Relevant bibliographies by topics / Enzymes - Kinetics

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Academic literature on the topic 'Enzymes - Kinetics'

Author: Grafiati
Published: 4 June 2021
Last updated: 6 September 2023

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Journal articles on the topic "Enzymes - Kinetics"

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Guerrieri, Antonio, Rosanna Ciriello, Giuliana Bianco, Francesca De Gennaro, and Silvio Frascaro. "Allosteric Enzyme-Based Biosensors—Kinetic Behaviours of Immobilised L-Lysine-α-Oxidase from Trichoderma viride: pH Influence and Allosteric Properties." Biosensors 10, no. 10 (October 17, 2020): 145. http://dx.doi.org/10.3390/bios10100145.

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The present study describes the kinetics of L-lysine-α-oxidase (LO) from Trichoderma viride immobilised by co-crosslinking onto the surface of a Pt electrode. The resulting amperometric biosensor was able to analyse L-lysine, thus permitting a simple but thorough study of the kinetics of the immobilised enzyme. The kinetic study evidenced that LO behaves in an allosteric fashion and that cooperativity is strongly pH-dependent. Not less important, experimental evidence shows that cooperativity is also dependent on substrate concentration at high pH and behaves as predicted by the Monod-Wyman-Changeux model for allosteric enzymes. According to this model, the existence of two different conformational states of the enzyme was postulated, which differ in Lys species landing on LO to form the enzyme–substrate complex. Considerations about the influence of the peculiar LO kinetics on biosensor operations and extracorporeal reactor devices will be discussed as well. Not less important, the present study also shows the effectiveness of using immobilised enzymes and amperometric biosensors not only for substrate analysis, but also as a convenient tool for enzyme kinetic studies.
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Hochendoner, Philip, Curtis Ogle, and William H. Mather. "A queueing approach to multi-site enzyme kinetics." Interface Focus 4, no. 3 (June 6, 2014): 20130077. http://dx.doi.org/10.1098/rsfs.2013.0077.

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Multi-site enzymes, defined as where multiple substrate molecules can bind simultaneously to the same enzyme molecule, play a key role in a number of biological networks, with the Escherichia coli protease ClpXP a well-studied example. These enzymes can form a low latency ‘waiting line’ of substrate to the enzyme's catalytic core, such that the enzyme molecule can continue to collect substrate even when the catalytic core is occupied. To understand multi-site enzyme kinetics, we study a discrete stochastic model that includes a single catalytic core fed by a fixed number of substrate binding sites. A natural queueing systems analogy is found to provide substantial insight into the dynamics of the model. From this, we derive exact results for the probability distribution of the enzyme configuration and for the distribution of substrate departure times in the case of identical but distinguishable classes of substrate molecules. Comments are also provided for the case when different classes of substrate molecules are not processed identically.
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Pyne, N. J., M. E. Cooper, and M. D. Houslay. "Identification and characterization of both the cytosolic and particulate forms of cyclic GMP-stimulated cyclic AMP phosphodiesterase from rat liver." Biochemical Journal 234, no. 2 (March 1, 1986): 325–34. http://dx.doi.org/10.1042/bj2340325.

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Two enzymes displaying cyclic GMP-stimulated cyclic AMP phosphodiesterase activity were purified from rat liver to apparent homogeneity: a ‘particulate enzyme’ found as an integral membrane protein associated with the plasma membrane, and a ‘soluble’ enzyme found in the cytosol. The physical properties of these enzymes were very similar, being dimers of Mr 134,000, composed in each instance of two subunits of Mr = 66,000-67,000. Both enzymes showed similar kinetics for cyclic AMP hydrolysis. They are both high-affinity enzymes, with kinetic constants for the particulate enzyme of Km = 34 microM and Vmax. = 4.0 units/mg of protein and for the cytosolic enzyme Km = 40 microM and Vmax. = 4.8 units/mg of protein. In both instances hydrolysis of cyclic AMP appeared to show apparent positive co-operativity, with Hill coefficients (happ.) of 1.5 and 1.6 for the particulate and cytosolic enzymes respectively. However, in the presence of 2 microM-cyclic GMP, the hydrolysis of cyclic AMP obeyed Michaelis kinetics (happ. = 1) for both enzymes. The addition of micromolar concentrations of cyclic GMP had little effect on the Vmax. for cyclic AMP hydrolysis, but lowered the Km for cyclic AMP hydrolysis to around 20 microM in both cases. However, at low cyclic AMP substrate concentrations, cyclic GMP was a more potent activator of the particulate enzyme than was the soluble enzyme. The activity of these enzymes could be selectively inhibited by cis-16-palmitoleic acid and by arachidonic acid. In each instance, however, the hydrolysis of cyclic AMP became markedly more sensitive to such inhibition when low concentrations of cyclic GMP were present. Tryptic peptide maps of iodinated preparations of these two purified enzyme species showed that there was considerable homology between these two enzyme forms.
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Brooks, S. P. J. "Equilibrium enzymes in metabolic pathways." Biochemistry and Cell Biology 74, no. 3 (May 1, 1996): 411–16. http://dx.doi.org/10.1139/o96-044.

