Relevant bibliographies by topics / Substrate specificity

Academic literature on the topic 'Substrate specificity'

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Published: 4 June 2021
Last updated: 11 March 2023

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Journal articles on the topic "Substrate specificity"

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Koudelakova, Tana, Eva Chovancova, Jan Brezovsky, Marta Monincova, Andrea Fortova, Jiri Jarkovsky, and Jiri Damborsky. "Substrate specificity of haloalkane dehalogenases." Biochemical Journal 435, no. 2 (March 29, 2011): 345–54. http://dx.doi.org/10.1042/bj20101405.

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An enzyme's substrate specificity is one of its most important characteristics. The quantitative comparison of broad-specificity enzymes requires the selection of a homogenous set of substrates for experimental testing, determination of substrate-specificity data and analysis using multivariate statistics. We describe a systematic analysis of the substrate specificities of nine wild-type and four engineered haloalkane dehalogenases. The enzymes were characterized experimentally using a set of 30 substrates selected using statistical experimental design from a set of nearly 200 halogenated compounds. Analysis of the activity data showed that the most universally useful substrates in the assessment of haloalkane dehalogenase activity are 1-bromobutane, 1-iodopropane, 1-iodobutane, 1,2-dibromoethane and 4-bromobutanenitrile. Functional relationships among the enzymes were explored using principal component analysis. Analysis of the untransformed specific activity data revealed that the overall activity of wild-type haloalkane dehalogenases decreases in the following order: LinB~DbjA>DhlA~DhaA~DbeA~DmbA>DatA~DmbC~DrbA. After transforming the data, we were able to classify haloalkane dehalogenases into four SSGs (substrate-specificity groups). These functional groups are clearly distinct from the evolutionary subfamilies, suggesting that phylogenetic analysis cannot be used to predict the substrate specificity of individual haloalkane dehalogenases. Structural and functional comparisons of wild-type and mutant enzymes revealed that the architecture of the active site and the main access tunnel significantly influences the substrate specificity of these enzymes, but is not its only determinant. The identification of other structural determinants of the substrate specificity remains a challenge for further research on haloalkane dehalogenases.
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Wilson, Charles, and David A. Agard. "Engineering substrate specificity." Current Opinion in Structural Biology 1, no. 4 (August 1991): 617–23. http://dx.doi.org/10.1016/s0959-440x(05)80086-7.

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Wong, W. "Specifying Substrate Specificity." Science Signaling 6, no. 280 (June 18, 2013): ec140-ec140. http://dx.doi.org/10.1126/scisignal.2004423.

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Houlston, C. E., M. Cummings, H. Lindsay, S. Pradhan, and R. L. P. Adams. "DNA substrate specificity of pea DNA methylase." Biochemical Journal 293, no. 3 (August 1, 1993): 617–24. http://dx.doi.org/10.1042/bj2930617.

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DNA methylase, present in low-salt extracts of nuclei prepared from Pisum sativum shoot tips, methylates model DNA substrates containing CNG trinucleotides or CI dinucleotides only. The binding to the hemimethylated trinucleotide substrates is very much stronger and more persistent than the binding to the unmethylated substrates or to the hemimethylated dinucleotide substrate. When the DNA concentration is limiting, the rate of methyl-group transfer with the hemimethylated CNG substrate is much greater than that with the unmethylated CNG. However, the Vmax. is similar for the two CNG substrates. On fractionation using Q-Sepharose, two peaks of activity are seen with different relative activities using the di- and trinucleotide substrates. The relative activity with these substrates changes during purification, during plant growth and on heating at 35 degrees C as well, indicating that more than one enzyme or more than one form of the enzyme may be present.
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LINDSTAD, I. Rune, Peter KÖLL, and John S. McKINLEY-McKEE. "Substrate specificity of sheep liver sorbitol dehydrogenase." Biochemical Journal 330, no. 1 (February 15, 1998): 479–87. http://dx.doi.org/10.1042/bj3300479.

