Relevant bibliographies by topics / Enzyme structure/function

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Enzyme structure/function'

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

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Journal articles on the topic "Enzyme structure/function"

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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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Latip, Wahhida, Victor Feizal Knight, Norhana Abdul Halim, Keat Khim Ong, Noor Azilah Mohd Kassim, Wan Md Zin Wan Yunus, Siti Aminah Mohd Noor, and Mohd Shukuri Mohamad Ali. "Microbial Phosphotriesterase: Structure, Function, and Biotechnological Applications." Catalysts 9, no. 8 (August 7, 2019): 671. http://dx.doi.org/10.3390/catal9080671.

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The role of phosphotriesterase as an enzyme which is able to hydrolyze organophosphate compounds cannot be disputed. Contamination by organophosphate (OP) compounds in the environment is alarming, and even more worrying is the toxicity of this compound, which affects the nervous system. Thus, it is important to find a safer way to detoxify, detect and recuperate from the toxicity effects of this compound. Phosphotriesterases (PTEs) are mostly isolated from soil bacteria and are classified as metalloenzymes or metal-dependent enzymes that contain bimetals at the active site. There are three separate pockets to accommodate the substrate into the active site of each PTE. This enzyme generally shows a high catalytic activity towards phosphotriesters. These microbial enzymes are robust and easy to manipulate. Currently, PTEs are widely studied for the detection, detoxification, and enzyme therapies for OP compound poisoning incidents. The discovery and understanding of PTEs would pave ways for greener approaches in biotechnological applications and to solve environmental issues relating to OP contamination.
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Sakiyama, Fumio. "Modification of enzyme structure and function." Kobunshi 35, no. 10 (1986): 950–53. http://dx.doi.org/10.1295/kobunshi.35.950.

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Hatzimanikatis, Vassily, Chunhui Li, Justin A. Ionita, and Linda J. Broadbelt. "Metabolic networks: enzyme function and metabolite structure." Current Opinion in Structural Biology 14, no. 3 (June 2004): 300–306. http://dx.doi.org/10.1016/j.sbi.2004.04.004.

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Thornton, Janet. "THE EVOLUTION OF ENZYME STRUCTURE AND FUNCTION." Biochemical Society Transactions 28, no. 3 (June 1, 2000): A53. http://dx.doi.org/10.1042/bst028a053.

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Kuriki, Takashi, Han-Ping Guan, and Jack Preiss. "Structure and Function of Starch Branching Enzyme." Journal of the agricultural chemical society of Japan 68, no. 11 (1994): 1581–84. http://dx.doi.org/10.1271/nogeikagaku1924.68.1581.

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von Grotthuss, M., D. Plewczynski, G. Vriend, and L. Rychlewski. "3D-Fun: predicting enzyme function from structure." Nucleic Acids Research 36, Web Server (May 19, 2008): W303—W307. http://dx.doi.org/10.1093/nar/gkn308.

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Carroll, Joanne M., Kwang Soo Kim, M. Elizabeth Ross, Marian J. Evinger, Soonjung L. Hahn, and Tong H. Joh. "Structure and function of catecholamine enzyme genes." Journal of the Autonomic Nervous System 33, no. 2 (May 1991): 129–30. http://dx.doi.org/10.1016/0165-1838(91)90160-5.

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ALDERTON, Wendy K., Chris E. COOPER, and Richard G. KNOWLES. "Nitric oxide synthases: structure, function and inhibition." Biochemical Journal 357, no. 3 (July 25, 2001): 593–615. http://dx.doi.org/10.1042/bj3570593.