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It is commonly believed that certain reactions in a metabolic sequence may be at or close to equilibrium because of the large excess of catalytic capacity compared to the flux through these enzyme loci. Simple algebraic manipulations can show that the equilibrium and steady state conditions are mutually exclusive. However, solution of the complete reaction schemes for model "equilibrium" reactions shows that they can remain far from equilibrium even though the ratio of enzyme flux to steady state flux through the overall pathway is high. These calculations show that a reaction's proximity to equilibrium depends on the overall flux through the enzyme locus as well as on the kinetic parameters of the other enzymes in the pathway. Thus, combinations of kinetic parameters may exist that allow certain reactions to approach equilibrium but these conditions are not universal.Key words: equilibria, theoretical kinetics, metabolic control.
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Cornish-Bowden, Athel, and Jan-Hendrik S. Hofmeyr. "Enzymes in context: Kinetic characterization of enzymes for systems biology." Biochemist 27, no. 2 (April 1, 2005): 11–14. http://dx.doi.org/10.1042/bio02702011.

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The kinetic behaviour of enzymes is typically observed in conditions appropriate for studying questions of mechanism of action, but these are not necessarily the most appropriate for studying their physiological roles, because they are often too far from those that exist in the living organism. Enzymes therefore need to be studied with natural substrates in the presence of all of the other small molecules likely to affect the activity in vivo, including the reaction products, so that the reverse reaction is not artificially prohibited. As complete reversible rate equations are often unmanageably complicated, especially for cooperative kinetics, care needs to be taken in choosing simpler equations that preserve the properties that are relevant in physiological conditions.
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Raggi, A., and M. Ranieri-Raggi. "Regulatory properties of AMP deaminase isoenzymes from rabbit red muscle." Biochemical Journal 242, no. 3 (March 15, 1987): 875–79. http://dx.doi.org/10.1042/bj2420875.

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We examined the kinetic and regulatory properties of the two isoenzymes of red muscle AMP deaminase, forms A and B, corresponding respectively to the single isoenzymes present in the heart and white skeletal muscle. At the optimal pH value, 6.5, both enzymes show hyperbolic substrate-velocity curves and are inhibited by GTP, inducing sigmoid kinetics. An effect similar to that of GTP is exerted on form B by ATP, whereas form A is almost insensitive to this nucleotide. At pH 7.1 both enzymes follow sigmoid kinetics. ATP enhances the sigmoidicity of the substrate-velocity curve of form B, but it stimulates form A, reverting sigmoidal to hyperbolic kinetics shown by the enzyme at optimal pH. At pH 7.1, form A is also less sensitive to the inhibitory action of Pi and GTP. These results suggest that, owing to the presence of form A, AMP deamination occurs in red muscle also at moderate work intensity. A possible role of this process in counteracting the production of adenosine by 5′-nucleotidase is hypothesized.
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Dong, Jianshu. "On Catalytic Kinetics of Enzymes." Processes 9, no. 2 (January 30, 2021): 271. http://dx.doi.org/10.3390/pr9020271.

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Classical enzyme kinetic theories are summarized and linked with modern discoveries here. The sequential catalytic events along time axis by enzyme are analyzed at the molecular level, and by using master equations, this writing tries to connect the microscopic molecular behavior of enzyme to kinetic data (like velocity and catalytic coefficient k) obtained in experiment: 1/k = t equals to the sum of the times taken by the constituent individual steps. The relationships between catalytic coefficient k, catalytic rate or velocity, the amount of time taken by each step and physical or biochemical conditions of the system are discussed, and the perspective and hypothetic equations proposed here regarding diffusion, conformational change, chemical conversion, product release steps and the whole catalytic cycle provide an interpretation of previous experimental observations and can be testified by future experiments.
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Schnitzer, M. J., and S. M. Block. "Statistical Kinetics of Processive Enzymes." Cold Spring Harbor Symposia on Quantitative Biology 60 (January 1, 1995): 793–802. http://dx.doi.org/10.1101/sqb.1995.060.01.085.

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Ruppe, Alex, Kathryn Mains, and Jerome M. Fox. "A kinetic rationale for functional redundancy in fatty acid biosynthesis." Proceedings of the National Academy of Sciences 117, no. 38 (September 3, 2020): 23557–64. http://dx.doi.org/10.1073/pnas.2013924117.

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Cells build fatty acids with biocatalytic assembly lines in which a subset of enzymes often exhibit overlapping activities (e.g., two enzymes catalyze one or more identical reactions). Although the discrete enzymes that make up fatty acid pathways are well characterized, the importance of catalytic overlap between them is poorly understood. We developed a detailed kinetic model of the fatty acid synthase (FAS) ofEscherichia coliand paired that model with a fully reconstituted in vitro system to examine the capabilities afforded by functional redundancy in fatty acid synthesis. The model captures—and helps explain—the effects of experimental perturbations to FAS systems and provides a powerful tool for guiding experimental investigations of fatty acid assembly. Compositional analyses carried out in silico and in vitro indicate that FASs with multiple partially redundant enzymes enable tighter (i.e., more independent and/or broader range) control of distinct biochemical objectives—the total production, unsaturated fraction, and average length of fatty acids—than FASs with only a single multifunctional version of each enzyme (i.e., one enzyme with the catalytic capabilities of two partially redundant enzymes). Maximal production of unsaturated fatty acids, for example, requires a second dehydratase that is not essential for their synthesis. This work provides a kinetic, control-theoretic rationale for the inclusion of partially redundant enzymes in fatty acid pathways and supplies a valuable framework for carrying out detailed studies of FAS kinetics.
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Ovádi, J., P. Tompa, B. Vértessy, F. Orosz, T. Keleti, and G. R. Welch. "Transient-time analysis of substrate-channelling in interacting enzyme systems." Biochemical Journal 257, no. 1 (January 1, 1989): 187–90. http://dx.doi.org/10.1042/bj2570187.