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The substrate specificity of sheep liver sorbitol dehydrogenase has been studied by steady-state kinetics over the range pH 7-10. Sorbitol dehydrogenase stereo-selectively catalyses the reversible NAD-linked oxidation of various polyols and other secondary alcohols into their corresponding ketones. The kinetic constants are given for various novel polyol substrates, including L-glucitol, L-mannitol, L-altritol, D-altritol, D-iditol and eight heptitols, as well as for many aliphatic and aromatic alcohols. The maximum velocities (kcat) and the substrate specificity-constants (kcat/Km) are positively correlated with increasing pH. The enzyme-catalysed reactions occur by a compulsory ordered kinetic mechanism with the coenzyme as the first, or leading, substrate. With many substrates, the rate-limiting step for the overall reaction is the enzyme-NADH product dissociation. However, with several substrates there is a transition to a mechanism with partial rate-limitation at the ternary complex level, especially at low pH. The kinetic data enable the elucidation of new empirical rules for the substrate specificity of sorbitol dehydrogenase. The specificity-constants for polyol oxidation vary as a function of substrate configuration with D-xylo > d-ribo > L-xylo > d-lyxo ≈ l-arabino > D-arabino > l-lyxo. Catalytic activity with a polyol or an aromatic substrate and various 1-deoxy derivatives thereof varies with -CH2OH >-CH2NH2 >-CH2OCH3 ≈-CH3. The presence of a hydroxyl group at each of the remaining chiral centres of a polyol, apart from the reactive C2, is also nonessential for productive ternary complex formation and catalysis. A predominantly nonpolar enzymic epitope appears to constitute an important structural determinant for the substrate specificity of sorbitol dehydrogenase. The existence of two distinct substrate binding regions in the enzyme active site, along with that of the catalytic zinc, is suggested to account for the lack of stereospecificity at C2 in some polyols.
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Ananvoranich, Sirinart, and Jean-Pierre Perreault. "Substrate Specificity ofδRibozyme Cleavage." Journal of Biological Chemistry 273, no. 21 (May 22, 1998): 13182–88. http://dx.doi.org/10.1074/jbc.273.21.13182.

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Crans, Debbie C., and George M. Whitesides. "Glycerol kinase: substrate specificity." Journal of the American Chemical Society 107, no. 24 (November 1985): 7008–18. http://dx.doi.org/10.1021/ja00310a044.

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Capecchi, John T., and Gordon Marc Loudon. "Substrate specificity of pyroglutamylaminopeptidase." Journal of Medicinal Chemistry 28, no. 1 (January 1985): 140–43. http://dx.doi.org/10.1021/jm00379a024.

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Ratnikov, Boris I., Piotr Cieplak, Albert G. Remacle, Elise Nguyen, and Jeffrey W. Smith. "Quantitative profiling of protease specificity." PLOS Computational Biology 17, no. 2 (February 22, 2021): e1008101. http://dx.doi.org/10.1371/journal.pcbi.1008101.

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Proteases are an important class of enzymes, whose activity is central to many physiologic and pathologic processes. Detailed knowledge of protease specificity is key to understanding their function. Although many methods have been developed to profile specificities of proteases, few have the diversity and quantitative grasp necessary to fully define specificity of a protease, both in terms of substrate numbers and their catalytic efficiencies. We have developed a concept of “selectome”; the set of substrate amino acid sequences that uniquely represent the specificity of a protease. We applied it to two closely related members of the Matrixin family–MMP-2 and MMP-9 by using substrate phage display coupled with Next Generation Sequencing and information theory-based data analysis. We have also derived a quantitative measure of substrate specificity, which accounts for both the number of substrates and their relative catalytic efficiencies. Using these advances greatly facilitates elucidation of substrate selectivity between closely related members of a protease family. The study also provides insight into the degree to which the catalytic cleft defines substrate recognition, thus providing basis for overcoming two of the major challenges in the field of proteolysis: 1) development of highly selective activity probes for studying proteases with overlapping specificities, and 2) distinguishing targeted proteolysis from bystander proteolytic events.
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Hatanaka, Akikazu, Tadahiko Kajiwara, Kenji Matsui, and Hiromitsu Toyota. "Substrate Specificity of Tea Leaf Hydroperoxide Lyase." Zeitschrift für Naturforschung C 47, no. 9-10 (October 1, 1992): 677–79. http://dx.doi.org/10.1515/znc-1992-9-1006.