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This review concentrates on advances in nitric oxide synthase (NOS) structure, function and inhibition made in the last seven years, during which time substantial advances have been made in our understanding of this enzyme family. There is now information on the enzyme structure at all levels from primary (amino acid sequence) to quaternary (dimerization, association with other proteins) structure. The crystal structures of the oxygenase domains of inducible NOS (iNOS) and vascular endothelial NOS (eNOS) allow us to interpret other information in the context of this important part of the enzyme, with its binding sites for iron protoporphyrin IX (haem), biopterin, l-arginine, and the many inhibitors which interact with them. The exact nature of the NOS reaction, its mechanism and its products continue to be sources of controversy. The role of the biopterin cofactor is now becoming clearer, with emerging data implicating one-electron redox cycling as well as the multiple allosteric effects on enzyme activity. Regulation of the NOSs has been described at all levels from gene transcription to covalent modification and allosteric regulation of the enzyme itself. A wide range of NOS inhibitors have been discussed, interacting with the enzyme in diverse ways in terms of site and mechanism of inhibition, time-dependence and selectivity for individual isoforms, although there are many pitfalls and misunderstandings of these aspects. Highly selective inhibitors of iNOS versus eNOS and neuronal NOS have been identified and some of these have potential in the treatment of a range of inflammatory and other conditions in which iNOS has been implicated.
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Watschinger, Katrin, Julian E. Fuchs, Vladimir Yarov-Yarovoy, Markus A. Keller, Georg Golderer, Albin Hermetter, Gabriele Werner-Felmayer, Nicolas Hulo, and Ernst R. Werner. "First insights into structure-function relationships of alkylglycerol monooxygenase." Pteridines 24, no. 1 (June 1, 2013): 99–103. http://dx.doi.org/10.1515/pterid-2013-0007.

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AbstractAlkylglycerol monooxygenase is a tetrahydrobiopterin-dependent enzyme that cleaves the O-alkyl-bond of alkylglycerols. It is an exceptionally unstable, hydrophobic membrane protein which has never been purified in active form. Recently, we were able to identify the sequence of alkylglycerol monooxygenase. TMEM195, the gene coding for alkylglycerol monooxygenase, belongs to the fatty acid hydroxylases, a family of integral membrane enzymes which have an 8-histidine motif crucial for catalysis. Mutation of each of these residues resulted in a complete loss of activity. We now extended the mutational analysis to another 25 residues and identified three further residues conserved throughout all members of the fatty acid hydroxylases which are essential for alkylglycerol monooxygenase activity. Furthermore, mutation of a specific glutamate resulted in an 18-fold decreased affinity of the protein to tetrahydrobiopterin, strongly indicating a potential important role in cofactor interaction. A glutamate residue in a comparable amino acid surrounding had already been shown to be responsible for tetrahydrobiopterin binding in the aromatic amino acid hydroxylases. Ab initio modelling of the enzyme yielded a structural model for the central part of alkylglycerol monooxygenase where all essential residues identified by mutational analysis are in close spatial vicinity, thereby defining the potential catalytic site of this enzyme.
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Dissertations / Theses on the topic "Enzyme structure/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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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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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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Brokx, Stephen John. "Structure and function of enzyme I of the PTS." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0029/NQ63848.pdf.

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Harris, Katharine Morse. "Studies of structure, function and mechanism in pyrimidine nucleotide biosynthesis." Thesis, Boston College, 2012. http://hdl.handle.net/2345/2594.