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The kinetics of dynamically interacting enzyme systems is examined, in the light of increasing evidence attesting to the widespread occurrence of this mode of organization in vivo. The transient time, a key phenomenological parameter for the coupled reaction, is expressed as a function of the lifetime of the intermediate substrate. The relationships between the transient time and the pseudo-first-order rate constants for the coupled reaction by the complexed and uncomplexed enzyme species are indicative of the mechanism of intermediate transfer (‘channelling’). In a dynamically interacting enzyme system these kinetic parameters are composite functions of those for the processes catalysed by the complex and by the separated enzymes. The mathematical paradigm can be extended to a linear sequence of N coupled reactions catalysed by dynamically (pair-wise) interacting enzymes.
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Dissertations / Theses on the topic "Enzymes - Kinetics"

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Ekici, Özlem Doğan. "Design, synthesis, and evaluation of novel irreversible inhibitors for caspases." Available online, Georgia Institute of Technology, 2004:, 2003. http://etd.gatech.edu/theses/available/etd-04062004-164633/unrestricted/ekici%5Fozlem%5Fd%5F200312%5Fphd.pdf.

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Qian, Yuhui. "Study of Basic Wood Decay Mechanisms and Their Biotechnological Applications." Fogler Library, University of Maine, 2008. http://www.library.umaine.edu/theses/pdf/QianY2008.pdf.

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Moore, Robert Goodwin Douglas C. "Towards the understanding of complex biochemical systems the significance of global protein structure and thorough parametric analysis /." Auburn, Ala, 2009. http://hdl.handle.net/10415/1766.

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Ekici, Ozlem Dogan. "Design, synthesis, and evaluation of novel irreversible inhibitors for caspases." Diss., Georgia Institute of Technology, 2003. http://hdl.handle.net/1853/5333.

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Epstein, Todd Matthew. "Structural and kinetic studies of two enzymes catalyzing phospholipase A2 activity." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file 2.39 Mb., 186 p, 2006. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pqdiss&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&rft_dat=xri:pqdiss:3200538.

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Fisher, Oriana. "Subcloning, enzymatic characterization, and in silico docking of transglutaminase 2." Waltham, Mass. : Brandeis University, 2009. http://dcoll.brandeis.edu/handle/10192/23253.

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Åström, Nina. "NADH/NAD⁺ analogues and cyclodextrins in enzyme mimicking systems an experimental and computational investigation /." Lund : Organic Chemistry 1, Lund University, 1995. http://catalog.hathitrust.org/api/volumes/oclc/39781586.html.

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Baloyi, Thembekile Feonah. "Effects of exogenous fibrolytic enzymes on in vitro fermentation kinetics of forage and mixed." Thesis, Stellenbosch : Stellenbosch University, 2008. http://hdl.handle.net/10019.1/19895.

