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Artigos de revistas sobre o tema "Enzyme activation"

Autor: Grafiati

Publicado: 4 de junho de 2021

Última modificação: 25 de julho de 2025

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1

Wollenberger, Ulla, and Frieder W. Scheller. "Enzyme activation for activator and enzyme activity measurement☆." Biosensors and Bioelectronics 8, no. 6 (1993): 291–97. http://dx.doi.org/10.1016/0956-5663(93)85009-d.

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2

Wang, Fang, Yuchen Liu, Chang Du, and Renjun Gao. "Current Strategies for Real-Time Enzyme Activation." Biomolecules 12, no. 5 (2022): 599. http://dx.doi.org/10.3390/biom12050599.

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Enzyme activation is a powerful means of achieving biotransformation function, aiming to intensify the reaction processes with a higher yield of product in a short time, and can be exploited for diverse applications. However, conventional activation strategies such as genetic engineering and chemical modification are generally irreversible for enzyme activity, and they also have many limitations, including complex processes and unpredictable results. Recently, near-infrared (NIR), alternating magnetic field (AMF), microwave and ultrasound irradiation, as real-time and precise activation strate

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3

Hamilton-Miller, J. M. T., and Q. Li. "Enzyme-Catalyzed Antimicrobial Activation." Antimicrobial Agents and Chemotherapy 46, no. 11 (2002): 3692. http://dx.doi.org/10.1128/aac.46.11.3692.2002.

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4

Hadfield, Andrea T. "Electron-Induced Enzyme Activation." Structure 14, no. 1 (2006): 1–2. http://dx.doi.org/10.1016/j.str.2005.12.002.

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5

Bott, R., G. Ganshaw, M. Soltis, P. Kuhn, and M. Knapp. "Snapshots of Enzyme Activation." Acta Crystallographica Section A Foundations of Crystallography 56, s1 (2000): s247. http://dx.doi.org/10.1107/s0108767300025319.

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6

Cassels, R., R. Fears, and R. A. Smith. "The interaction of streptokinase.plasminogen activator complex, tissue-type plasminogen activator, urokinase and their acylated derivatives with fibrin and cyanogen bromide digest of fibrinogen. Relationship to fibrinolytic potency in vitro." Biochemical Journal 247, no. 2 (1987): 395–400. http://dx.doi.org/10.1042/bj2470395.

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The effects of purified soluble fibrin and of fibrinogen fragments (fibrin mimic) on the activation of Lys-plasminogen (i.e. plasminogen residues 77-790) to plasmin by streptokinase.plasminogen activator complex and by tissue-type plasminogen activator were studied. Dissociation constants of both activators were estimated to lie in the range 90-160 nM (fibrin) and 16-60 nM (CNBr-cleavage fragments of fibrinogen). The kinetic mechanism for both types of activator comprised non-essential enzyme activation via a Rapid Equilibrium Ordered Bireactant sequence. In order to relate the fibrin affinity

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7

Arcus, Vickery L., and Adrian J. Mulholland. "Temperature, Dynamics, and Enzyme-Catalyzed Reaction Rates." Annual Review of Biophysics 49, no. 1 (2020): 163–80. http://dx.doi.org/10.1146/annurev-biophys-121219-081520.

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We review the adaptations of enzyme activity to different temperatures. Psychrophilic (cold-adapted) enzymes show significantly different activation parameters (lower activation enthalpies and entropies) from their mesophilic counterparts. Furthermore, there is increasing evidence that the temperature dependence of many enzyme-catalyzed reactions is more complex than is widely believed. Many enzymes show curvature in plots of activity versus temperature that is not accounted for by denaturation or unfolding. This is explained by macromolecular rate theory: A negative activation heat capacity f

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8

KHOLODENKO, Boris N., and Guy C. BROWN. "Paradoxical control properties of enzymes within pathways: can activation cause an enzyme to have increased control?" Biochemical Journal 314, no. 3 (1996): 753–60. http://dx.doi.org/10.1042/bj3140753.

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It is widely assumed that within a metabolic pathway inhibition of an enzyme causes the control exerted by that enzyme over the flux through its own reaction to increase, whereas activation causes its control to decrease. This assumption forms the basis of a number of experimental methods. For a pathway conceptually divided into two enzyme groups connected via a single metabolite we have derived a general condition under which this assumption is false, and thus the pathway shows paradoxical control behaviour, i.e. increased control with activation and decreased control with inhibition of an en

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9

Vater, C. A., H. Nagase, and E. D. Harris. "Proactivator-dependent activation of procollagenase induced by treatment with EGTA." Biochemical Journal 237, no. 3 (1986): 853–58. http://dx.doi.org/10.1042/bj2370853.

