recognition in Mammalian Cells, 71–92. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4684-6468-9_4.

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Mateo, Cesar, Benevides C. C. Pessela, Valeria Grazu, Rodrigo Torres, Fernando López-Gallego, Jose M. Guisan, and Roberto Fernandez-Lafuente. "One-Step Purification, Immobilization, and Stabilization of Poly-Histidine-Tagged Enzymes Using Metal Chelate-Epoxy Supports." In Immobilization of Enzymes and Cells, 117–28. Totowa, NJ: Humana Press, 2006. http://dx.doi.org/10.1007/978-1-59745-053-9_11.

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Baronas, Romas, Feliksas Ivanauskas, and Juozas Kulys. "One-Layer Multi-Enzyme Models of Biosensors." In Springer Series on Chemical Sensors and Biosensors, 113–37. Dordrecht: Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-3243-0_7.

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Guisan, Jose M., Fernando López-Gallego, Juan M. Bolivar, Javier Rocha-Martín, and Gloria Fernandez-Lorente. "One-Point Covalent Immobilization of Enzymes on Glyoxyl Agarose with Minimal Physico-Chemical Modification: Immobilized “Native Enzymes”." In Methods in Molecular Biology, 83–92. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0215-7_4.

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Conference papers on the topic "OYE Enzymes"

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Wallace, Robert W., E. Ann Tallant, and Lynn M. Brumley. "POSSIBLE ROLE FOR THE CA2+-DEPENDENT PROTEASE (CALPAIN I) AS AN IRREVERSIBLE ACTIVATOR OF CA2+/CALMODULIN-MEDIATED REACTIONS IN THE HUMAN PLATELET." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644528.

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Calmodulin (CaM)-binding proteins have been identified in human platelets using Western blotting techniques and 125I-CaM. Ten proteins of 245, 225. 175, 150, 90. 82(2), 60 and 41(2) kilodaltons (kDa) bind 125I-CaM in a Ca2+-dependent manner; the binding is blocked by both trifluoperazine and nonradiolabeled CaM. The 225 and 90 kDa proteins are labeled by antisera against myosin light chain kinase (MLCK); the 60 kDa and one of the 82 kDa proteins have been identified as the CaM-dependent phosphatase (calcineurin) and caldesmon. The other proteins are presumed to be other Ca2+/CaM regulated enzymes and proteins which may be important in platelet function. Most of the CaM-binding proteins are degraded upon addition of Ca2+ to a platelet homogenate; the degradation may be blocked by either EGTA, leupeptin or N-ethylmaleimide which suggests that the degradation is due to a Ca2+-dependent protease. Activation of intact platelets under conditions which promote platelet aggregation (i.e. stirring with extracellular Ca2+) also results in limited proteolysis of CaM-binding proteins including those labeled with anti sera against MLCK and the phosphatase. In vitro studies utilizing purified phosphatase and calpain I indicate that the phosphatase is irreversibly activated upon Ca2+-dependent proteolysis. The proteolytically-activated enzyme is insensitive to either Ca2+ or Ca2+/CaM; in addition, its activity in the absence of Ca2+ is even greater than the activity of the unproteolyzed enzyme in the presence of Ca2+ and CaM. Proteolytic stimulation of the phosphatase is accompanied by degradation of the 60 kDa subunit of the enzyme (subunit A) to 56, 52 and 45 kDa fragments, sequentially; proteolysis results in the loss of CaM binding to the enzyme. These results suggest that the Ca2+-dependent protease may have a physiological role in platelet activation as an irreversible activator of Ca2+/ CaM-dependent reactions. Supported by NIH grant HL29766.
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Polster, J., W. Hobel, A. Papperger, and H. L. Schmidt. "Fundamentals Of Enzyme Substrate Determinations By Fiber Optics Spectroscopy." In OE/FIBERS '89, edited by Robert A. Lieberman and Marek T. Wlodarczyk. SPIE, 1990. http://dx.doi.org/10.1117/12.963197.

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Kuzikova, Irina, Irina Kuzikova, Vera Safronova, Vera Safronova, Nadezda Medvedeva, and Nadezda Medvedeva. "IMPACT OF NONYLPHENOL ON THE PHYSIOLOGICAL ACTIVITY OF FUNGI FROM THE COASTAL AREA OF THE GULF OF FINLAND." In Managing risks to coastal regions and communities in a changing world. Academus Publishing, 2017. http://dx.doi.org/10.21610/conferencearticle_58b431765a62a.