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Thesis (MScAgric)--Stellenbosch University, 2008.
ENGLISH ABSTRACT: Two in vitro experiments were conducted to evaluate the effect of exogenous fibrolytic enzyme application on dry matter (DM) and neutral detergent fibre (NDF) degradation and gas production (GP) of mature forages and forage-concentrate mixtures. The forages used in the first experiment were lucerne hay (LH), oat hay (OH) and wheat straw (WS). The same forages were used in the second experiment, but they were mixed with a concentrate feed to make three mixtures consisting of 80% (HC), 50% (MC) or 20% (LC) concentrate. The extracellular enzyme fraction (supernatant) of a fungal strain, ABO 374, was used as feed additive. The supernatant was used in a fresh (SU-ABO374) or lyophilized (CSIR-ABO374) form, the latter being reconstituted with water immediately before application. The liquid supernatants were applied to the incubation medium and not directly to the substrate, at a rate equivalent to 7.5 ml/kg feed DM. In the control treatments of both experiments, water was used instead of the liquid supernatants. For the DM and NDF degradability trials in both experiments, 500 mg forage samples were weighed into 50 x 50 mm dacron bags which were incubated anaerobically at 39ºC in 1.4L of a rumen liquid inoculated buffered medium in 2L fermentation jars. Bags from all treatments were removed after 2, 4, 8, 12, 24, 48, 72 and 96 h of incubation. For the gas production determinations, 500 mg of the respective substrate samples were weighed into 120 ml glass vials which were incubated for 96 h in 40 ml inoculated medium to which 0.5 ml of the respective enzyme solutions were added. Gas pressure was recorded manually with a digital pressure gauge after 2, 4, 8, 12, 24, 48, 72 and 96 h and pressure was converted to volume with a predetermined regression. The 96 h substrate residues were washed, dried, weighed and analyzed for NDF and OM. In both experiments the substrates differed in terms of DM and NDF degradability and gas production rates, but the enzyme treatments had no effect. The lack of response to enzyme application was ascribed to a number of factors, including the fact that enzyme application was into the incubation medium and not directly onto the substrates and also that no significant pre-incubation interaction time was allowed. The same preparations gave positive results in previous trials where they were applied directly onto the substrates and where a pre-incubation interaction time of 16 hours was allowed. (Key words: Exogenous enzymes, forages, concentrate based diets, DM and NDF degradation, gas production )
AFRIKAANSE OPSOMMING: Die invloed van eksogene fibrolitiese ensieme op in vitro fermentasiekinetika van ruvoer- en gemengde voersubstrate. Twee in vitro-experimente is uitgevoer om die invloed van eksogene fibrolitiese ensieme op droëmateriaal (DM) en neutraal-onoplosbare vesel (NDF) degradering en gasproduksie (GP) van volwasse ruvoersubstrate en ruvoer-kragvoermengsels te bepaal. Ruvoere in die eerste eksperiment was lusernhooi (LH), hawerhooi (HH) en koringstrooi (KS). Dieselfde ruvoere is in die tweede eksperiment gebruik, maar hulle is met ‘n kragvoer gemeng om drie mengsels te maak, bestaande uit 80% (HK), 50% (MK) of 20% (LK) kragvoer. Die ekstrasellulêre ensiemfraksie (supernatant) van ‘n fungiale stam, ABO 374, is as ‘n voertoedieningsmiddel gebruik. Die supernatant is is in ‘n vars (SU-ABO374) of gevriesdroogde (WNNR-ABO374) vorm gebruik, waar laasgenoemde onmiddellik voor toediening gerekonstitueer is. Die vloeistof-supernatante is nie direk op die substrate gevoeg nie, maar tot die inkubasiemedium gevoeg, teen ‘n hoeveelheid ekwivalent aan 7.5 ml/kg voer DM. In die kontrolebehandeling van beide eksperimente, is water in plaas van die vloeistofsupernatante gebruik. Vir die DM- en NDF-degraderingsproewe in beide eksperimente, is 500 mg van die onderskeie ruvoere in 50 x 50 mm dacronsakkies geweeg wat anaerobies by 39ºC geïnkubeer is in 1.4L van ‘n rumenvloeistof-geïnokkuleerde medium in 2L fermentasieflesse. Vir alle behandelings is sakkies na 2, 4, 8, 12, 24, 48, 72 en 96 h inkubasie verwyder. Vir gasproduksiebepalings is 500 mg van die onderskeie substraatmonsters in 120 ml glasbotteltjies geweeg en vir 96 h in 40 ml geïnokkuleerde medium geïnkubeer waarin 0.5 ml van die onderskeie ensiemoplossings gevoeg is. Gasdruk is na 2, 4, 8, 12, 24, 48, 72 en 96 h bepaal met behulp van ‘n digitale drukmeter en druk is met behulp van ‘n voorafbepaalde regressie na volume omgeskakel. Die 96 h substraatresidue is gewas, gedroog, geweeg en ontleed vir NDF en OM. In beide eksperimente het die substrate verskil ten opsigte van DM- en NDF-degradeerbaarheid en gasproduksietempo’s, maar die ensiembehandelings het geen invloed gehad nie. Die gebrek aan respons is aan verskeie faktore toegeskryf, insluitend die feit dat ensiemtoediening in die inkubasiemedium toegedien is en nie direk op die substrate nie, asook die feit dat daar nie ‘n noemenswaardige pre-inkubasie interaksietyd toegalaat is nie. Dieselfde ensiempreparate het positiewe resultate gelewer in vorige proewe waar dit direk op die substraat toegedien is en waar ‘n pre-inkubasie interaksietyd van 16 ure toegelaat is. (Sleutelwoorde: Eksogene ensieme, ruvoere, kragvoerdiëte, DM- en NDF-degradering, gasproduksie)
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Finnigan, William John Andrew. "The exploitation of thermophiles and their enzymes for the construction of multistep enzyme reactions from characterised enzyme parts." Thesis, University of Exeter, 2016. http://hdl.handle.net/10871/27323.

