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Relevant bibliographies by topics / Enzyme function

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Academic literature on the topic 'Enzyme function'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Enzyme function"

1

Dunaway-Mariano, Debra. "Enzyme Function Discovery." Structure 16, no. 11 (November 2008): 1599–600. http://dx.doi.org/10.1016/j.str.2008.10.001.

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Tan, Yong Quan, Bo Xue, and Wen Shan Yew. "Genetically Encodable Scaffolds for Optimizing Enzyme Function." Molecules 26, no. 5 (March 4, 2021): 1389. http://dx.doi.org/10.3390/molecules26051389.

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Enzyme engineering is an indispensable tool in the field of synthetic biology, where enzymes are challenged to carry out novel or improved functions. Achieving these goals sometimes goes beyond modifying the primary sequence of the enzyme itself. The use of protein or nucleic acid scaffolds to enhance enzyme properties has been reported for applications such as microbial production of chemicals, biosensor development and bioremediation. Key advantages of using these assemblies include optimizing reaction conditions, improving metabolic flux and increasing enzyme stability. This review summarizes recent trends in utilizing genetically encodable scaffolds, developed in line with synthetic biology methodologies, to complement the purposeful deployment of enzymes. Current molecular tools for constructing these synthetic enzyme-scaffold systems are also highlighted.

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Gerlt, John A., Karen N. Allen, Steven C. Almo, Richard N. Armstrong, Patricia C. Babbitt, John E. Cronan, Debra Dunaway-Mariano, et al. "The Enzyme Function Initiative." Biochemistry 50, no. 46 (November 22, 2011): 9950–62. http://dx.doi.org/10.1021/bi201312u.

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Romero, Philip A., Tuan M. Tran, and Adam R. Abate. "Dissecting enzyme function with microfluidic-based deep mutational scanning." Proceedings of the National Academy of Sciences 112, no. 23 (May 26, 2015): 7159–64. http://dx.doi.org/10.1073/pnas.1422285112.

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Natural enzymes are incredibly proficient catalysts, but engineering them to have new or improved functions is challenging due to the complexity of how an enzyme’s sequence relates to its biochemical properties. Here, we present an ultrahigh-throughput method for mapping enzyme sequence–function relationships that combines droplet microfluidic screening with next-generation DNA sequencing. We apply our method to map the activity of millions of glycosidase sequence variants. Microfluidic-based deep mutational scanning provides a comprehensive and unbiased view of the enzyme function landscape. The mapping displays expected patterns of mutational tolerance and a strong correspondence to sequence variation within the enzyme family, but also reveals previously unreported sites that are crucial for glycosidase function. We modified the screening protocol to include a high-temperature incubation step, and the resulting thermotolerance landscape allowed the discovery of mutations that enhance enzyme thermostability. Droplet microfluidics provides a general platform for enzyme screening that, when combined with DNA-sequencing technologies, enables high-throughput mapping of enzyme sequence space.

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Page, Michael J., and Enrico Di Cera. "Role of Na+and K+in Enzyme Function." Physiological Reviews 86, no. 4 (October 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 unexpected connections with ion transporters. Kinetic expressions are derived for the analysis of type I and type II activation. In conclusion, we address evolutionary implications of Na+binding in the trypsin-like proteases of vertebrate blood coagulation. From this analysis, M+complexation has the potential to be an efficient regulator of enzyme catalysis and stability and offers novel strategies for protein engineering to improve enzyme function.

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Duskey, Jason Thomas, Federica da Ros, Ilaria Ottonelli, Barbara Zambelli, Maria Angela Vandelli, Giovanni Tosi, and Barbara Ruozi. "Enzyme Stability in Nanoparticle Preparations Part 1: Bovine Serum Albumin Improves Enzyme Function." Molecules 25, no. 20 (October 9, 2020): 4593. http://dx.doi.org/10.3390/molecules25204593.