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Thesis advisor: Evan R. Kantrowitz
Thesis advisor: Mary F. Roberts
Living organisms depend on enzymes for the synthesis using small molecule precursors of cellular building blocks. For example, the amino acid aspartate is synthesized in one step by the amination of oxaloacetate, an intermediate compound produced in the citric acid cycle, exclusively by means of an aminotransferase enzyme. Therefore, function of this aminotransferase is critical to produce the amino acid. In the Kantrowitz Lab, we seek to understand the molecular rational for the function of enzymes that control rates for the biosynthesis of cellular building blocks. If one imagines the above aspartate-synthesis example as a single running conveyer belt, any oxaloacetate that finds its way onto that belt will be chemically transformed to give aspartate. We can extend this notion of a conveyer belt to any enzyme. Therefore, the rate at which the belt moves dictates the rate of synthesis. Now imagine many, many conveyer belts lined in a row to give analogy to a biosynthesis pathway requiring more than one enzyme for complete chemical synthesis. This is such the case for the biosynthesis of nucleotides and glucose. Nature has developed clever tricks to exquisitely control the rate of product output but means of altering the rate of one or some of the belts in the line of many, without affecting the rate of others. This type of biosynthetic rate regulation is termed allostery. Studies described in this dissertation will address questions of allosteric processes and the chemistry performed by two entirely different enzymes and biosynthetic pathways. The first enzyme of interest is fructose-1,6-bisphosphatase (FBPase) and its role in the biosynthesis of glucose. Following FBPase introduction in Chapter One, Chapter Two describes the minimal atomic scaffold necessary in a new class of allosteric type 2 diabetes drug molecules to effect catalytic inhibition of Homo sapiens FBPase. Following, is the second enzyme of interest, aspartate transcarbamoylase (ATCase) and its role in the biosynthesis of pyrimidine nucleotides. Succeeding ATCase introduction in Chapter Three, Chapter Four describes a body of work exclusively about the catalysis by ATCase. This work was inspired by the human form of the enzyme following the human genome project completion providing data that show likely Homo sapiens ATCase is not allosterically regulated. Chapter Five describes work on a allosterically-regulated, mutant ATCase and provides a biochemical model for the molecular rational for the catalytic inhibition upon cytidine triphosphate (CTP) binding to the allosteric site. The experimental techniques used for answering research questions were enzyme X-ray crystallography, in silico docking, kinetic assay experiments, genetic sub-cloning and genetic mutation
Thesis (PhD) — Boston College, 2012
Submitted to: Boston College. Graduate School of Arts and Sciences
Discipline: Chemistry
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Loftus, Katherine Marie. "Studies of the Structure and Function of E.coli Aspartate Transcarbamoylase." Thesis, Boston College, 2006. http://hdl.handle.net/2345/580.

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Thesis advisor: Evan R. Kantrowitz
E.coli Aspartate transcarbamoylase (ATCase) is the allosteric enzyme that catalyzes the committed step of the de novo pyrimidine biosynthesis pathway. ATCase facilitates the reaction between L-aspartate and carbamoyl phosphate to form N-carbamoyl-L-aspartate and inorganic phosphate. The holoenzyme is a dodecamer, consisting of two trimers of catalytic chains, and three dimers of regulatory chains. ATCase is regulated homotropically by its substrates, and heterotropically by the nucleotides ATP, CTP, and UTP. These nucleotides bind to the regulatory chains, and alter the activity of the enzyme at the catalytic site. ATP activates the rate of ATCase's reaction, while CTP inhibits it. Additionally, UTP and CTP act together to inhibit the enzyme synergistically, each nucleotide enhancing the inhibitory effects of the other. Two classes of CTP binding sites have been observed, one class with a high affinity for CTP, and one with a low affinity. It has been theorized that the asymmetry of the binding sites is intrinsic to each of the three regulatory dimers. It has been hypothesized that the second observed class of CTP binding sites, are actually sites intended for UTP. To test this hypothesis, and to gain more information about heterotropic regulation of ATCase and signal transmission in allosteric enzymes, the construction of a hybrid regulatory dimer was proposed. In the successfully constructed hybrid, each of the three regulatory dimers in ATCase would contain one regulatory chain with compromised nucleotide binding. This project reports several attempts at constructing the proposed hybrid, but ultimately the hybrid enzyme was not attained. This project also reports preliminary work on the characterization of the catalytic chain mutant D141A. This residue is conserved in ATCase over a wide array of species, and thus was mutated in order to ascertain its significance
Thesis (BS) — Boston College, 2006
Submitted to: Boston College. College of Arts and Sciences
Discipline: Chemistry
Discipline: College Honors Program
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Charnock, Simon James. "Structure/function analysis of a family 10 glycosol hydrolase." Thesis, University of Newcastle upon Tyne, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.262920.

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Luu, Luong. "Structure/function studies of hP450RAI, a retinoic acid metabolizing enzyme." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp01/MQ36051.pdf.

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Chang, Cheng-Fu. "Structure-function and regulation studies of angiotensin-converting enzyme 2." Doctoral thesis, University of Cape Town, 2009. http://hdl.handle.net/11427/3122.