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Biocatalysis is a field rapidly expanding to meet a demand for green and sustainable chemical processes. As the use of enzymes for synthetic chemistry becomes more common, the construction of multistep enzyme reactions is likely to become more prominent providing excellent cost and productivity benefits. However, the design and optimisation of multistep reactions can be challenging. An enzyme toolbox of well-characterised enzyme parts is critical for the design of novel multistep reactions. Furthermore, while whole-cell biocatalysis offers an excellent platform for multistep reactions, we are limited to the use of mesophilic host organisms such as Escherichia coli. The development of a thermophilic host organism would offer a powerful tool allowing whole-cell biocatalysis at elevated temperatures. This study aimed to investigate the construction of a multistep enzyme reaction from well-characterised enzyme parts, consisting of an esterase, a carboxylic acid reductase and an alcohol dehydrogenase. A novel thermostable esterase Af-Est2 was characterised both biochemically and structurally. The enzyme shows exceptional stability making it attractive for industrial biocatalysis, and features what is likely a structural or regulatory CoA molecule tightly bound near the active site. Five carboxylic acid reductases (CARs) taken from across the known CAR family were thoroughly characterised. Kinetic analysis of these enzymes with various substrates shows they have a broad but similar substrate specificity and that electron rich acids are favoured. The characterisation of these CARs seeks to provide specifications for their use as a biocatalyst. The use of isolated enzymes was investigated as an alternative to whole-cell biocatalysis for the multistep reaction. Additional enzymes for the regeneration of cofactors and removal of by-products were included, resulting in a seven enzyme reaction. Using characterised enzyme parts, a mechanistic mathematical model was constructed to aid in the understanding and optimisation of the reaction, demonstrating the power of this approach. Thermus thermophilus was identified as a promising candidate for use as a thermophilic host organism for whole-cell biocatalysis. Synthetic biology parts including a BioBricks vector, custom ribosome binding sites and characterised promoters were developed for this purpose. The expression of enzymes to complete the multistep enzyme reaction in T. thermophilus was successful, but native T. thermophilus enzymes prevented the biotransformation from being completed. In summary, this work makes a number of contributions to the enzyme toolbox of well-characterised enzymes, and investigates their combination into a multistep enzyme reaction both in vitro and in vivo using a novel thermophilic host organism.
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Väljamäe, Priit. "The kinetics of cellulose enzymatic hydrolysis : Implications of the synergism between enzymes." Doctoral thesis, Uppsala University, Department of Biochemistry, 2002. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-3120.

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The hydrolysis kinetics of bacterial cellulose and its derivatives by Trichoderma reesei cellulases was studied. The cellulose surface erosion model was introduced to explain the gradual and strong retardation of the rate of enzymatic hydrolysis of cellulose. This model identifies the decrease in apparent processivity of cellobiohydrolases during the hydrolysis as a major contributor to the decreased rates. Both enzyme-related (non-productive binding) and substrate-related (erosion of cellulose surface) processes contribute to the decrease in apparent processivity. Furthermore, the surface erosion model allows, in addition to conventional endo-exo synergism, the possibility for different modes of synergistic action between cellulases. The second mode of synergism operates in parallel with the conventional one and was found to be predominant in the hydrolysis of more crystalline celluloses and also in the synergistic action of two cellobiohydrolases.

A mechanism of substrate inhibition in synergistic hydrolysis of bacterial cellulose was proposed whereby the inhibition is a result of surface dilution of reaction components (bound cellobiohydrolase and cellulose chain ends) at lower enzyme-to-substrate ratios.

The inhibition of cellulases by the hydrolysis product, cellobiose, was found to be strongly dependent on the nature of the substrate. The hydrolysis of a low molecular weight model substrate, such as para-nitrophenyl cellobioside, by cellobiohydrolase I is strongly inhibited by cellobiose with a competitive inhibition constant around 20 μM, whereas the hydrolysis of cellulose is more resistant to inhibition with an apparent inhibition constant around 1.5 mM for cellobiose.

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Books on the topic "Enzymes - Kinetics"

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Cornish-Bowden, Athel. Enzyme kinetics. Oxford: IRL Press, 1988.

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Kuby, Stephen Allen. Enzyme catalysis, kinetics, and substrate binding. Boca Raton: CRC Press, 1991.

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Enzyme kinetics: From diastase to multi-enzyme systems. Cambridge: Cambridge University Press, 1994.

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Punekar, N. S. ENZYMES: Catalysis, Kinetics and Mechanisms. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-0785-0.

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Kinetics for the life sciences: Receptors, transmitters, and catalysts. Cambridge: Cambridge University Press, 1995.

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Enzyme kinetics: Principles and methods. 2nd ed. Weinheim (Federal Republic of Germany): WILEY-VCH, 2005.

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W, Wharton Christopher, ed. Enzyme kinetics. Oxford: IRL Press, 1988.

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1930-, Cleland W. W., ed. Enzyme kinetics and mechanism. New York: Taylor & Francis Group, 2007.

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Enzyme kinetics and mechanisms. Dordrecht: Kluwer Academic Pub., 2002.

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Leskovac, Vladimir. Comprehensive enzyme kinetics. New York: Kluwer Academic/Plenum Pub., 2003.

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Book chapters on the topic "Enzymes - Kinetics"

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Bergethon, Peter R. "Kinetics: Enzymes and Electrons." In The Physical Basis of Biochemistry, 498–515. New York, NY: Springer New York, 1998. http://dx.doi.org/10.1007/978-1-4757-2963-4_32.

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Punekar, N. S. "Enzymes: Historical Aspects." In ENZYMES: Catalysis, Kinetics and Mechanisms, 5–13. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-0785-0_2.