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A new mechanism for activation of the proactivator of procollagenase [Vater, Nagase & Harris (1983) J. Biol. Chem. 258, 9374-9382] has been found. Collagenolytic and other proteolytic enzyme activities in the medium of cultured rabbit synovial fibroblasts were found to be activated by a new mechanism: short-term incubation at 37 degrees C performed in the presence of EGTA followed by replacement of Ca2+ during enzyme assay. The crucial event in procollagenase activation is the production of a functional activator enzyme. Activation of procollagenase in the culture medium did not occur when

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10

Shisler, Krista A., Rachel U. Hutcheson, Masaki Horitani, et al. "Monovalent Cation Activation of the Radical SAM Enzyme Pyruvate Formate-Lyase Activating Enzyme." Journal of the American Chemical Society 139, no. 34 (2017): 11803–13. http://dx.doi.org/10.1021/jacs.7b04883.

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11

Park, Yong-Doo, Yi Yang, Qing-Xi Chen, Hai-Ning Lin, Qiang Liu, and Hai-Meng Zhou. "Kinetics of complexing activation by the magnesium ion on green crab (Scylla serrata) alkaline phosphatase." Biochemistry and Cell Biology 79, no. 6 (2001): 765–72. http://dx.doi.org/10.1139/o01-152.

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As with mammalian enzymes, green crab (Scylla serrata) alkaline phosphatase can be activated by Mg2+through a time-dependent course. The activation is mainly a Vmaxeffect. Tsou's method was used to study the kinetic course of activation. The results show that the enzyme was activated by a complexing scheme that had not been previously identified: the enzyme first reversibly and quickly binds Mg2+and then undergoes a slow reversible course to activation, with a relatively high activation energy (78 ± 4 kJ/mol) and a slow conformational change. The activation reaction is a single molecule reacti

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12

Hung, Hui-Chih, Meng-Wei Kuo, Gu-Gang Chang, and Guang-Yaw Liu. "Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human mitochondrial NAD(P)+-dependent malate dehydrogenase (malic enzyme)." Biochemical Journal 392, no. 1 (2005): 39–45. http://dx.doi.org/10.1042/bj20050641.

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Human mitochondrial NAD(P)+-dependent malate dehydrogenase (decarboxylating) (malic enzyme) can be specifically and allosterically activated by fumarate. X-ray crystal structures have revealed conformational changes in the enzyme in the absence and in the presence of fumarate. Previous studies have indicated that fumarate is bound to the allosteric pocket via Arg67 and Arg91. Mutation of these residues almost abolishes the activating effect of fumarate. However, these amino acid residues are conserved in some enzymes that are not activated by fumarate, suggesting that there may be additional f

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13

Lee, Moo-Yeal, and Jonathan S. Dordick. "Enzyme activation for nonaqueous media." Current Opinion in Biotechnology 13, no. 4 (2002): 376–84. http://dx.doi.org/10.1016/s0958-1669(02)00337-3.

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14

Takegawa, Mai, Tsubasa Tagawa, Ayumi Ogata, Shigeru Shimamoto, and Yuji Hidaka. "Enzyme Activation Mechanism of Cocoonase." Biophysical Journal 118, no. 3 (2020): 532a. http://dx.doi.org/10.1016/j.bpj.2019.11.2919.

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15

BOATRIGHT, Kelly M., Cristina DEIS, Jean-Bernard DENAULT, Daniel P. SUTHERLIN, and Guy S. SALVESEN. "Activation of caspases-8 and -10 by FLIPL." Biochemical Journal 382, no. 2 (2004): 651–57. http://dx.doi.org/10.1042/bj20040809.

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The first step in caspase activation is transition of the latent zymogen to an active form. For the initiator caspases, this occurs through dimerization of monomeric zymogens at an activating complex. Recent studies have suggested that FLIPL [FLICE-like inhibitory protein, long form; FLICE is FADD (Fas-associated death domain protein)-like interleukin-1β-converting enzyme], previously thought to act solely as an inhibitor of caspase-8 activation, can under certain circumstances function to enhance caspase activation. Using an in vitro induced-proximity assay, we demonstrate that activation of

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16

Ghosh, S. K., S. Majumder, N. K. Mukhopadhyay, and S. K. Bose. "Functional characterization of constituent enzyme fractions of mycobacillin synthetase." Biochemical Journal 230, no. 3 (1985): 785–89. http://dx.doi.org/10.1042/bj2300785.