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Enzymes have gained attention for their role in numerous disease states, calling for research for their efficient delivery. Loading enzymes into polymeric nanoparticles to improve biodistribution, stability, and targeting in vivo has led the field with promising results, but these enzymes still suffer from a degradation effect during the formulation process that leads to lower kinetics and specific activity leading to a loss of therapeutic potential. Stabilizers, such as bovine serum albumin (BSA), can be beneficial, but the knowledge and understanding of their interaction with enzymes are not fully elucidated. To this end, the interaction of BSA with a model enzyme B-Glu, part of the hydrolase class and linked to Gaucher disease, was analyzed. To quantify the natural interaction of beta-glucosidase (B-Glu,) and BSA in solution, isothermal titration calorimetry (ITC) analysis was performed. Afterwards, polymeric nanoparticles encapsulating these complexes were fully characterized, and the encapsulation efficiency, activity of the encapsulated enzyme, and release kinetics of the enzyme were compared. ITC results showed that a natural binding of 1:1 was seen between B-Glu and BSA. Complex concentrations did not affect nanoparticle characteristics which maintained a size between 250 and 350 nm, but increased loading capacity (from 6% to 30%), enzyme activity, and extended-release kinetics (from less than one day to six days) were observed for particles containing higher B-Glu:BSA ratios. These results highlight the importance of understanding enzyme:stabilizer interactions in various nanoparticle systems to improve not only enzyme activity but also biodistribution and release kinetics for improved therapeutic effects. These results will be critical to fully characterize and compare the effect of stabilizers, such as BSA with other, more relevant therapeutic enzymes for central nervous system (CNS) disease treatments.

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BORMAN, STU. "PROBING ENZYME FUNCTION IN CELLS." Chemical & Engineering News 84, no. 44 (October 30, 2006): 12. http://dx.doi.org/10.1021/cen-v084n044.p012a.

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Mitchell, John BO. "Enzyme function and its evolution." Current Opinion in Structural Biology 47 (December 2017): 151–56. http://dx.doi.org/10.1016/j.sbi.2017.10.004.

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Crunkhorn, Sarah. "Enzyme inhibitor improves cognitive function." Nature Reviews Drug Discovery 13, no. 10 (September 19, 2014): 726. http://dx.doi.org/10.1038/nrd4452.

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Poulos, Thomas L. "Heme Enzyme Structure and Function." Chemical Reviews 114, no. 7 (January 8, 2014): 3919–62. http://dx.doi.org/10.1021/cr400415k.

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Dissertations / Theses on the topic "Enzyme function"

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Friemann, Rosmarie. "Structure-function studies of iron-sulfur enzyme systems /." Uppsala : Dept. of Molecular Biology, Swedish Univ. of Agricultural Sciences, 2005. http://epsilon.slu.se/a504.pdf.

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O'Neil, Crystal L. "Enzyme Exploitation: Manipulating Enzyme Function for Therapy, Synthesis and Natural Product Modification." The Ohio State University, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=osu1293722936.

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Gwozd, Chantelle Sabrina. "The structural basis of ubiquitin conjugating enzyme function." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/nq22989.pdf.

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Friemann, Rosmarie. "Structure-function studies of iron-sulfur enzyme systems /." Uppsala : Dept. of Molecular Biology, Swedish Univ. of Agricultural Sciences, 2004. http://epsilon.slu.se/a504-ab.html.

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Roden, D. L. "High specificity automatic function assignment for enzyme sequences." Thesis, University College London (University of London), 2011. http://discovery.ucl.ac.uk/1321566/.

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The number of protein sequences being deposited in databases is currently growing rapidly as a result of large-scale high throughput genome sequencing efforts. A large proportion of these sequences have no experimentally determined structure. Also, relatively few have high quality, specific, experimentally determined functions. Due to the time, cost and technical complexity of experimental procedures for the determination of protein function this situation is unlikely to change in the near future. Therefore, one of the major challenges for bioinformatics is the ability to automatically assign highly accurate, high-specificity functional information to these unknown protein sequences. As yet this problem has not been successfully solved to a level both acceptable in terms of detailed accuracy and reliability for use as a basis for detailed biological analysis on a genome wide, automated, high-throughput scale. This research thesis aims to address this shortfall through the provision and benchmarking of methods that can be used towards improving the accuracy of high-specificity protein function prediction from enzyme sequences. The datasets used in these studies are multiple alignments of evolutionarily related protein sequences, identified through the use of BLAST sequence database searches. Firstly, a number of non-standard amino acid substitution matrices were used to re-score the benchmark multiple sequence alignments. A subset of these matrices were shown to improve the accuracy of specific function annotation, when compared to both the original BLAST sequence similarity ordering and a random sequence selection model. Following this, two established methods for the identification of functional specificity determining amino acid residues (fSDRs) were used to identify regions within the aligned sequences that are functionally and phylogenetically informative. These localised sequence regions were then used to re-score the aligned sequences and provide an assessment of their ability to improve the specific functional annotation of the benchmark sequence sets. Finally, a machine learning approach (support vector machines) was followed to evaluate the possibility of identifying fSDRs, which improve the annotation accuracy, directly from alignments of closely related protein sequences without prior knowledge of their specific functional sub-types. The performance of this SVM based method was then assessed by applying it to the automatic functional assignment of a number of well studied classes of enzymes.