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Books on the topic "Enzyme structure/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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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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Linder, Markus. Structure-function relationships in fungal cellulose-binding domains. Espoo, Finland: VTT, Technical Research Centre of Finland, 1996.

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Koivula, Anu. Structure-function studies of two polysaccharide-degrading enzymes: Bacillus strearothermophilus Ü-amylase and trichoderma reesei cellobiohydrolase II. Espoo: VTT, Technical Research Centre of Finland, 1996.

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Georgiev, Bojidor. Serpins and protein kinase inhibitors: Novel functions, structural features and molecular mechanisms. New York: Nova Science Publishers, 2010.

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Sliz, Piotr. Structure, function and interactions of enzyme IIA from the phosphoenolpyruvate: Lactose phosphotransferase system. 2000.

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Relationships between structure and function of Cytochrome P-450: Experiments, calculations, models. Berlin: Akademie Verlag, 1992.

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Clarke, Andrew. Temperature and reaction rate. Oxford University Press, 2017. http://dx.doi.org/10.1093/oso/9780199551668.003.0007.

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All other things being equal, physiological reaction rate increases roughly exponentially with temperature. Organisms that have adapted over evolutionary time to live at different temperatures can have enzyme variants that exhibit similar kinetics at the temperatures to which they have adapted to operate. Within species whose distribution covers a range of temperatures, there may be differential expression of enzyme variants with different kinetics across the distribution. Enzymes adapted to different optimum temperatures differ in their amino acid sequence and thermal stability. The Gibbs energy of activation tends to be slightly lower in enzyme variants adapted to lower temperatures, but the big change is a decrease in the enthalpy of activation, with a corresponding change in the entropy of activation, both associated with a more open, flexible structure. Despite evolutionary adjustments to individual enzymes involved in intermediary metabolism (ATP regeneration), many whole-organism processes operate faster in tropical ectotherms compared with temperate or polar ectotherms. Examples include locomotion (muscle power output), ATP regeneration (mitochondrial function), nervous conduction and growth.
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Book chapters on the topic "Enzyme structure/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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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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Douzou, Pierre, and Gaston Hui Bon Hoa. "Single Step Kinetics of Enzyme Dynamics." In Structure, Dynamics and Function of Biomolecules, 86–92. Berlin, Heidelberg: Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-71705-5_19.

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Choudhary, Devendra K., and Ajit Varma. "Nitrogenase (a Key Enzyme): Structure and Function." In Soil Biology, 293–307. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-64982-5_14.

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Wong, Chung F., and J. Andrew McCammon. "Thermodynamics of Enzyme Folding and Activity: Theory and Experiment." In Structure, Dynamics and Function of Biomolecules, 51–55. Berlin, Heidelberg: Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-71705-5_12.

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Taylor, Susan S., José Bubis, Janusz Sowadski, Jean A. Toner, and Lakshmi D. Saraswat. "Relation Between Structure and Function in cAMP-Dependent Protein Kinases." In Enzyme Dynamics and Regulation, 327–41. New York, NY: Springer New York, 1988. http://dx.doi.org/10.1007/978-1-4612-3744-0_38.

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Hedrick, Jerry L., Umbert A. Urch, and Daniel M. Hardy. "Structure—Function Properties of the Sperm Enzyme Acrosin." In ACS Symposium Series, 215–29. Washington, DC: American Chemical Society, 1989. http://dx.doi.org/10.1021/bk-1989-0389.ch015.

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Clark, Douglas S., Louise Creagh, Paul Skerker, Mark Guinn, John Prausnitz, and Harvey Blanch. "Enzyme Structure and Function in Water-Restricted Environments." In ACS Symposium Series, 104–14. Washington, DC: American Chemical Society, 1989. http://dx.doi.org/10.1021/bk-1989-0392.ch008.

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Pavlovic, Mirjana. "Proteomics: Enzyme: Structure, Function, Kinetics, and Engineering Aspects." In Bioengineering, 49–55. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-10798-1_5.