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The enzyme fraction A, a constituent enzyme of the three-fraction enzyme mycobacillin synthetase, independently and sequentially activated five amino acids starting from L-proline, producing the pentapeptide Pro(Asp1,Glu1,Tyr1)Asp. The fractions B and C were unable to function independently. However, the fraction B synthesized the nonapeptide Pro(Asp3,Glu1,Tyr2,Ser1)Leu, sequentially activating the pentapeptide and next four amino acids, whereas the fraction C synthesized mycobacillin by the sequential activation of the nonapeptide and the remaining four amino acids. The pH optima of the above

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17

GRIGG, Michael E., Kleoniki GOUNARIS, and Murray E. SELKIRK. "Characterization of a platelet-activating factor acetylhydrolase secreted by the nematode parasite Nippostrongylus brasiliensis." Biochemical Journal 317, no. 2 (1996): 541–47. http://dx.doi.org/10.1042/bj3170541.

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Nippostrongylus brasiliensis, a small nematode parasite of the gastrointestinal tract of rodents, secretes an enzyme that cleaves the proinflammatory molecule platelet-activating factor to its inactive lyso- form. The enzyme activity is Ca2+-dependent and does not exhibit interfacial activation. It does not require the addition of reducing agents for maximal activity, and is not inhibited by thiol-active reagents. Sensitivity to inhibitors suggests the involvement of serine and histidine residues in the enzyme activity. As described for other platelet-activating factor acetylhydrolases, it can

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18

Dušeková, Eva, Martin Berta, Dagmar Sedláková, et al. "Specific anion effect on properties of HRV 3C protease." Biophysical chemistry 287 (May 11, 2022): 106825. https://doi.org/10.1016/j.bpc.2022.106825.

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Specific salts effect is intensively studied from the prospective of modification of different physico-chemical properties of biomacromolecules. Limited knowledge of the specific salts effect on enzymes led us to address the influence of five sodium anions: sulfate, phosphate, chloride, bromide, and perchlorate, on catalytic and conformational properties of human rhinovirus-14 (HRV) 3C protease. The enzyme conformation was monitored by circular dichroism spectrum (CD) and by tyrosines fluorescence. Stability and flexibility of the enzyme have been analyzed by CD in the far-UV region, different

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19

Chau, Helen S., and Stephen K. Ng. "Activation of phosphoenolpyruvate carboxykinase isolated from Veillonella parvula." Biochemistry and Cell Biology 64, no. 9 (1986): 898–905. http://dx.doi.org/10.1139/o86-120.

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Phosphoenolpyruvate carboxykinase (PEPCK, EC 4.1.1.49) has been purified 940-fold from Veillonella parvula using protamine sulphate treatment, ammonium sulphate precipitation, and column chromatography. The purified enzyme was substantially free of contaminating enzymes or proteins. Maximum activity in the direction of oxaloacetate (OAA) decarboxylation was exhibited at pH 9.0. At this pH, the V. parvula enzyme catalysed phosphenolpyruvate formation in the presence of Mn2+ ions. In the presence of varying concentrations of OAA and ATP, the PEPCK from V. parvula exhibited hyperbolic kinetics wi

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20

Komatsu, Masayuki, Madhu Biyani, Sunita Ghimire Gautam, and Koichi Nishigaki. "Peptide-Modulated Activity Enhancement of Acidic Protease Cathepsin E at Neutral pH." International Journal of Peptides 2012 (December 17, 2012): 1–7. http://dx.doi.org/10.1155/2012/316432.

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Enzymes are regulated by their activation and inhibition. Enzyme activators can often be effective tools for scientific and medical purposes, although they are more difficult to obtain than inhibitors. Here, using the paired peptide method, we report on protease-cathepsin-E-activating peptides that are obtained at neutral pH. These selected peptides also underwent molecular evolution, after which their cathepsin E activation capability improved. Thus, the activators we obtained could enhance cathepsin-E-induced cancer cell apoptosis, which indicated their potential as cancer drug precursors.

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21

Zhang, Wei-Wei, Kent Redman, Sharon Churchill та Perry Churchill. "Comparison of D-β-hydroxybutyrate dehydrogenase from rat liver and brain mitochondria". Biochemistry and Cell Biology 68, № 10 (1990): 1225–30. http://dx.doi.org/10.1139/o90-182.