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Szeto, Michelle Wing Yan. "QM/MM studies of enzyme structure and function." Thesis, University of Bristol, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.445894.

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Liou, Geoffrey. "Enzyme structure, function, and evolution in flavonoid biosynthesis." Thesis, Massachusetts Institute of Technology, 2019. https://hdl.handle.net/1721.1/122067.

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This electronic version was submitted by the student author. The certified thesis is available in the Institute Archives and Special Collections.
Thesis: Ph. D., Massachusetts Institute of Technology, Department of Biology, 2019
Cataloged from student-submitted PDF version of thesis.
Includes bibliographical references.
Plant specialized metabolism is a key evolutionary adaptation that has enabled plants to migrate from water onto land and subsequently spread throughout terrestrial environments. Flavonoids are one particularly important class of plant specialized metabolites, playing a wide variety of roles in plant physiology including UV protection, pigmentation, and defense against herbivores and pathogens. Flavonoid diversity has increased in conjunction with land plant evolution over the past 470 million years. This dissertation examines the structure, function, and evolution of enzymes in the flavonoid biosynthetic pathway. First, we structurally and biochemically characterized orthologs of chalcone synthase (CHS), the enzyme that catalyzes the first step of flavonoid biosynthesis, from diverse plant lineages. By doing so, we gained insight into the sequence changes that gave rise to increased reactivity of the catalytic cysteine residue in CHS orthologs in euphyllophytes compared to basal land plants. We then developed methods and transgenic plant lines to study the in vivo function of these CHS orthologs, as well as whether their functional differences play a role in redox-based regulation of flavonoid biosynthesis. Finally, we examined enzymes involved in the biosynthesis of galloylated catechins, a highly enriched class of flavonoids in tea that are thought to have health benefits in humans. These findings contribute to an understanding of the evolution of enzyme structure and function in flavonoid biosynthesis, and how it has facilitated the adaptation of plants to a wide variety of terrestrial habitats.
by Geoffrey Liou.
Ph. D.
Ph.D. Massachusetts Institute of Technology, Department of Biology

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Ljungberg, Liza. "Angiotensin-converting enzyme in cardiovascular function and dysfunction." Doctoral thesis, Linköpings universitet, Fysiologi, 2011. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-67215.

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Angiotensin-converting enzyme (ACE) is a key enzyme in the renin-angiotensin system, converting angiotensin I to the vasoactive peptide angiotensin II, and degrading bradykinin. Angiotensin II is a multifunctional peptide, acting on a number of different tissues. A common genetic variation in the gene encoding ACE; ACE I/D polymorphism influences the level of ACE in the circulation, and has been linked to increased risk for cardiovascular disease. This thesis aimed to explore the connection between ACE and cardiovascular function and dysfunction. The impact of nicotine and nicotine metabolites on ACE in cultured human endothelial cells was studied. Nicotine as well as nicotine metabolites induced increased ACE activity in cultured human endothelial cells. In elderly men a higher ACE level was seen in smokers compared to non-smokers. Furthermore, diabetes was associated with higher circulating ACE. Increased ACE level may represent a cellular mechanism which contributes to vascular damage. Elderly men carrying the ACE D allele had higher abdominal aortic stiffness compared to men carrying the I/I genotype. Our data suggest that the mechanism by which the ACE D allele modulates aortic wall mechanics is independent of circulating ACE levels. Previous studies have indicated a link between the D allele and abdominal aortic aneurysm. Increased aortic stiffness suggests impaired vessel wall integrity, which combined with local hemodynamic and/or inflammatory factors may have a role in aneurysm formation. Subjects with left ventricular dysfunction had higher levels of circulating ACE compared to those with normal left ventricular function, while there was no association between ACE and central hemodynamics. ACE might play a role in the pathogenesis of left ventricular dysfunction and our findings suggest a direct effect on the heart rather than affecting central blood pressure.