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Substrate specificity of tea leaf fatty acid hydroperoxide lyase was systematically investigated using an entire series of ω 6-(5)-hydroperoxy-C14-C24 dienoic and trienoic acids as substrates. Unexpectedly, the hydroperoxides of C22 but not natural substrates, i.e., those of C18, showed the highest reactivities for the lyase. The reactivities of the hydroperoxides of trienoic acids were always four to ten times higher than those of the dienoic acids.
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Dissertations / Theses on the topic "Substrate specificity"

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Babcock, Gwen. "Maize β-glucosidase substrate specificity and natural substrates." Thesis, Virginia Tech, 1993. http://hdl.handle.net/10919/45360.

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Babcock, Gwen. "Maize [beta]-glucosidase substrate specificity and natural substrates /." This resource online, 1993. http://scholar.lib.vt.edu/theses/available/etd-10312009-020235/.

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Allison, Timothy Murray. "Substrate specificity and mutational studies of KDO8PS." Thesis, University of Canterbury. Chemistry, 2012. http://hdl.handle.net/10092/6684.

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The enzyme 3-deoxy-D-manno-octulosonate 8-phosphate synthase (KDO8PS) catalyses the stereospecific aldol-like condensation between phosphoenolpyruvate (PEP) and the five-carbon sugar D-arabinose 5-phosphate (A5P). This is the first biosynthetic step in the formation of 3-deoxy-D-manno-octulosonate (KDO), an essential lipopolysaccharide component of all Gram-negative bacteria. KDO8PS is evolutionarily related to the shikimate pathway enzyme 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAH7PS), which catalyses a similar condensation reaction between PEP and the four-carbon sugar D-erythrose 4-phosphate (E4P), in the first step of the shikimate pathway to aromatic compounds in plants and microorganisms. As well as being a one-carbon shorter substrate, E4P has the opposite C2-OH configuration to A5P. While there are both metal-dependent and metal-independent forms of KDO8PS, in contrast, all DAH7PS are metal-dependent enzymes. Little is understood about the key sequence features that distinguish KDO8PS and DAH7PS. These features, particularly those that contribute to A5P or E4P binding, are thought to be responsible for the differences in substrate specificity between the two enzymes. This thesis describes the functional and structural studies of KDO8PS mutants to examine the roles of these residues, using the metal-dependent KDO8PS from Acidithiobacillus ferrooxidans and the metal-independent KDO8PS from Neisseria meningitidis. In Chapter 2 an extensive KDO8PS and DAH7PS sequence analysis is presented. The results, which identify sequence conservation in both enzymes, are discussed in the context of the (β/α)8 TIM-barrel structure. Some of the differences in conservation between the two enzymes were highlighted as being obvious in having a role or contributing to the different substrate selection preferences of the two enzymes, such as an extended β7α7 loop in KDO8PS, and motif differences on the β2α2 and β4α4 loops. A similar analysis was also used to compare metal-dependent and metal-independent KDO8PSs, and it was found the two forms differ in the conservation of only three residues. Chapter 3 describes the characterisation of A. ferrooxidans KDO8PS (AfeKDO8PS) and investigates aspects of metal dependency in KDO8PS. The enzyme was found to be metal dependent, and like all other KDO8PS enzymes, to possess a tetrameric quaternary structure, and display tight substrate specificity. The β8α8 loop was found to have a critical role in binding and positioning the substrates, and AfeKDO8PS could not be engineered to be a metal-independent enzyme. The role of the KDO8PS-conserved KANRS motif, present on the β2α2 loop and one of the main contributors to the A5P binding site, is probed in Chapter 4. Individual residues of the motif were mutated to investigate function, and the motif was converted to the equivalent motif found in DAH7PS (KPRS). It was found that the Lys plays a critical role in enzymatic catalysis, and is likely intimately involved in the enzyme mechanism. The Asn residue of the motif in KDO8PS was found to be an important contributor to KDO8PS stereospecificity. The work described in Chapter 5 investigates the role of the β7α7 loop in KDO8PS. This long active-site loop, which exists in a shorter version in DAH7PS, was found not to be essential for catalysis in KDO8PS, but was necessary for efficient catalysis. The two conserved residues on the loop provide interactions to A5P, but the presence of the extended loop as a whole was found to be most important for catalytic efficiency. In Chapter 6 a conserved residue on the re face of PEP is investigated. In KDO8PS the residue is conserved as Asp, and in DAH7PS the same residue is conserved as a Glu. Mutational analysis found that in KDO8PS the Asp residue appears to be important for enzyme activity but unimportant for PEP binding. Mutating this Asp in KDO8PS to Glu was accommodated by KDO8PS, but it was found its introduction could potentially be optimised by coupling the change with mutation to other conserved differences. In KDO8PS, one of the interfaces between adjacent subunits in the tetrameric structure is partially composed of a conserved sequence motif, PAFLxR. In Chapter 7, the roles of the residues in this motif are explored. The Arg of the motif was found to be important for A5P binding. The equivalent (and also conserved) motif in DAH7PS is GARNxQ, and mutation of residues in the KDO8PS motif to the equivalent residues in DAH7PS was tolerated by KDO8PS, but negatively impacted upon the enzyme kinetic parameters. The sequence features investigated in the other chapters were combined with those to the subunit interface to create a DAH7PS-like protein. This extensively engineered protein lost all KDO8PS activity, but nor did it gain DAH7PS activity. Lastly, in Chapter 8 the results from all chapters are reviewed and ideas are discussed for advancing the research presented in this thesis.
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Chappell, Lucy. "Engineering the substrate specificity of galactose oxidase." Thesis, University of Leeds, 2013. http://etheses.whiterose.ac.uk/5741/.