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The properties of D-β-hydroxybutyrate dehydrogenase (BDH) from rat liver and brain mitochondria were compared to determine if isozymes of this enzyme exist in these tissues. The BDHs from these tissues behaved similarly during the purification process. The enzymes were indistinguishable by sodium dodecyl sulfate – polyacrylamide or acid-urea – polyacrylamide gel electrophoresis and they had identical isoelectric points. The BDHs from rat liver and brain were also quite similar in functional parameters determined by kinetic analysis and phospholipid activation of apo-BDH (i.e., the lipid-free e

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22

Markovic, Milica, Shimon Ben-Shabat, and Arik Dahan. "Computational Simulations to Guide Enzyme-Mediated Prodrug Activation." International Journal of Molecular Sciences 21, no. 10 (2020): 3621. http://dx.doi.org/10.3390/ijms21103621.

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Prodrugs are designed to improve pharmaceutical/biopharmaceutical characteristics, pharmacokinetic/pharmacodynamic properties, site-specificity, and more. A crucial step in successful prodrug is its activation, which releases the active parent drug, exerting a therapeutic effect. Prodrug activation can be based on oxidation/reduction processes, or through enzyme-mediated hydrolysis, from oxidoreductases (i.e., Cytochrome P450) to hydrolytic enzymes (i.e., carboxylesterase). This study provides an overview of the novel in silico methods for the optimization of enzyme-mediated prodrug activation

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23

LEE, Sang Hyoung, J. David JOHNSON, Michael P. WALSH, et al. "Differential regulation of Ca2+/calmodulin-dependent enzymes by plant calmodulin isoforms and free Ca2+ concentration." Biochemical Journal 350, no. 1 (2000): 299–306. http://dx.doi.org/10.1042/bj3500299.

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Multiple calmodulin (CaM) isoforms are expressed in plants, but their biochemical characteristics are not well resolved. Here we show the differential regulation exhibited by two soya bean CaM isoforms (SCaM-1 and SCaM-4) for the activation of five CaM-dependent enzymes, and the Ca2+ dependence of their target enzyme activation. SCaM-1 activated myosin light-chain kinase as effectively as brain CaM (Kact 1.8 and 1.7nM respectively), but SCaM-4 produced no activation of this enzyme. Both CaM isoforms supported near maximal activation of CaM-dependent protein kinase II (CaM KII), but SCaM-4 exh

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24

Cárdenas, M. L., and A. Cornish-Bowden. "Characteristics necessary for an interconvertible enzyme cascade to generate a highly sensitive response to an effector." Biochemical Journal 257, no. 2 (1989): 339–45. http://dx.doi.org/10.1042/bj2570339.

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A monocyclic interconvertible enzyme cascade, in which active and inactive states of an enzyme are interconverted by two opposing enzyme-catalysed reactions, does not necessarily produce a greater degree of sensitivity to an effector than one could expect from direct interaction between effector and target reaction. On the contrary, a cascade in which an effector acts on one of the enzymes catalysing the interconversion reactions by altering the apparent value of its specificity constant will always generate a less sensitive response than direct interaction would give. Nonetheless, even if bot

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25

Sharrock, Abigail V., Jeff S. Mumm, Elsie M. Williams, et al. "Structural Evaluation of a Nitroreductase Engineered for Improved Activation of the 5-Nitroimidazole PET Probe SN33623." International Journal of Molecular Sciences 25, no. 12 (2024): 6593. http://dx.doi.org/10.3390/ijms25126593.

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Bacterial nitroreductase enzymes capable of activating imaging probes and prodrugs are valuable tools for gene-directed enzyme prodrug therapies and targeted cell ablation models. We recently engineered a nitroreductase (E. coli NfsB F70A/F108Y) for the substantially enhanced reduction of the 5-nitroimidazole PET-capable probe, SN33623, which permits the theranostic imaging of vectors labeled with oxygen-insensitive bacterial nitroreductases. This mutant enzyme also shows improved activation of the DNA-alkylation prodrugs CB1954 and metronidazole. To elucidate the mechanism behind these enhanc

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26

Pederick, Jordan L., Andrew P. Thompson, Stephen G. Bell, and John B. Bruning. "d-Alanine–d-alanine ligase as a model for the activation of ATP-grasp enzymes by monovalent cations." Journal of Biological Chemistry 295, no. 23 (2020): 7894–904. http://dx.doi.org/10.1074/jbc.ra120.012936.