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Khan, Amjad. "NMR spectroscopy studies of enzyme function and inhibition." Thesis, University of Oxford, 2016. https://ora.ox.ac.uk/objects/uuid:698d69c7-d4f1-4bc7-bf0b-3b9e7fb3a4fe.

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The work described in this Thesis focuses on the application of NMR spectroscopy methods in understanding the function and inhibition of two protein systems; these are ?-butyrobetaine hydroxylase (BBOX) and the bacterial potassium ion efflux (Kef) system. BBOX belongs to the super family of enzymes called the 2- oxoglutarate (2OG) and FeII dependent oxygenase and is involved in the biosynthesis of L-carnitine in humans and other prokaryotes. BBOX is a current drug target for the treatment of myocardial infarction. Kef is a ligandgated system that protects bacteria from toxic electrophilic species. Kef is inhibited by the binding of cytoplasmic glutathione (GSH) to KTN (K+ transport and nucleotide) binding domains and activated by glutathione-S-conjugates (GS-X). Since bacterial Kef activation during electrophilic exposure is a critical determinant of their survival, perturbation of Kef activity is potentially a novel target for the development of antibiotic drugs. 1H NMR direct ligand-observation was employed to study the binding interaction of the natural substrate ?- butyrobetaine (GBB) and co-substrate 2OG with BBOX. A 1H NMR-based dual-reporter ligand displacement method was developed to assess the nature of inhibitor binding to BBOX i.e to determine whether an inhibitor competes with GBB or 2OG or both. The method was exemplified with a set of isoquinoline-based inhibitors; the results reveal 'cystallographically unexpected' structure-activity relationship with some inhibitors competing 2OG only and some competing both 2OG and GBB. Using 1H NMR spectroscopy, a simple and efficient BBOX inhibition assay was developed for inhibitor IC50 measurement. Similarly, 1H NMR-based assays were applied to demonstrate that the cation-p interaction between the substrates and aromatic cage residues of BBOX play a critical role in BBOX substrate recognition. 1H NMR spectroscopy was applied to show that in the absence of a 2OG oxygenase, ascorbate in the assay mixture is slowly degraded by the dissolved oxygen to yield H2O2 which simultaneously leads to 2OG breakdown into succinate. It is proposed that in the assays of 2OG oxygenases, the apparent increase in the level of "uncoupled" 2OG turnover with ascorbate over time could possibly be due to the artifacts of the ascorbate induced-2OG breakdown instead of being due to enzyme catalysis. Other reducing agents were also found to oxidise identically by the dissolved oxygen as ascorbate in the mixture and result in 2OG breakdown. In the Kef system, 1H NMR direct ligand-observation was applied to investigate the influence of each functional group of the Kef activating ligand glutathione-S-N-tertiary butylsuccinimide on its binding interaction (KD 0.4 μM) with Kef-QCTD (Q-linker carboxy terminal domain; a KTN domain) from Shewanella denitrificans (sd) with the aim of developing novel non-peptidic ligands (antibacterial agents) of Kef. In addition, 19F NMR was employed to develop an efficient ligand-observed binding assay for Kef that was used for ligand screening as well as measuring their binding dissociation constant value from a single NMR spectrum. Finally, a 1H NMR technique was applied to confirm that the electron density found in the nucleotide binding pocket in the crystal structure of apo-sdKef-QCTD is unambiguously an AMP molecule that is naturally bound to the protein and has a role in stabilising the dimeric form of KTN domains (Kef proteins).

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Hamilton, Russell S. "DAROGAN : enzyme function prediction from multiple sequence alignments." Thesis, University of Edinburgh, 2006. http://hdl.handle.net/1842/14972.