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Conference papers on the topic "Enzyme structure/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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Suzuki, Koji, Yoshihiro Deyashiki, Junji Nishioka, Kazunori Toma, and Shuji Yamamoto. "THE INHIBITOR OF ACTIVATED PROTEIN C: STRUCTURE AND FUNCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642963.

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In the final step of protein C pathway, activated protein C (APC) is neutralized with a plasma inhibitor, termed protein C inhibitor (PCI). PCI was first described by Marlar and Griffin (1980) and then isolated from human plasma as a homogeneous form and characterized by the authors (1983). PCI is a single chain glycoprotein with M 57,000 and a plasma concentration of 5 ug/ml. Analysis of a cDNA nucleotide sequence has clarified that a precursor of human PCI consists of a mature protein of 387 amino acid residues (M 43,759) and a signal peptide of 19 amino acid residues. Only one cysteine residue is present in the entire protein as in α1antitrypsin (α1AT) and α1antichymotrypsin (α1ACT). Three Asn-X-Ser/Thr sequences and two Ser/Thr-X-X-Pro sequences are present as potential attachment sites of carbohydrate chains. Based on the amino acid sequence of the carboxyl-terminal peptide released from the inhibitor by APC digestion, the reactive site peptide bond of PCI was found to be Arg(354)-Ser(355). It is similar to the reactive sites of the other serine protease inhibitors which are located to their carboxyl-terminal Arg(393)-Ser (394), Met(358)-Ser(359) and Leu(358)-Ser(359) in antithrombin III, α1AT and α1ACT, respectively. The alignment of the amino acid sequence of PCI with heparin cofactor II, α1plasmin inhibitor, ovalbumin, angiotensinogen and the above noted plasma inhibitors showed that PCI is a member of serine protease inhibitor superfamily. PCI inhibits APC noncompetitively in a 1:1 stoichiometry and forms a covalent acyl-bond with a Ser residue in the active center of APC. The half life of APC in plasma approximately 30 min, which is rather slow compared with the other protease inhibitors. However, optimal concentrations of heparin, dextran sulfate and its derivatives potentiate the rate of inhibition 30-60 fold. PCI has Ki of 10-8m for APC, and can inhibit thrombin, Factor Xa, urokinase and tissue plasminogen activator as well in the presence of heparin or dextran sulfate, though the Ki for these enzymes is slightly higher. During the complex formation with APC, PCI is cleaved by the complexed APC to form a modified form with M 54,000. PCI is synthesized in several hepatoma cell lines and decreased in plasma of patients with liver cirrhosis. It is also decreased in patients with DIC or those during cardiopulmonary bypass in parallel with the decrease in protein C, suggesting that PCI participates in regulation of the protein C pathway in intravascular coagulation. Recently, we have obtained the recombinant PCI from COS-1 cells which were transfected with expression vector pSV2 containing the cDNA of PCI. The recombinant PCI had the same Mr and specific activity as the protein purified from plasma. It also had an affinity for heparin and dextran sulfate. Moreover, we have predicted a three dimentional structure of the proteolytically modified PCI with computer graphics based on its amino acid sequence homology with the modified α1AT whose structure had been elucidated with X-ray crystallography. All potential carbohydrate attachment sites were estimated to exist on the surface of the protein. Succesively we have constructed the interaction model between the intact PCI predicted from the modified form and the active center of APC which was simulated from that of trypsin. From the model, it was observed that the amino-group of Arg (354, PI site) of PCI could strongly interact with the carboxy1-group of Asp (88, SI site) of the heavy chain of APC at the base of the active center pocket of the enzyme.
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Ventetuolo, Corey E., Emilia Bagiella, R. G. Barr, David A. Bluemke, Michael R. Bristow, Harjit Chahal, Jorge Kizer, David J. Lederer, Joao A. C. Lima, and Steven M. Kawut. "Angiotensin-Converting Enzyme Inhibitor And Angiotensin II Receptor Blocker Use And Right Ventricular Structure And Function: The MESA-Right Ventricle Study." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a4854.