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The ATP-grasp superfamily of enzymes shares an atypical nucleotide-binding site known as the ATP-grasp fold. These enzymes are involved in many biological pathways in all domains of life. One ATP-grasp enzyme, d-alanine–d-alanine ligase (Ddl), catalyzes ATP-dependent formation of the d-alanyl–d-alanine dipeptide essential for bacterial cell wall biosynthesis and is therefore an important antibiotic drug target. Ddl is activated by the monovalent cation (MVC) K+, but despite its clinical relevance and decades of research, how this activation occurs has not been elucidated. We demonstrate here t

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27

EDWARDS, Robert A., Michael P. WALSH, Cindy SUTHERLAND, and Hans J. VOGEL. "Activation of calcineurin and smooth muscle myosin light chain kinase by Met-to-Leu mutants of calmodulin." Biochemical Journal 331, no. 1 (1998): 149–52. http://dx.doi.org/10.1042/bj3310149.

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The effects of replacement of each of the individual Met in calmodulin (CaM) with Leu on the activation of two CaM target enzymes [smooth muscle myosin light chain kinase (smMLCK) and calcineurin (CN)] were investigated. The KD and Pmax (percentage maximal activation) values for activation of both enzymes by M76L-CaM were indistinguishable from wild-type (wt)-CaM, which is consistent with the location of Met-76 in the central linker that is not involved in target protein interaction. The other eight Met in CaM are exposed in the hydrophobic surfaces that are involved in target-enzymes binding,

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28

Plafker, Scott M., Kendra S. Plafker, Allan M. Weissman, and Ian G. Macara. "Ubiquitin charging of human class III ubiquitin-conjugating enzymes triggers their nuclear import." Journal of Cell Biology 167, no. 4 (2004): 649–59. http://dx.doi.org/10.1083/jcb.200406001.

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Ubiquitin is a small polypeptide that is conjugated to proteins and commonly serves as a degradation signal. The attachment of ubiquitin (Ub) to a substrate proceeds through a multi-enzyme cascade involving an activating enzyme (E1), a conjugating enzyme (E2), and a protein ligase (E3). We previously demonstrated that a murine E2, UbcM2, is imported into nuclei by the transport receptor importin-11. We now show that the import mechanism for UbcM2 and two other human class III E2s (UbcH6 and UBE2E2) uniquely requires the covalent attachment of Ub to the active site cysteine of these enzymes. Th

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29

Anderson, Louise, and Per Gardeström. "Reductive light activation of enzyme activity." Physiologia Plantarum 110, no. 3 (2008): 295. http://dx.doi.org/10.1111/j.1399-3054.2000.1100301.x.

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Rana, S., N. Pozzi, L. A. Pelc, and E. Di Cera. "Redesigning allosteric activation in an enzyme." Proceedings of the National Academy of Sciences 108, no. 13 (2011): 5221–25. http://dx.doi.org/10.1073/pnas.1018860108.

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Rooseboom, Martijn, Jan N. M. Commandeur, and Nico P. E. Vermeulen. "Enzyme-Catalyzed Activation of Anticancer Prodrugs." Pharmacological Reviews 56, no. 1 (2004): 53–102. http://dx.doi.org/10.1124/pr.56.1.3.

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Anderson, Louise, and Per Gardestrom. "Reductive light activation of enzyme activity." Physiologia Plantarum 110, no. 3 (2000): 295. http://dx.doi.org/10.1034/j.1399-3054.2000.1100301.x.

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Yang, Yan-hui, Herve Aloysius, Daigo Inoyama, Yu Chen, and Long-qin Hu. "Enzyme-mediated hydrolytic activation of prodrugs." Acta Pharmaceutica Sinica B 1, no. 3 (2011): 143–59. http://dx.doi.org/10.1016/j.apsb.2011.08.001.

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Chakrabarty, Arindam, Debajyoti Dutta, Mithu Baidya, Anirudha Dutta, Amit Kumar Das, and Sudip K. Ghosh. "Metronidazole Activation by a Deeply Entangled Dimeric Malic Enzyme in Entamoeba histolytica." Pathogens 14, no. 3 (2025): 277. https://doi.org/10.3390/pathogens14030277.