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The function of an enzyme is often dependent on a few key functional residues and the principal objective of this project was to develop a novel function prediction system which takes advantage of this by comparing the conserved amino acids in known enzyme families to those in a putative enzyme. Multiple sequence alignments of well characterised enzyme families (with an E.C. number assigned) are used to create unordered sets of conserved functional residues, termed Treads. Comparison of a query proteins Tread to the reference Treads is undertaken by projecting them in multidimensional space and measuring distance between them. A major advantage of this prediction strategy implemented in DAROGAN is that it should be able to recognise similarities in the functions of enzymes that are not similar in structure or sequence. The method has been tested with regard to its ability to predict cofactor-dependencies toward pyridoxal-5’-phosphate, thiamine, glutathione and folic acid utilising enzymes. An area of application for DAROGAN is the prediction of previously described enzyme functions in organisms with completed genomes to which no gene and protein sequence could be assigned though the standard annotation processes. Investigations were made into the potential of utilising the DAROGAN method to propose candidates for the missing pyridoxal-5’-phosphate utilising enzymes in the E. coli genome according to EcoCyc. Candidates are proposed by assessing the 511 sequences from the GeneQuiz project, to which there are homologues in other species, but with uncertain functions. The assessment takes the form of using the DAROGAN method to determine the similarities of each of the sequences to the reference Treads.

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Books on the topic "Enzyme function"

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service), ScienceDirect (Online, ed. Structure, function and regulation of Tor complexes from yeasts to mammals. Amsterdam: Elsevier/Academic Press, 2010.

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Labrou, Nikolaos, ed. Therapeutic Enzymes: Function and Clinical Implications. Singapore: Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-13-7709-9.

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Stöcker, Walter, and Klaudia Brix. Proteases: Structure and function. Wien: Springer, 2013.

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Park, Kwan-Hwa. Carbohydrate-active enzymes: Structure, function and applications. Cambridge: Woodhead Publishing Ltd, 2008.

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Agricultural Biotechnology Symposium on "Carbohydrate-Active Enzymes: Structure, Function, and Applications" (2008 Seoul National University). Carbohydrate-active enzymes: Structure, function and applications. Boca Raton: CRC Press, 2008.

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Jono, Viviana. High-efficiency paper additives based on enzyme recognition functions. Ottawa: National Library of Canada, 2002.

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Roussel, Marc R. Functional equation methods in steady-state enzyme kinetics. Ottawa: National Library of Canada, 1990.

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Mu, Wanmeng, Wenli Zhang, and Qiuming Chen, eds. Novel enzymes for functional carbohydrates production. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-33-6021-1.

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Linder, Markus. Structure-function relationships in fungal cellulose-binding domains. Espoo, Finland: VTT, Technical Research Centre of Finland, 1996.

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Microbial production of food ingredients, enzymes and nutraceuticals. [S.l.]: Woodhead Publishing Limited, 2013.

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Book chapters on the topic "Enzyme function"

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Deshpande, S. S. "Antibodies: Biochemistry, Structure, and Function." In Enzyme Immunoassays, 24–51. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-1169-0_2.

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Rupley, John A., and Giorgio Careri. "Enzyme Hydration and Function." In The Enzyme Catalysis Process, 223–34. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4757-1607-8_15.

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von Schassen, Henrike, Jutta Keller, and Peter Layer. "METHODS AND PRINCIPLES OF PANCREATIC FUNCTION TESTS." In Enzyme Technologies, 335–39. Hoboken, NJ: John Wiley & Sons, Inc, 2013. http://dx.doi.org/10.1002/9781118739907.ch10.

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Buxbaum, Engelbert. "Enzyme Kinetics and Mechanism." In Fundamentals of Protein Structure and Function, 111–40. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-19920-7_5.

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Buxbaum, Engelbert. "Enzyme Kinetics: Special Cases." In Fundamentals of Protein Structure and Function, 185–91. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-19920-7_8.

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Gupta, M. N. "Enzyme function in organic solvents." In Interface between Chemistry and Biochemistry, 49–65. Basel: Birkhäuser Basel, 1995. http://dx.doi.org/10.1007/978-3-0348-9061-8_3.

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Gupta, Munishwar N. "Enzyme function in organic solvents." In EJB Reviews, 17–24. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-78046-2_2.

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Cooper, Alan, and David T. F. Dryden. "Thermodynamic Fluctuations and Function in Proteins." In The Enzyme Catalysis Process, 159–71. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4757-1607-8_12.

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Syed, Umar, and Golan Yona. "Enzyme Function Prediction with Interpretable Models." In Methods in Molecular Biology, 373–420. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-243-4_17.