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Hong, Huang Chun, Hu Tian, Wu Xin Yin, Jie Ke Ming, Yan Nian long, and Ying Mu Ying. "Structure and function of ubiquitin-conjugating enzymes." In International conference on Human Health and Medical Engineering. Southampton, UK: WIT Press, 2014. http://dx.doi.org/10.2495/hhme130411.

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Sandgren, M., P. Gualfetti, A. Day, L. Gross, M. L. Saldajeno, C. Mitchinson, T. A. Jones, and A. Shaw. "STRUCTURE AND FUNCTION ANALYSIS OF CELL2A ENZYMES." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.761.

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Temiyasathit, Sara, Ronald Y. Kwon, Padmaja Tummala, Clarence C. Quah, and Christopher R. Jacobs. "Adenylyl Cyclase 6 Mediates Primary Cilia-Dependent Changes in Cyclic Adenosine Monophosphate in Response to Dynamic Fluid Flow." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206200.

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It is well accepted that fluid flow is an important mechanical signal in regulating bone structure and function. Primary cilia, which are solitary, microtubule-based organelles that extend from the centrosome into extracellular space in many cell types, have been shown to mediate fluid flow-induced osteogenic responses in MLO-Y4 osteocyte-like cells [1], however, primary cilia did not mediate increases in intracellular Ca2+ concentration [1]. Recently, we identified cAMP as a novel early signaling molecule in primary cilia-dependent mechanotransduction of fluid flow in osteocytes. Specifically, we show that MLO-Y4 osteocyte-like cells respond to oscillatory flow with a rapid decrease in intracellular levels of cAMP that is dependent on the primary cilium [2]. Adenylyl cyclase 6 (AC6) is an enzyme responsible for the synthesis of cAMP from ATP. We found that AC 6 localizes to the primary cilium of bone cells (Fig. 1). In this study, our goal was to determine whether AC6 mediates the primary cilia-dependent, flow-induced decrease in cAMP.
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Mehner, Philipp J., Anthony Beck, Mathias Busek, Andreas Voigt, Uwe Marschner, and Andreas Richter. "Description of a Hydrogel-Based Micro-Valve As a Library Element for Matlab Simulink." In ASME 2019 Conference on Smart Materials, Adaptive Structures and Intelligent Systems. American Society of Mechanical Engineers, 2019. http://dx.doi.org/10.1115/smasis2019-5614.

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Abstract We propose a planar hydrogel-based micro-valve design which is modeled as a library element for Matlab Simulink. For this test case, a pressure pump (voltage source) in series with a micro-valve model (variable fluidic resistance) is built up. The micro-valve subsystem is separated in four main parts. Based on the applied temperature stimulus, the equilibrium length is determined according to an experimentally verified fit function. Furthermore, the equilibrium length considers a static hysteresis effect which is modeled in analogy to the saturation of magnetization in electric transformers. In a second step, the transient behavior follows a first order differential equation, but the cooperate diffusion coefficient is size dependent affecting the rise time of the system. This causes a faster swelling than deswelling of the hydrogel. In the third section, the stiffness property is implemented to calculate the maximum sealing pressure and the resulting gap between the hydrogel and the wall. The fluidic resistance of the micro-valve considers a three-dimensional geometry and is calculated based on a look-up table, extracted from a fluid-structure-interaction (FSI) model generated from a finite element structure. The proposed model allows a full description of the fluidic hydrogel-based micro-valve and is part of an upcoming microfluidic toolbox for Matlab Simulink containing passive elements and optional chemical reactions like mixing fluids and enzyme reactions for future applications.
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Zhang, Nanyan, Jining Xie, and Vijay K. Varadan. "Functional carbon nanotube material-based enzyme biosensors for glucose sensing." In Smart Structures and Materials, edited by Vijay K. Varadan. SPIE, 2005. http://dx.doi.org/10.1117/12.608143.

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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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Jedrzejas, Mark J. "STRUCTURE AND FUNCTION OF POLYSACCHARIDE DEGRADING ENZYMES: DEGRADATION OF HYALURONAN." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.444.

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Reports on the topic "Enzyme structure/function"

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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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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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