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Metronidazole is the preferred drug for treating amoebiasis caused by Entamoeba histolytica. Its antiamoebic activity is primarily attributed to activation by various reductases. This study reports an alternative activation pathway in E. histolytica mediated by the decarboxylating malic enzyme. Functional characterization of this NADPH-dependent enzyme reveals that it is secreted into the extracellular milieu and may play a role in E. histolytica adhesion to human enteric cells. Structural analysis of the E. histolytica malic enzyme (EhME) demonstrates that the protein forms a strict dimer, wi

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35

Pyatakova, N. V., and I. S. Severina. "Soluble guanylate cyclase in the molecular mechanism underlying the therapeutic action of drugs." Biomeditsinskaya Khimiya 58, no. 1 (2012): 32–42. http://dx.doi.org/10.18097/pbmc20125801032.

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The influence of ambroxol - a mucolytic drug - on the activity of human platelet soluble guanylate cyclase and rat lung soluble guanylate cyclase and activation of both enzymes by NO-donors (sodium nitroprusside and Sin-1) were investigated. Ambroxol in the concentration range from 0.1 to 10 μM had no effect on the basal activity of both enzymes. Ambroxol inhibited in a concentration-dependent manner the sodium nitroprusside-induced human platelet soluble guanylate cyclase and rat lung soluble guanylate cyclase with the IC50 values 3.9 and 2.1 μM, respectively. Ambroxol did not influence the s

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Berger, Stefanie, Cornelia Welte, and Uwe Deppenmeier. "Acetate Activation inMethanosaeta thermophila: Characterization of the Key Enzymes Pyrophosphatase and Acetyl-CoA Synthetase." Archaea 2012 (2012): 1–10. http://dx.doi.org/10.1155/2012/315153.

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The thermophilic methanogenMethanosaeta thermophilauses acetate as sole substrate for methanogenesis. It was proposed that the acetate activation reaction that is needed to feed acetate into the methanogenic pathway requires the hydrolysis of two ATP, whereas the acetate activation reaction inMethanosarcina sp.is known to require only one ATP. As these organisms live at the thermodynamic limit that sustains life, the acetate activation reaction inMt. thermophilaseems too costly and was thus reevaluated. It was found that of the putative acetate activation enzymes one gene encoding an AMP-formi

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Trusek, Anna. "Graphene oxide flake activation via divinylsulfone – a procedure for efficient β-galactosidase immobilization". Polish Journal of Chemical Technology 21, № 1 (2019): 27–32. http://dx.doi.org/10.2478/pjct-2019-0006.

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Abstract Flaky graphene oxide was activated with divinylsulfone followed by immobilization of the β-galactosidase enzyme. An active and stable preparation was obtained. β-galactosidase stability after immobilization was much higher than with the native enzyme. The half-life time of the immobilized enzyme was estimated as 165 hours, while for the native form, the estimate was only 5 hours. The developed procedure for the preparation of flaked graphene and its use in the chemical immobilization of enzymes can be used for any enzyme. A processing solution for continuous operation was proposed and

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Marshall, Andrew C., and John B. Bruning. "Engineering potassium activation into biosynthetic thiolase." Biochemical Journal 478, no. 15 (2021): 3047–62. http://dx.doi.org/10.1042/bcj20210455.

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Activation of enzymes by monovalent cations (M+) is a widespread phenomenon in biology. Despite this, there are few structure-based studies describing the underlying molecular details. Thiolases are a ubiquitous and highly conserved family of enzymes containing both K+-activated and K+-independent members. Guided by structures of naturally occurring K+-activated thiolases, we have used a structure-based approach to engineer K+-activation into a K+-independent thiolase. To our knowledge, this is the first demonstration of engineering K+-activation into an enzyme, showing the malleability of pro

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Tran, Giang Thi Linh, and Oanh Ngoc Huynh. "Preparation and immobilization Glucoamylase and Pectinase by CLEA method." Science and Technology Development Journal 17, no. 2 (2014): 45–51. http://dx.doi.org/10.32508/stdj.v17i2.1358.

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CLEA method (cross-linking enzyme aggregates) combines enzyme preparation and immobilization from solution culture into the same step. In this study, we applied CLEA method to immobilize two enzymes, glucoamylase and pectinase, from crude enzyme solution obtained from semi-solid culture of Aspergillus niger. The results showed that: In the same immobilized conditions (glucoamylase: 7% glutaraldehyde, 5°C, 2 hours; pectinase: 10% glutaraldehyde, 5°C, 2 hours), the immobilized enzyme from crude enzyme solution, has the abilities to be reused and activation stability under the influences of pH an

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Demirkan, Elif, Tuba Avci, and Yakup Aykut. "Protease immobilization on cellulose monoacetate/chitosan-blended nanofibers." Journal of Industrial Textiles 47, no. 8 (2017): 2092–111. http://dx.doi.org/10.1177/1528083717720205.