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Barrio, Jorge R., N. Satyamurthy, M. Namavari, and G. Lacan. "Radiofluorinated Enzyme Probes of Dopaminergic Function." In Chemists’ Views of Imaging Centers, 419–24. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-9670-4_45.

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Conference papers on the topic "Enzyme function"

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PEGG, SCOTT C. H., SHOSHANA BROWN, SUNIL OJHA, CONRAD C. HUANG, THOMAS E. FERRIN, and PATRICIA C. BABBITT. "REPRESENTING STRUCTURE-FUNCTION RELATIONSHIPS IN MECHANISTICALLY DIVERSE ENZYME SUPERFAMILIES." In Proceedings of the Pacific Symposium. WORLD SCIENTIFIC, 2004. http://dx.doi.org/10.1142/9789812702456_0034.

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Lee, Bum Ju, and Keun Ho Ryu. "Feature Extraction from Protein Sequences and Classification of Enzyme Function." In 2008 International Conference on Biomedical Engineering And Informatics (BMEI). IEEE, 2008. http://dx.doi.org/10.1109/bmei.2008.341.

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Kumar, Chetan, Gang Li, and Alok Choudhary. "Enzyme Function Classification Using Protein Sequence Features and Random Forest." In 2009 3rd International Conference on Bioinformatics and Biomedical Engineering (iCBBE). IEEE, 2009. http://dx.doi.org/10.1109/icbbe.2009.5162790.

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Bum Ju Lee, Heon Gyu Lee, and Keun Ho Ryu. "Design of a Novel Protein Feature and Enzyme Function Classification." In 2008 IEEE 8th International Conference on Computer and Information Technology Workshops. CIT Workshops 2008. IEEE, 2008. http://dx.doi.org/10.1109/cit.2008.workshops.59.

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"REACTION KERNELS - Structured Output Prediction Approaches for Novel Enzyme Function." In International Conference on Bioinformatics. SciTePress - Science and and Technology Publications, 2010. http://dx.doi.org/10.5220/0002741700480055.

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Lee, Hyeseung, Dean Ho, Benjamin Chu, Karen Kuo, and Carlo Montemagno. "Reconstituting Membrane Proteins Into Artificial Membranes and Detection of Their Activities." In ASME 2004 3rd Integrated Nanosystems Conference. ASMEDC, 2004. http://dx.doi.org/10.1115/nano2004-46016.

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We have successfully purified BR from purple membrane of Halobacterium Salinarium and Cox from the genetically engineered plasmid inserted in Rhodobacter Sphaeroides. The activities of the purified enzymes have shown in lipid vesicles as well as in polymer vesicles and planar membranes. Phosphatidylcholine derived lipid vesicles created the most nature like environment for the enzymes. Triblock copolymer membrane was the alternative choice for membrane protein reconstitution since polymers are more durable, ideal for industrial applications and support enzyme activities better. We also demonstrated the backward function of Cox in vitro by changing proton concentration in the surrounding medium. Langmuir-Blodgett method was used to reconstitute the enzymes into the planar lipid or polymer membranes. The enzyme activities of the enzymes in planar membrane system were tested by impedance spectroscopy.

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Lee, Bum Ju, Heon Gu Lee, Jong Yun Lee, and Keun Ho Ryu. "Classification of Enzyme Function from Protein Sequence based on Feature Representation." In 2007 IEEE 7th International Symposium on BioInformatics and BioEngineering. IEEE, 2007. http://dx.doi.org/10.1109/bibe.2007.4375643.

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Asmussen, Sven, Eva Bartha, Yusuke Yamamoto, Hiroshi Ito, Robert A. Cox, Hal K. Hawkins, Perenlei Enkhbaatar, Lilian D. Traber, Daniel L. Traber, and Csaba Szabo. "Angiotensin Converting Enzyme Inhibitor Treatment Influences Cardiopulmonary Function In Ovine Acute Lung Injury." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5232.

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Ribeiro, António, Gemma Holliday, Nicholas Furnham, and Janet Thornton. "Using the Mechanism and Catalytic Site Atlas (M-CSA) to understand enzyme function and evolution." In MOL2NET 2017, International Conference on Multidisciplinary Sciences, 3rd edition. Basel, Switzerland: MDPI, 2017. http://dx.doi.org/10.3390/mol2net-03-05078.