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Nonylphenol (NP) is the most abundant environmental estrogen listed as one of the priority hazardous substances in the Water Framework Directive (EC 2000) and the priority pollutant of Baltic Sea (HELCOM 2010). The present study aims to compare the effects of technical nonylphenol (tNP) on the cellulase, amylase and protease activity of the terrestrial fungal strains played a significant role in aquatic ecosystems due to their high adaptive capacity and a large range of functional activity. The study also attempts to understand the mechanisms behind the varying sensitivity of the terrestrial fungi to tNP. The fungal strains were isolated from the bottom sediments of the coastal area of the eastern part of the Gulf of Finland. The terrestrial fungi were identified based on their morphological characteristics and nucleotide sequence analysis of internal transcribed space region. One reason for significant differences in sensitivity to the toxicant studied among the fungi is the change in the fungal cell permeability, in particular in cell membrane permeability, induced by NP. Environmentally relevant concentrations of tNP cause significant changes in activity of hydrolytic enzymes in the terrestrial fungi Aspergillus tubingensis, Penicillium expansum, Penicillium glabrum, and Cadophora fastigiata involved in organic matter degradation in bottom sediments. There can be increasing or decreasing trend, depending on both the type of enzyme and the tNP concentration. The revealed changes may disrupt the destructive processes in bottom sediments, as well as succession and stability of microbial communities functioning in the aquatic environment. It was found that tNP contributes to the activation of proteolytic enzymes, considered as potential fungal virulence factors. This may lead to emergence fungal strains with enhanced virulence in aquatic microbiocenoses. The investigations of the physiological responses of terrestrial fungi under nonylphenol will be important for biochemical processes dynamics and their environmental consequences evaluation.
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Kuzikova, Irina, Irina Kuzikova, Vera Safronova, Vera Safronova, Nadezda Medvedeva, and Nadezda Medvedeva. "IMPACT OF NONYLPHENOL ON THE PHYSIOLOGICAL ACTIVITY OF FUNGI FROM THE COASTAL AREA OF THE GULF OF FINLAND." In Managing risks to coastal regions and communities in a changing world. Academus Publishing, 2017. http://dx.doi.org/10.31519/conferencearticle_5b1b93c5890b52.86067390.

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Nonylphenol (NP) is the most abundant environmental estrogen listed as one of the priority hazardous substances in the Water Framework Directive (EC 2000) and the priority pollutant of Baltic Sea (HELCOM 2010). The present study aims to compare the effects of technical nonylphenol (tNP) on the cellulase, amylase and protease activity of the terrestrial fungal strains played a significant role in aquatic ecosystems due to their high adaptive capacity and a large range of functional activity. The study also attempts to understand the mechanisms behind the varying sensitivity of the terrestrial fungi to tNP. The fungal strains were isolated from the bottom sediments of the coastal area of the eastern part of the Gulf of Finland. The terrestrial fungi were identified based on their morphological characteristics and nucleotide sequence analysis of internal transcribed space region. One reason for significant differences in sensitivity to the toxicant studied among the fungi is the change in the fungal cell permeability, in particular in cell membrane permeability, induced by NP. Environmentally relevant concentrations of tNP cause significant changes in activity of hydrolytic enzymes in the terrestrial fungi Aspergillus tubingensis, Penicillium expansum, Penicillium glabrum, and Cadophora fastigiata involved in organic matter degradation in bottom sediments. There can be increasing or decreasing trend, depending on both the type of enzyme and the tNP concentration. The revealed changes may disrupt the destructive processes in bottom sediments, as well as succession and stability of microbial communities functioning in the aquatic environment. It was found that tNP contributes to the activation of proteolytic enzymes, considered as potential fungal virulence factors. This may lead to emergence fungal strains with enhanced virulence in aquatic microbiocenoses. The investigations of the physiological responses of terrestrial fungi under nonylphenol will be important for biochemical processes dynamics and their environmental consequences evaluation.
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Otter, ALbin, Nicole Robert, Keiko Sujino, Piers Nash, Grant McFadden, Ronald J. Jackson, and Monica M. Palcic. "OPTIMIZATION OF A MULTI-ENZYME ONE POT SYNTHESIS BY 1H-NMR." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.758.

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Asakura, S., N. Yoshida, and M. Matsuda. "MONOCLONAL ANTIBODIES AGAINST THROHBIN-ANTITHROMBIN III COMPLEX: EPITOPE SPECIFICITY AND EFFECT ON THROMBIN-ANTITHROMBIN III INTERACTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643673.