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Chitosan-blended cellulose monoacetate nanofibers were prepared through electrospinning process. Neat nanofibers and their sodium hydroxide-treated analogs were used as support surfaces for protease immobilization via physical adsorption method. Morphologies of the nanofibers were observed with a scanning electron microscopy. Chemical analyses were conducted with Fourier transform infrared spectroscopy, and thermal analyses were carried out with differential scanning calorimeter and thermogravimetric analyzer. Immobilized enzyme activities were measured by using casein substrate. In order to t

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Akram, Muhammad, Urooj Rehman, Misbah Ahmed, and Isaac John Umaru. "Exploring the Dynamics of Enzyme Activity: Environmental and Biological Influences." African Journal of Biochemistry and Molecular Biology Research 2, no. 2 (2025): 125–34. https://doi.org/10.58578/ajbmbr.v2i2.5268.

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The work presents the classification of enzymes and factors that are affecting enzymatic reactions in the living systems. Factors such as temperature, pH, enzyme concentration, substrate concentration, factors of inhibition, factors of activation, and incubation time are important in influencing enzyme reactions, which are responsible for controlling components in living systems. The majority of enzymes are three-dimensional molecules with complex molecular networks and sensitive to various environmental factors.

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Page, Michael J., and Enrico Di Cera. "Role of Na+and K+in Enzyme Function." Physiological Reviews 86, no. 4 (2006): 1049–92. http://dx.doi.org/10.1152/physrev.00008.2006.

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Metal complexation is a key mediator or modifier of enzyme structure and function. In addition to divalent and polyvalent metals, group IA metals Na+and K+play important and specific roles that assist function of biological macromolecules. We examine the diversity of monovalent cation (M+)-activated enzymes by first comparing coordination in small molecules followed by a discussion of theoretical and practical aspects. Select examples of enzymes that utilize M+as a cofactor (type I) or allosteric effector (type II) illustrate the structural basis of activation by Na+and K+, along with unexpect

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Edmund, Aaron B., Timothy F. Walseth, Nicholas M. Levinson, and Lincoln R. Potter. "The pseudokinase domains of guanylyl cyclase–A and –B allosterically increase the affinity of their catalytic domains for substrate." Science Signaling 12, no. 566 (2019): eaau5378. http://dx.doi.org/10.1126/scisignal.aau5378.

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Natriuretic peptides regulate multiple physiologic systems by activating transmembrane receptors containing intracellular guanylyl cyclase domains, such as GC-A and GC-B, also known as Npr1 and Npr2, respectively. Both enzymes contain an intracellular, phosphorylated pseudokinase domain (PKD) critical for activation of the C-terminal cGMP-synthesizing guanylyl cyclase domain. Because ATP allosterically activates GC-A and GC-B, we investigated how ATP binding to the PKD influenced guanylyl cyclase activity. Molecular modeling indicated that all the residues of the ATP-binding site of the protot

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Saito, T., L. Small, and UW Goodenough. "Activation of adenylyl cyclase in Chlamydomonas reinhardtii by adhesion and by heat." Journal of Cell Biology 122, no. 1 (1993): 137–47. http://dx.doi.org/10.1083/jcb.122.1.137.

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Adhesion between Chlamydomonas reinhardtii gametes generates a rapid rise in cAMP levels which stimulates mating responses and zygotic cell fusion (Pasquale and Goodenough, 1987). We show here that sexual adhesion in vivo results in a twofold stimulation of flagellar adenylyl cyclase activity when the enzyme is subsequently assayed in vitro, a stimulation that is specifically blocked by Cd2+. A twofold stimulation is also elicited by the in vitro presentation of soluble cross-linking reagents (antisera and concanavalin A). In contrast, the 10-30-fold stimulation of the flagellar cyclase by in

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Iwase, Katsumi, Brian C. W. Hummel, and Paul G. Walfish. "Cytosol components from human placenta and rat liver in iodothyronine 5- and 5′-deiodination." Biochemistry and Cell Biology 67, no. 1 (1989): 58–63. http://dx.doi.org/10.1139/o89-009.