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Biocatalysis, the use of enzymes to catalyse the generation of specific chemicals, has a number of advantages including high specificity, lower energy requirements and greater sustainability over an equivalent chemical process. Several methods exist for optimisation of enzymes for use in industrial processes, including introduction of mutations to generate libraries of variants which are then screened for the desired properties, such as stability or substrate specificity. Galactose oxidase catalyses the oxidation of primary alcohols to the corresponding aldehyde, with concomitant reduction of dioxygen to hydrogen peroxide. It has already been developed for use in a range of biotechnological processes and is an ideal candidate for further development due to features including high stability, a surface exposed active site displaying broad substrate specificity, and an autocatalytically-generated cofactor. Research presented in this thesis investigates the effect on activity towards a range of alternative substrates of mutations at selected active site residues with the aim of expanding the biotechnological potential of galactose oxidase. Libraries of variants were designed and generated using high quality oligonucleotides constructed using trimer phosphoramidites. Screening assays used by other groups were optimised by varying different components. These assays were then used to identify a number of variants displaying enhanced activity towards D-arabinose, D-glucose, D-xylose or glycerol. A selection of these variants were then further characterised in order to understand the biochemical basis of the altered activities and determine some of the conditions required for potential industrial application of the variants. The most exciting results include identification of a variant displaying higher levels of activity towards glycerol than towards the native substrate D-galactose; determination of the position of oxidation of D-arabinose at the C-4 hydroxyl; and the observation that mutation of Phe194 significantly affects binding of D-glucose in the active site.
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Ahn, Jinwoo. "DNA polymerase ? : Control of substrate specificity and fidelity /." The Ohio State University, 1997. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487943610785207.

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Björnberg, Olof. "Viral dUTPases recombinant expression, purification, and substrate specificity /." [Lund] : Dept. of Biochemistry, Lund University, Sweden, 1995. http://books.google.com/books?id=hvZqAAAAMAAJ.

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Lee, Nicholas Yong Kyu. "Characterizing substrate specificity and affinity in zebrafish deiodinases." Thesis, Boston University, 2012. https://hdl.handle.net/2144/12472.