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James, Margaret O. "Enzyme Kinetics of Conjugating Enzymes: PAPS Sulfotransferase." In Methods in Molecular Biology, 187–201. Totowa, NJ: Humana Press, 2014. http://dx.doi.org/10.1007/978-1-62703-758-7_10.

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Punekar, N. S. "Chemical Kinetics: Fundamentals." In ENZYMES: Catalysis, Kinetics and Mechanisms, 85–96. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-0785-0_9.

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Punekar, N. S. "pH Studies with Enzymes." In ENZYMES: Catalysis, Kinetics and Mechanisms, 267–74. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-0785-0_24.

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Burgot, Jean-Louis. "Enzymes—Kinetics of Enzymatic Reactions." In Thermodynamics in Bioenergetics, 203–11. Boca Raton, FL : CRC Press, 2019. | “A science publishers book.”: CRC Press, 2019. http://dx.doi.org/10.1201/9781351034227-30.

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Punekar, N. S. "Enzymes: Their Place in Biology." In ENZYMES: Catalysis, Kinetics and Mechanisms, 3–4. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-0785-0_1.

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Punekar, N. S. "Exploiting Enzymes: Technology and Applications." In ENZYMES: Catalysis, Kinetics and Mechanisms, 15–31. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-0785-0_3.

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Khade, S. M., S. K. Srivastava, L. H. Kamble, and J. Srivastava. "Food Enzymes: General Properties and Kinetics." In Novel Food Grade Enzymes, 1–15. Singapore: Springer Nature Singapore, 2022. http://dx.doi.org/10.1007/978-981-19-1288-7_1.

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Punekar, N. S. "Enzyme Inhibition Analyses." In ENZYMES: Catalysis, Kinetics and Mechanisms, 231–36. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-0785-0_20.

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Conference papers on the topic "Enzymes - Kinetics"

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Díaz, Sebastián A., Joyce C. Breger, Anthony Malanoski, Jonathan C. Claussen, Scott A. Walper, Mario G. Ancona, Carl W. Brown, et al. "Modified kinetics of enzymes interacting with nanoparticles." In SPIE Nanoscience + Engineering, edited by Hooman Mohseni, Massoud H. Agahi, and Manijeh Razeghi. SPIE, 2015. http://dx.doi.org/10.1117/12.2188212.

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Kurkina, Yu N., A. S. Barskova, and E. P. Esina. "Kinetics of micromycetes that produce lignolytic enzymes in vitro." In CURRENT STATE, PROBLEMS AND PROSPECTS OF THE DEVELOPMENT OF AGRARIAN SCIENCE. Federal State Budget Scientific Institution “Research Institute of Agriculture of Crimea”, 2019. http://dx.doi.org/10.33952/09.09.2019.110.

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Jordan, R. E., R. M. Nelson, and J. Kilpatrick. "KINETICS OF THE HEPARIN-DEPENDENT INACTIVATION OF ANTITHROMBIN BY NEUTROPHIL ELASTASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643898.

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The rate of inhibition of coagulation enzymes by antithrombin III is greatly increased by an interaction between the inhibitor and a limited, anticoagulantly-active subfraction of heparin molecules. We have observed that this same heparin sub-fraction also greatly stimulates the rate of inactivation of antithrombin by neutrophil elastase. Inactivation rates were increased several hundred-fold by catalytic amounts of the anticoagulantly active heparin species and were unaffected by the inactive heparin fraction or other glycosaminoglycans. Addition of catalytic amounts of elastase (1:400) to a solution of antithrombin in the presence of saturating levels of anticoagulantly-active heparin caused an approximately 30% decrease in the ultraviolet fluorescence emission of the inhibitor. The rate of fluorescence loss corresponded exactly with the loss of inhibitory activity in a parallel incubation under the same conditions. The use of the fluorescence technique for kinetic measurement of inactivation rates indicated a Km of less than 1 uM for the heparin-antithrombin complex substrate and a turnover of several hundred per minute per enzyme molecule. Although the specificity of the heparin effect appears to be at the level of its interaction with antithrombin, an elastase-heparin interaction could also be detected in kinetic analyses. Chromatographic studies employing immobilized heparin confirmed that elastase itself binds tightly to the complex carbohydrate. These results suggest a subtle mechanism, of potential relevance to thrombosis associated with inflammatory conditions, in which both heparin and elastase act catalytically to direct the inactivation of antithrombin. Since anticoagulantly-active heparin species are present on endothelial cells, the above mechanism could markedly affect the balance between procoagulant and anticoagulant processes on the usually non-thrombogenic endothelial surface.
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Berjawi, Amal Ahmed. "Insecticide mortality,in vitrodetoxifying enzymes kinetics, and inhibition in two honey bee species,Apis melliferaandA. florea." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.117564.

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Frediansyah, Andri, Muhammad Kurniadi, Nurul Noviandi Nahdia Putri, and Eka Sunarwidhi Prasedya. "The kinetics of enzymes that involved in cassava fermentation produce by co-culture starter of two lactic acid bacteria." In PROCEEDINGS OF THE 2ND INTERNATIONAL CONFERENCE ON BIOSCIENCE, BIOTECHNOLOGY, AND BIOMETRICS 2019. AIP Publishing, 2019. http://dx.doi.org/10.1063/1.5141280.