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Using either human placental microsomal 5-deiodinase as enzyme (5-DI) and thyroxine as substrate or rat liver (RL) microsomal 5′-deiodinase (5′ DI) as enzyme and reverse [(3′- or 5′-)-125I]triiodo-L-thyronine ([125I]rT3) as substrate, activation of 5′-DI in the presence of NADPH was observed using either human placental or rat liver cytosolic components, but there was no activation of 5-DI. Both could be activated by DTT, with higher concentrations being required for 5-DI than for 5′-DI. Iopanoic acid, dicumarol, and sodium arsenite inhibited 5′-DI and 5-DI activated by DTT. In the presence of

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Chosa, Naoyuki, Takashi Fukumitsu, Kengo Fujimoto, and Eiji Ohnishi. "Activation of prophenoloxidase A1 by an activating enzyme in Drosophila melanogaster." Insect Biochemistry and Molecular Biology 27, no. 1 (1997): 61–68. http://dx.doi.org/10.1016/s0965-1748(96)00070-7.

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Kazemi, Masoud, Fahmi Himo, and Johan Åqvist. "Enzyme catalysis by entropy without Circe effect." Proceedings of the National Academy of Sciences 113, no. 9 (2016): 2406–11. http://dx.doi.org/10.1073/pnas.1521020113.

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Entropic effects have often been invoked to explain the extraordinary catalytic power of enzymes. In particular, the hypothesis that enzymes can use part of the substrate-binding free energy to reduce the entropic penalty associated with the subsequent chemical transformation has been very influential. The enzymatic reaction of cytidine deaminase appears to be a distinct example. Here, substrate binding is associated with a significant entropy loss that closely matches the activation entropy penalty for the uncatalyzed reaction in water, whereas the activation entropy for the rate-limiting cat

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Tiganescu, Ana, Melanie Hupe, Yoshikazu Uchida, Theodora Mauro, Peter M. Elias, and Walter M. Holleran. "Increased glucocorticoid activation during mouse skin wound healing." Journal of Endocrinology 221, no. 1 (2014): 51–61. http://dx.doi.org/10.1530/joe-13-0420.

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Glucocorticoid (GC) excess inhibits wound healing causing increased patient discomfort and infection risk. 11β-hydroxysteroid dehydrogenase type 1 (11β-HSD1) activates GCs (converting 11-dehydrocorticosterone to corticosterone in rodents) in many tissues including skin, wherede novosteroidogenesis from cholesterol has also been reported. To examine the regulation of 11β-HSD1 and steroidogenic enzyme expression during wound healing, 5 mm wounds were generated in female SKH1 mice and compared at days 0, 2, 4, 8, 14, and 21 relative to unwounded skin. 11β-HSD1 expression (mRNA and protein) and en

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Fillat, M. F., D. E. Edmondson, and C. Gomez-Moreno. "Light-dependent de-activation/re-activation of Anabaena variabilis ferredoxin: NADP+ reductase." Biochemical Journal 274, no. 3 (1991): 781–86. http://dx.doi.org/10.1042/bj2740781.

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The activity of ferredoxin: NADP+ reductase (FNR) was found to decline to approximately 20% maximal levels with little or no loss in enzyme levels when cultures of the cyanobacterium Anabaena variabilis were maintained in the stationary phase of growth. Re-activation of enzyme activity occurred when cells were diluted into either fresh or re-utilized media and illuminated. This reversible de-activation/re-activation process was found, in vivo, to be dependent on the intensity of light illuminating the cells. The de-activated form of FNR was purified to homogeneity and exhibited the same molecu

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Arnold, Laurence H., Simone Kunzelmann, Martin R. Webb, and Ian A. Taylor. "A Continuous Enzyme-Coupled Assay for Triphosphohydrolase Activity of HIV-1 Restriction Factor SAMHD1." Antimicrobial Agents and Chemotherapy 59, no. 1 (2014): 186–92. http://dx.doi.org/10.1128/aac.03903-14.

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ABSTRACTThe development of deoxynucleoside triphosphate (dNTP)-based drugs requires a quantitative understanding of any inhibition, activation, or hydrolysis by off-target cellular enzymes. SAMHD1 is a regulatory dNTP-triphosphohydrolase that inhibits HIV-1 replication in human myeloid cells. We describe here an enzyme-coupled assay for quantifying the activation, inhibition, and hydrolysis of dNTPs, nucleotide analogues, and nucleotide analogue inhibitors by triphosphohydrolase enzymes. The assay facilitates mechanistic studies of triphosphohydrolase enzymes and the quantification of off-targ

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