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Thesis (M.A.)--Boston University PLEASE NOTE: Boston University Libraries did not receive an Authorization To Manage form for this thesis or dissertation. It is therefore not openly accessible, though it may be available by request. If you are the author or principal advisor of this work and would like to request open access for it, please contact us at open-help@bu.edu. Thank you.
Thyroid hormones are important for development and growth and their metabolism is mediated by a special class of enzymes called deiodinases. In this study, we cloned zebrafish deiodinases 1-3 (sequences from GenBank) and transfected them into mammalian cells. A special sequence called the selenocysteine insertion sequence was also cloned and transfected to express zebrafish deiodinases at high levels. Deiodination activity from the cloned zebrafish deiodinases indicated that GenBank sequences encode functional enzymes with the same specificity as human deiodinases. Zebrafish D1 was highly effective in catalyzing the outer ring deiodination of rT3. Zebrafish D2 catalyzed the outer ring deiodination of all tested substrates but showed no inner ring deiodination activity. Zebrafish D3 only catalyzed the inner ring deiodination of T3 into T2. We also observed that all zebrafish deiodinases required the SECIS element for enzyme activity. Furthermore, we demonstrated that the optimal temperature for zebrafish D3 catalyzed T3 deiodination is at room temperature instead of previously thought 28.5° C. The dramatic difference in zebrafish D3 (23.0° C compared to human D3 at 37.0° C) illustrated that there is an important difference between species. Finally, we demonstrated that zebrafish D3 has high affinity for T3 through Lineweaver Burk analysis and showed that the Km value of zebrafish D3 is in the low nanomolar range similar to human D3. Together with high substrate specificity for T3, we demonstrated that"zebrafish D3 is the primary inactiviator of T3 in zebrafish. We concluded that zebrafish deiodinase sequences in GenBank encode functional enzymes with high affinity and specificity but require the presence of the SECIS element for enzyme activity. Furthermore, we concluded that there is an important difference in optimal temperature between mammalian and zebrafish D3.
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Townsend, Andrew Paul. "Nitrogen mustards as tools in determining methyltransferase substrate specificity." Thesis, University of Nottingham, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.517857.

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Bolt, Amanda Helen. "Probing the substrate specificity and stereoselectivity of an aldolase." Thesis, University of Leeds, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.507677.

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Cohen, H. "Investigating and engineering the substrate specificity of DNA methyltransferases." Thesis, University of Cambridge, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.597811.

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DNA methyltransferases catalyse the transfer of methyl groups from the cofactor S-adenosyl-L-methionine to a target base (adenine or cytosine) within a cognate recognition sequence. I have studied cofactor binding, DNA specificity and the role of conserved amino acid motifs in the cytosine C5 methyltransferase M.HaeIII. By measuring the competitive inhibition of methylation by a series of cofactor analogues, each modified at a single position, the importance of each functional group for cofactor binding to M.HaeIII was probed. The functional significance of amino-acid residues in M.HaeIII was investigated using in vitro compartmentalisation (IVC), an activity-based selection method. IVC was used to obtain active variants of M.HaeIII from libraries diversified at conserved motifs in the catalytic and DNA binding domains. M.HaeIII modifies the central cytosine of the sequence (5’-GGCC-3’). Using bisulphite sequencing, cytosines in a variety of other sequence contexts were found to be methylated at lower levels by M.HaeIII both in vivo and in vitro. IVC was then used to select mutant enzymes with an improved ability to methylate the non-canonical site AGCC.
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Books on the topic "Substrate specificity"

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J, Chapman Peter, and United States. Environmental Protection Agency, eds. Physiological properties and substrate specificity of a pentachlorophenol-degrading Pseudomonas species. [Washington, D.C.?: Environmental Protection Agency], 1994.

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Physiological properties and substrate specificity of a pentachlorophenol-degrading Pseudomonas species. [Washington, D.C.?: Environmental Protection Agency], 1994.

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Sheps, Jonathan Ahab. Specificity and diversity: Substrate recognition in the hemolysin transporter of escherichia coli. 1996.

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Oblong, John Erich. Subunit characterization and substrate specificity of the chloroplast soluble proteolytic processing enzyme. 1992.