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

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Calmodulin (CaM)-binding proteins have been identified in human platelets using Western blotting techniques and 125I-CaM. Ten proteins of 245, 225. 175, 150, 90. 82(2), 60 and 41(2) kilodaltons (kDa) bind 125I-CaM in a Ca2+-dependent manner; the binding is blocked by both trifluoperazine and nonradiolabeled CaM. The 225 and 90 kDa proteins are labeled by antisera against myosin light chain kinase (MLCK); the 60 kDa and one of the 82 kDa proteins have been identified as the CaM-dependent phosphatase (calcineurin) and caldesmon. The other proteins are presumed to be other Ca2+/CaM regulated enzymes and proteins which may be important in platelet function. Most of the CaM-binding proteins are degraded upon addition of Ca2+ to a platelet homogenate; the degradation may be blocked by either EGTA, leupeptin or N-ethylmaleimide which suggests that the degradation is due to a Ca2+-dependent protease. Activation of intact platelets under conditions which promote platelet aggregation (i.e. stirring with extracellular Ca2+) also results in limited proteolysis of CaM-binding proteins including those labeled with anti sera against MLCK and the phosphatase. In vitro studies utilizing purified phosphatase and calpain I indicate that the phosphatase is irreversibly activated upon Ca2+-dependent proteolysis. The proteolytically-activated enzyme is insensitive to either Ca2+ or Ca2+/CaM; in addition, its activity in the absence of Ca2+ is even greater than the activity of the unproteolyzed enzyme in the presence of Ca2+ and CaM. Proteolytic stimulation of the phosphatase is accompanied by degradation of the 60 kDa subunit of the enzyme (subunit A) to 56, 52 and 45 kDa fragments, sequentially; proteolysis results in the loss of CaM binding to the enzyme. These results suggest that the Ca2+-dependent protease may have a physiological role in platelet activation as an irreversible activator of Ca2+/ CaM-dependent reactions. Supported by NIH grant HL29766.

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Reports on the topic "Enzyme function"

1

McCarty, Perry L., Alfred M. Spormann, and Craig S. Criddle. Biodegradation of Chlorinated Solvents: Reactions near DNAPL and Enzyme Function. Office of Scientific and Technical Information (OSTI), June 2001. http://dx.doi.org/10.2172/833505.

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2

McCarty, Perry L., Alfred M. Spormann, and Craig S. Criddle. Biodegradation of Chlorinated Solvents: Reactions near DNAPL and Enzyme Function. Office of Scientific and Technical Information (OSTI), June 2003. http://dx.doi.org/10.2172/833508.

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3

McCarty, P. L., Alfred M. Spormann, and Craig, S. Criddle. Biodegradation of Chlorinated Solvents: Reactions near DNAPL and Enzyme Function. Office of Scientific and Technical Information (OSTI), December 2003. http://dx.doi.org/10.2172/820096.

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4

McCarty, Perry L., Alfred M. Spormann, and Craig S. Criddle. Biodegradation of Chlorinated Solvents: Reactions near DNAPL and Enzyme Function. Office of Scientific and Technical Information (OSTI), June 2002. http://dx.doi.org/10.2172/833507.

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5

Jack Preiss. Structure Function Relationships of ADP-Glucose Pyrophosphorylase and Branching Enzyme: Manipulation of Their Genes for Alteration of Starch Quanlity and Quantity. Office of Scientific and Technical Information (OSTI), February 2006. http://dx.doi.org/10.2172/876435.

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Leech, Anna, and Jeremy Walker. Development of Enzyme-Containing Functional Nanoparticles. Fort Belvoir, VA: Defense Technical Information Center, August 2012. http://dx.doi.org/10.21236/ada564802.

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Geiger, Jim. Structure, function and regulation of the enzymes in the starch biosynthetic pathway. Office of Scientific and Technical Information (OSTI), November 2013. http://dx.doi.org/10.2172/1164083.

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8

Computer Simulations Reveal Multiple Functions for Aromatic Residues in Cellulase Enzymes (Fact Sheet). Office of Scientific and Technical Information (OSTI), July 2012. http://dx.doi.org/10.2172/1046309.

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