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Ashafa, O., and S. Sabiu. "Membrane stabilization and kinetics of carbohydrate metabolizing enzymes (α-amylase and α-glucosidase) inhibitory potentials of Eucalyptus obliqua L. ethanolic leaf extract." In GA 2017 – Book of Abstracts. Georg Thieme Verlag KG, 2017. http://dx.doi.org/10.1055/s-0037-1608388.

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Khalil, Hilal S., Hemanth Tummala, Tedd Hupp, and Nikolai Zhelev. "Abstract 3103: Differences in the DDR enzymes activation kinetics between normal and cancer cells could be utilized to achieve targeted cellular sensitivity towards genotoxic agents." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3103.

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Setiawan, W. A., L. M. Yusiati, C. Hanim, and Muhlisin. "Ruminal hydrolytic enzymes activity and In Vitro gas production kinetics of pelleted leaves mixture as tannin source: Acacia mangium willd, Swietenia mahagoni, and Artocarpus heterophyllus." In PROCEEDINGS OF THE 4TH INTERNATIONAL CONFERENCE OF ANIMAL SCIENCE AND TECHNOLOGY (ICAST 2021). AIP Publishing, 2023. http://dx.doi.org/10.1063/5.0144018.

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Caner, Nazli, and Jeffrey W. Ruberti. "Detection of MMP-13 Activity on Intentionally Strain-Released Type-II Collagen Network in Bovine Articular Cartilage." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53913.

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Articular cartilage is a specialized avascular connective tissue found at the contact regions of diarthrodial joints. Cartilage has few cells (< 5% of the volume), though these cells can maintain the balance of turnover in healthy tissue, when the tissue is damaged, they are not able to repair the defects [1–3]. Extra cellular matrix (ECM) in cartilage comprises water, collagen (principally type II), proteoglycans and noncollagenous proteins. The type II collagen network, which is the dominant structural protein in cartilage ECM, constrains the expansion of the resident PGs and is generally held in mechanical tension. In osteoarthritis (OA), the balance of cartilage tissue production/degradation is thought to be affected by abnormal mechanical stimuli leading to net matrix resorption through production of excess degradative enzymes (e.g. matrix metalloproteinases (MMP) and aggrecanases) [4–8]. In OA tissue the amount of MMP-13 is thought to be increased relative to healthy tissue. OA typically occurs in older adults where, as cartilage ages, there is a marked decrease in the fixed charge density (FCD), the hydration and, consequently, mechanical tension on the collagen type II network [9–11]. We have hypothesized that loss of tension on the collagen network accelerates degradation by MMP. Detection of the effect of MMP on loaded, native cartilage could lead to insight about cartilage degradation kinetics in OA. However, it is quite difficult to controllably deliver MMP to cartilage, to activate the MMP during detensioning of the collagen network and to detect the effect on the cartilage mechanics (because cost limits the amount of MMP used). We have developed a transpirational enzyme loading method which is capable of precisely dosing bovine cartilage explants with a small, known quantity of MMP-13. Following enzyme insertion, we are able to detect the activity of the MMP on osmotically compressed cartilage (i.e. cartilage with a detensioned collagen network) via a simple hydration measurement.
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Kabir, Md Fauzul, and Lu-Kwang Ju. "Temperature effects on enzyme stability for carbohydrate hydrolysis of soy materials." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/srjx5896.

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Carbohydrate makes up one-third of the soybean mass. The oligo-/poly-meric carbohydrate lowers the value of soy protein products. Carbohydrate-rich byproducts like soy molasses are undervalued without large-volume applications. It is highly desirable to selectively remove carbohydrate and convert it to monosaccharides, as good fermentation feedstock for making biofuels and bioproducts. Enzymatic hydrolysis is an environment-friendly method to accomplish these, but it requires a complex mixture of enzymes including at least a-galactosidase, sucrase, pectinase, cellulase, and xylanase. Further, while the hydrolysis benefits from being done at elevated temperatures for faster reaction rates, the high temperatures pose challenges to the stability of enzymes. Here we investigated the short-term and long-term effects of high temperatures on these enzymes, to determine their optimum temperatures. For the short-term effects, enzyme broths produced from Aspergillus niger fermentations were analyzed at different temperatures for individual enzyme activities (a-galactosidase, sucrase, ...). The enzyme-assisted Arrhenius model developed by DeLong et al., which considered the temperature effects on enzyme conformation, was used to fit the temperature-dependent activity and determine its short-term optimum temperature. For long-term stability effects, enzyme broths were incubated at multiple temperatures for up to 72 h, and samples were taken at different times and analyzed to follow the activity changes. Regression with kinetic degradation models using the time-dependent activity changes gave the best-fit degradation constant for each enzyme at each temperature. Fitting these constants with the Arrhenius law gave a model that incorporated both effects of temperature and time on enzyme activity. As an application example, we also evaluated the performance of soybean molasses hydrolysis at the selected optimum temperature where the reaction rate was fast enough while denaturation of a-galactosidase, the key enzyme for stachyose and raffinose hydrolysis, was not too fast. Detailed results and discussion will be presented.
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Reports on the topic "Enzymes - Kinetics"

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Sandermann, Heinrich, Duncan Jr., and Thomas M. Lipid-Dependent Membrane Enzymes. Kinetic Modelling of the Activation of Protein Kinase C by Phosphatidylserine. Fort Belvoir, VA: Defense Technical Information Center, January 1991. http://dx.doi.org/10.21236/ada302987.