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Provencher, Louis R. *. A survey of the substrate specificity L-lactate dehydrogenase from "Bacillus Stear". 1988.

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Ruckpaul, Klaus. Cytochrome P-450 Dependent Biotransformation of Endogenous Substrates (Frontiers in Biotransformation). Vch Pub, 1991.

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Hansson, Lars O. Redesign of Substrate Specificity of Glutathione Transferase and Glutathione Reductase: Enzyme Engineering by Directed Mutagenesis, Phage-Display Selection ... Summaries of Uppsala Dissertations, 450). Uppsala Universitet, 1999.

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Zalatoris, Jeffrey Joseph. Development and partial structural characterization of a recombinant inhibitor of pepsin from Ascaris. 1999.

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Book chapters on the topic "Substrate specificity"

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Keil, Borivoj. "Essential Substrate Residues for Action of Endopeptidases." In Specificity of Proteolysis, 43–228. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-48380-6_5.

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Jenner, Matthew. "Substrate Specificity of Ketosynthase Domains Part III: Elongation-Based Substrate Specificity." In Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases, 131–54. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-32723-5_6.

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Lin, Y. Y., Charles Yi, Julie Olsen, and Anthony H. C. Huang. "Substrate Specificity of Plant Lipases." In The Metabolism, Structure, and Function of Plant Lipids, 341–43. Boston, MA: Springer New York, 1987. http://dx.doi.org/10.1007/978-1-4684-5263-1_61.

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Plapp, Bryce V., David W. Green, Hong-Wei Sun, Doo-Hong Park, and Keehyuk Kim. "Substrate Specificity of Alcohol Dehydrogenases." In Advances in Experimental Medicine and Biology, 391–400. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2904-0_41.

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Page, M. I. "The specificity of enzyme—substrate interactions." In Accuracy in Molecular Processes, 37–66. Dordrecht: Springer Netherlands, 1986. http://dx.doi.org/10.1007/978-94-009-4097-0_3.

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Cook, Shelley M., and David L. Daleke. "Substrate Specificity of the Aminophospholipid Flippase." In Transmembrane Dynamics of Lipids, 199–223. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9781118120118.ch10.

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Yoshinaka, Yoshiyuki, Iyoko Katoh, and Kohei Oda. "Retroviral Protease: Substrate Specificity and Inhibitors." In Retroviral Proteases, 31–39. London: Macmillan Education UK, 1990. http://dx.doi.org/10.1007/978-1-349-11907-3_5.

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Ernst, Beat, and Reinhold Oehrlein. "Substrate and donor specificity of glycosyl transferases." In Glycotechnology, 81–90. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-5257-4_7.

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Madison, Edwin L. "Substrate Specificity of Tissue Type Plasminogen Activator." In Advances in Experimental Medicine and Biology, 109–21. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-5391-5_11.

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Thiem, J. "Substrate Specificity and Synthetic Use of Glycosyltransferases." In Leucocyte Trafficking, 75–94. Berlin, Heidelberg: Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-662-05397-3_5.

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Conference papers on the topic "Substrate specificity"

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Alexeev, C. S., K. M. Polyakov, G. G. Sivets, T. N. Safonova, and S. N. Mikhailov. "Substrate specificity of E. coli uridine phosphorylase. Evidence of high-syn conformation of substrate." In XVIth Symposium on Chemistry of Nucleic Acid Components. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2014. http://dx.doi.org/10.1135/css201414213.

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Chen, Jeff. "The evolution of substrate specificity in poplar beta-ketoacyl-coA synthases." In ASPB PLANT BIOLOGY 2020. USA: ASPB, 2020. http://dx.doi.org/10.46678/pb.20.1052967.

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Robb, Charlene, Timothy Ferguson, Kelly Moffitt, Darragh McCafferty, and Brian Walker. "Examining the specificity of an internally quenched fluorogenic substrate for neutrophil elastase." In ERS International Congress 2017 abstracts. European Respiratory Society, 2017. http://dx.doi.org/10.1183/1393003.congress-2017.pa4000.