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Among monoclonal antibodies (MCA´s) raised against human thrombin (T)-antithrombin m (AT) complex (TAT), two MCA´s designated as JITAT-16 and 17 with high affinity, Kd = 4.6nMand 4.1 nfi, respectively, were selected and characterized for specificity and functions. Their respective immunoglobulin subclasses are IgGi and IgG2a, and epitopes were found to be different from each Dther as shown by crisscross inhibition experiments. Immuno-alotting of normal plasma and serum electrophoresed on non-SDS aolyacrylamide gel showed that these antibodies reacted with normal serum but not with plasma. This was verified by an anzyme-linked differential antibody immunosorbent assay using aither one of the MCA´s as the first antibody and the other MCA labeled with peroxidase as the second one. By immunoblotting after SDS-PAGE, we found that both antibodies reacted with TAT, nut not with its respective nascent constituent, AT or T. However, they reacted with reactive site-cleaved AT (or thrombin-nodified AT, ATM) and also a complex of AT with activated factor K (Xa-AT). These results indicate that both of these antibodies recognize enzyme-treated forms of AT, including AT molecules :omplexed with enzymes reversibly or irreversibly as well as ATM. Jpon incubation of T with AT in the presence of JITAT-16, T activity remained nearly unchanged and formation of irreversible rAT did not proceed as expected. Moreover, AT was preferentially :onverted to ATM. When JITAT-16 was added after completion of FAT formation, however, neither recovery of T activity nor generation of ATM was observed. These findings were not obtained vhen JITAT-17 had been substituted for JITAT-16. These data suggest that JITAT-16 may have converted AT from an inhibitor to a substrate for T after having recognized a possible intermediate reversible complex of AT with T. Undoubtedly, in the presence of a polyclonal antibody against AT, neither TAT formation nor ATM neneration was observed at all. The mechanism of the unique Function of JITAT-16 has not been fully clarified as yet, but this antibody seems to give us new information on the kinetic study of TAT formation and ATM generation when AT was allowed to react with enzymes.
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Kojima, T., M. Tanimoto, T. Kamiya, Y. Obata, K. Kurachi, and H. Saito. "ANALYSIS OF FACTOR IX GENE IN NORMAL SUBJECTS AND HEMOPHILIA B PATIENTS IN JAPAN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644077.

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We have examined DNA samples from 25 hemophilia B patients (21 B- patients, 2 BR patients and 2 B+ patients) and 51 normal subjects with molecular probes (pHFIX and 2 genomic fragments). By structural gene analysis, 4 out of 7 patients who developed anti-factor IX antibodies were detected to have gross factor IX gene deletion. Although these four patients showed normal pattern of HPRT gene detected by pCDHPRT, the gene deletions were found to expand more than 34kb including with entire factor IX exons. Quantitative Southern blot analysis of factor IX gene of the patient's family members indicated that the gene deletion was inherited in one family, establishing the carrier status of 2 aunts, 2 cousins and one sister. The 'de novo' mutation of factor IX gene was also established in 2 families. Three patients with anti-factor IX antibodies and 17 patients without antibody to factor IX had normal pattern of factor IX gene by several restriction enzyme digestions. Analysis of factor IX gene of three patients with anti-factor IX antibodies and two B+ patients are now underway to detect the unique gene defects which may be responsible for the disease Phenotypes. Common RFLPs in factor IX gene were studied in normal Japanese subjects. More than 80 X chromosomes were analysed with BamHI, Ddel, MspI, TaqI or XmnI digestion, followed by hybridization with pHFIX. RFLPs produced by these enzymes were found to be uncommon or possibly absent in normal Japanese subjects. These results imply that racial differences in the frequency of gene polymorphisms should be seriously considered before initiating the gene counseling by the genetic probes.
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Liu, Jia, Jingang Shi, Jian Li, and Xingzhong Yuan. "Effects of Surfactants Tween 80 and Rhamnolipid on the Extracellular Enzymes Amylase, Protease, CMCase and Xylanase of One Strain." In 2011 International Conference on Computer Distributed Control and Intelligent Environmental Monitoring (CDCIEM). IEEE, 2011. http://dx.doi.org/10.1109/cdciem.2011.481.

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Nayeen, Md Junayed, Khushbu Shah, Aamod Dekhne, Changwon Ning, Carrie O'Connor, Jade M. Katinas, Jennifer Wong, et al. "Abstract 811: Multi-targeted inhibitors of mitochondrial one-carbon metabolism and cytosolicde novopurine synthesis enzymes as anti-tumor agents." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-811.

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Nayeen, Md Junayed, Khushbu Shah, Aamod Dekhne, Changwon Ning, Carrie O'Connor, Jade M. Katinas, Jennifer Wong, et al. "Abstract 811: Multi-targeted inhibitors of mitochondrial one-carbon metabolism and cytosolicde novopurine synthesis enzymes as anti-tumor agents." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-811.

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Reports on the topic "OYE Enzymes"

1

Kassem, Hala A., David J. Fryauff, Magdi G. Shehata, and Bahira M. El Sawaf. Enzyme Polymorphism and Genetic Variability of One Colonized and Several Field Populations of Phlebotomus papatasi (Diptera: Psychodidae). Fort Belvoir, VA: Defense Technical Information Center, January 1993. http://dx.doi.org/10.21236/ada266319.

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