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Chikwana, Vimbai. Discovery of Novel Amidotransferase Activity Involved In Archaeosine Biosynthesis and Structural and Kinetic Investigation of QueF, an Enzyme Involved in Queuosine Biosynthesis. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.140.

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Pesis, Edna, and Mikal Saltveit. Postharvest Delay of Fruit Ripening by Metabolites of Anaerobic Respiration: Acetaldehyde and Ethanol. United States Department of Agriculture, October 1995. http://dx.doi.org/10.32747/1995.7604923.bard.

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The use of pretreatments for 24 h prior to storage, under anaerobic condtions, or in the presence of the natural metabolic products, acetaldehyde (AA) and ethanol, to delay fruit ripening, was found to be effective with several climacteric fruits, among them avocado, mango, peach and tomato. The delay in ripening of avocado, peach and tomato was accompanied by inhibition of ethylene production and of fruit softening. The maintenance of fruit firmness was associated with a decrease in the activities of cell-wall-degrading enzymes, including endoglucanases (Cx), polygalacturonases (PG) and b-galactosidases. In peaches the AA- and N2-treated fruits were firmer after 3 weeks storage and contained higher amount of insoluble pectin than untreated controls. We showed that AA vapors are able to inhibit ripening, ethylene production and ethylene induction in the presence of 1-amino-cyclopropane-1-carboxylic acid (ADD) in avocado and mango tissue. Ethylene induced by ACC is taken as an indicator of ACC oxidase activity. ACC oxidase activity in AA-treated avocado fruit was much lower than in the untreated fruit. In carnation flowers very little ethylene was produced by ethanol-treated flowers, and the normal increases in ACC content and ACC oxidase activity were also suppressed. Using kinetic studies and inhibitors of alcohol dehydrogenase (ADH), we showed that AA, not ethanol, was the active molecule in inhibiting ripening of tomato fruit. Application of anaerobiosis or anaerobic metabolites was effective in reduction of chilling injury (CI) in various plant tissues. Pretreatment with a low-O2 atmosphere reduced CI symptoms in avocado; this effect was associated with higher content of the free sylfhydryl (SH) group, and induction of the detoxification enzymes, catalase and peroxidase. Application of AA maintained firmer and brighter pulp tissue (non-oxidative), which was associated with higher free SH content, lower ethylene and ACC oxidase activities, and higher activities of catalase and peroxidase. Ethanol was found to reduce CI in other plant tissue. In roots of 24-h-old germinated cucumber seeds, exposure to 0.4-M ethanol shock for 4 h reduced chilling-induced ion leakage. In cucumber cotyledons it appears that alcohols may reduce CI by inducing stomata closure. In cotyledon discs held in N2 at 10C for 1 day, there accumulated sufficient endogenously synthesized ethanol to confer tolerance to chilling at 2.5C for 5 days.
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Shoseyov, Oded, Steven A. Weinbaum, Raphael Goren, and Abhaya M. Dandekar. Biological Thinning of Fruit Set by RNAase in Deciduous Fruit Trees. United States Department of Agriculture, August 1993. http://dx.doi.org/10.32747/1993.7568110.bard.

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Fruit thinning is a common and necessary practice for commercial fruit production in many deciduous tree fruit species. Fruit thinning in apple may be accomplished with a variety of chemical thinning agents, but the use of these chemicals is a subject of environmental concern. It has been shown recently that RNase enzyme, secreted from the stigma and the style, inhibits pollen germination and pollen tube elongation. In this study we have been able to show that Aspergillus niger B-1 RNase can effectively inhibit peach and apple pollen germination, and tube elongation in-vitro, as well as thin fruit in peach and apple, and reduce the number of seeds in citrus. The objectives of the research were to detrmine the conditions for effective thinning of (USA and Israel), develop fermentation process for cost effective production of RNase from A. niger. (Israel), and clone apple S-RNase cDNA (USA). All the objectives of the research were addressed. We have determined the optimal fermentation conditions for cost effective production of the A. niger at a 20,000 liters scale. TheA. niger B1 RNase was isolated to homogeneity and its kinetic and biochemical properties including its N-terminal sequence were fully characterized. The field test results both in Israel and California have shown variability in effectiveness and more work is needed to define the RNase concentration necessary to completely inhibit pollen development. Plant transformation vectors expressing anti-sense apple S-RNase genes were constructed (USA) with an attempt to produce self compatible transgenic apple trees. Bovine S-Protein cDNA was cloned and successfully expressed in E. coli (Israel). Plant transformation vector expressing the S-Protein gene was constructed (USA) with an attempt to produce transgenic plants expressing S-protein in the style. Exogenous application of S-peptide to these plants will result in active RNase and consequently prevention of fertilization.
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