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Howell, P. L., Y. Lobsanov, F. Vallee, P. Yip, A. Imberty, T. Yoshida, K. Karaveg, et al. "STRUCTURAL BASIS FOR CATALYSIS AND SUBSTRATE SPECIFICITY OF CLASS I ALPHA1,2-MANNOSIDASES." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.418.

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Nayak, (D) Deepak Ranjan, and Siva Umapathy. "Surface Enhanced Raman Spectroscopic Studies using Galvanic Nano-buds." In JSAP-OSA Joint Symposia. Washington, D.C.: Optica Publishing Group, 2017. http://dx.doi.org/10.1364/jsap.2017.6a_a410_1.

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Raman spectroscopy has attracted considerable attention in analytical measurements but lacks the sensitivity due to low scattering cross section. However, surface enhanced Raman spectroscopy (SERS) has brought both specificity and sensitivity on the same platform. The specificity in SERS technique is largely owing to the unique vibrational frequency of the molecules giving rise to finger print like spectra. Sensitivity, however, is tailored from electric field enhancement in plasmonic nanostructure and fabrication of nanostructure for a specific wavelength. Control of size, shape of suitable plasmonic material and there by excitation of localized surface plasmon resonance of a metal nanoparticle or nanostructured surface is essential in understanding the fundamental process of SERS. Optical property of the surrounding medium has profound effect on the plasmonic response of the metal nanoparticles. Such type of interaction in SERS substrates, associated to plasmon-substrate interaction, brings out simple yet effective method to fabricate SERS substrate.
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Tsai, Shih-Chong, Kuen-Jou Wei, Chia-Chi Lin, and Chu-His Fan. "The mutation at H254 of organophosphorus hydrolase increases the substrate specificity of profenofos." In 2009 IEEE International Conference on Bioinformatics and Biomedicine Workshop, BIBMW. IEEE, 2009. http://dx.doi.org/10.1109/bibmw.2009.5332087.

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"Features of the substrate specificity of a novel AP endonuclease from Pyrococcus furiosus." In Bioinformatics of Genome Regulation and Structure/Systems Biology (BGRS/SB-2022) :. Institute of Cytology and Genetics, the Siberian Branch of the Russian Academy of Sciences, 2022. http://dx.doi.org/10.18699/sbb-2022-573.

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Basavapathruni, Aravind, Jodi Gureasko, Margaret Porter Scott, P. Ann Boriack-Sjodin, Timothy J. Wigle, Thomas V. Riera, and Robert A. Copeland. "Abstract 104: ATF7IP does not alter the substrate specificity of the lysine methyltransferase SETDB1." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-104.

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Awai, Takako, and Hiroyuki Hori. "Broad substrate RNA specificity of Trm1 (tRNA (m22G26) methyltransferase) from Aquifex aeolicus." In 2008 International Symposium on Micro-NanoMechatronics and Human Science (MHS). IEEE, 2008. http://dx.doi.org/10.1109/mhs.2008.4752442.

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Bachor, Remigiusz, Aneta Paluch, Wioletta Rut, Marcin Darg, and Zbigniew Szewczuk. "On-bead Analysis of Substrate Specificity of Caspases using Peptide Modified by Qauternary AmmoniumGroup as Ionization Enhancers." In 35th European Peptide Symposium. Prompt Scientific Publishing, 2018. http://dx.doi.org/10.17952/35eps.2018.212.

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Reports on the topic "Substrate specificity"

1

Anderson, C. W., M. A. Connelly, H. Zhang, J. A. Sipley, S. P. Lees-Miller, L. G. Lintott, Kazuyasu Sakaguchi, and E. Appella. The human DNA-activated protein kinase, DNA-PK: Substrate specificity. Office of Scientific and Technical Information (OSTI), November 1994. http://dx.doi.org/10.2172/113929.

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Chen, Wilfred. Tuning Biphenyl Dioxygenase for Extended Substrate Specificity and Enhanced Activity. Fort Belvoir, VA: Defense Technical Information Center, September 1997. http://dx.doi.org/10.21236/ada335315.

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