Relevant bibliographies by topics / Zinc metalloenzyme

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Reports

Academic literature on the topic 'Zinc metalloenzyme'

Author: Grafiati
Published: 4 June 2021
Last updated: 20 February 2023

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Journal articles on the topic "Zinc metalloenzyme"

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Stoecker, Walter, Russell L. Wolz, Robert Zwilling, Daniel J. Strydom, and David S. Auld. "Astacus protease, a zinc metalloenzyme." Biochemistry 27, no. 14 (July 12, 1988): 5026–32. http://dx.doi.org/10.1021/bi00414a012.

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Vallee, B. L. "Zinc metalloenzyme structure and function." Journal of Inorganic Biochemistry 36, no. 3-4 (August 1989): 299. http://dx.doi.org/10.1016/0162-0134(89)84446-0.

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Haeggström, Jesper Z., Anders Wetterholm, Robert Shapiro, Bert L. Vallee, and Bengt Samuelsson. "Leukotriene A4 hydrolase: A zinc metalloenzyme." Biochemical and Biophysical Research Communications 172, no. 3 (November 1990): 965–70. http://dx.doi.org/10.1016/0006-291x(90)91540-9.

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Hadianawala, Murtuza, and Bhaskar Datta. "Design and development of sulfonylurea derivatives as zinc metalloenzyme modulators." RSC Advances 6, no. 11 (2016): 8923–29. http://dx.doi.org/10.1039/c5ra27341b.

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Millian, Norman S., and Timothy A. Garrow. "Human Betaine–Homocysteine Methyltransferase Is a Zinc Metalloenzyme." Archives of Biochemistry and Biophysics 356, no. 1 (August 1998): 93–98. http://dx.doi.org/10.1006/abbi.1998.0757.

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González, Julio C., Katrina Peariso, James E. Penner-Hahn, and Rowena G. Matthews. "Cobalamin-Independent Methionine Synthase fromEscherichia coli: A Zinc Metalloenzyme†." Biochemistry 35, no. 38 (January 1996): 12228–34. http://dx.doi.org/10.1021/bi9615452.

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Brothers, Edward N., Dimas Suarez, David W. Deerfield, and Kenneth M. Merz. "PM3-compatible zinc parameters optimized for metalloenzyme active sites." Journal of Computational Chemistry 25, no. 14 (2004): 1677–92. http://dx.doi.org/10.1002/jcc.20086.

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Tanaka, Tomoaki, and Eiji Ichishima. "Molecular properties of aminopeptidase ey as a zinc-metalloenzyme." International Journal of Biochemistry 25, no. 11 (November 1993): 1681–88. http://dx.doi.org/10.1016/0020-711x(93)90528-m.

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Shapir, Nir, Charlotte Pedersen, Omer Gil, Lisa Strong, Jennifer Seffernick, Michael J. Sadowsky, and Lawrence P. Wackett. "TrzN from Arthrobacter aurescens TC1 Is a Zinc Amidohydrolase." Journal of Bacteriology 188, no. 16 (August 15, 2006): 5859–64. http://dx.doi.org/10.1128/jb.00517-06.

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ABSTRACT TrzN, the broad-specificity triazine hydrolase from Arthrobacter and Nocardioides spp., is reportedly in the amidohydrolase superfamily of metalloenzymes, but previous studies suggested that a metal was not required for activity. To help resolve that conundrum, a double chaperone expression system was used to produce multimilligram quantities of functionally folded, recombinant TrzN. The TrzN obtained from Escherichia coli (trzN) cells cultured with increasing zinc in the growth medium showed corresponding increases in specific activity, and enzyme obtained from cells grown with 500 μ
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Álvarez-Santos, Silvia, Àngels González-Lafont, and José M. Lluch. "Effect of the hydrogen bond network in carbonic anhydrase II zinc binding site. A theoretical study." Canadian Journal of Chemistry 76, no. 7 (July 1, 1998): 1027–32. http://dx.doi.org/10.1139/v98-098.

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The hydrogen bond network influence on the carbonic anhydrase II (CAII) zinc binding site has been studied theoretically by using the semiempirical AM1 method. To this aim, quantum mechanical reduced models of wild-type CAII and several CAII variants have been constructed. We have shown that, when a direct metal ligand donates a hydrogen bond to an indirect metal ligand, the first-shell residues enhance their electrostatic interaction with the zinc cation. Thus, the hydrogen-bond network is able to modulate the zinc binding affinity and the zinc-water pKa.Key words: hydrogen bond network, carb
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Dissertations / Theses on the topic "Zinc metalloenzyme"

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Xie, Juan. "Synthèse, étude biologique et pharmacologique de nouveaux inhibiteurs des enzymes de dégradation des enképhalines." Paris 5, 1988. http://www.theses.fr/1988PA05P617.

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McMillen, Lyle, and l. mcmillen@sct gu edu au. "Isolation and Characterisation of the 5'-Nucleotidase from Escherichia coli." Griffith University. School of Biomolecular and Biomedical Science, 2001. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20030226.153545.

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Escherichia coli 5'-nucleotidase is a periplasmically localised enzyme capable of hydrolysing a broad range of substrates, including all 5'-ribo- and 5'-deoxyribonucleotides, uridine diphosphate sugars, and a number of synthetic substrates such as bis (r-nitrophenyl) phosphate. The enzyme has been shown to contain at least one zinc ion following purification, and to have two metal binding sites in the catalytic cleft. 5'-Nucleotidase activity is significantly stimulated by the addition of particular divalent metal ions, most notably cobalt which results in a 30-50 fold increase in activity.
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McMillen, Lyle. "Isolation and Characterisation of the 5'-Nucleotidase from Escherichia coli." Thesis, Griffith University, 2001. http://hdl.handle.net/10072/366487.

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Escherichia coli 5'-nucleotidase is a periplasmically localised enzyme capable of hydrolysing a broad range of substrates, including all 5'-ribo- and 5'-deoxyribonucleotides, uridine diphosphate sugars, and a number of synthetic substrates such as bis (r-nitrophenyl) phosphate. The enzyme has been shown to contain at least one zinc ion following purification, and to have two metal binding sites in the catalytic cleft. 5'-Nucleotidase activity is significantly stimulated by the addition of particular divalent metal ions, most notably cobalt which results in a 30-50 fold increase in activity.
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Myers, Andrew Ross. "Cloning, Expression, and Sequence Analysis of Camelysin, a Zinc Metalloprotease from Bacillus anthracis and B. cereus." [Tampa, Fla.] : University of South Florida, 2005. http://purl.fcla.edu/fcla/etd/SFE0001218.

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Nedonchelle, Elsa. "Les anticorps catalytiques : des outils pour la production et l'étude des anticorps catalytiques semi-synthétiques et auto-immuns." Compiègne, 2000. http://www.theses.fr/2000COMP1320.

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Les anticorps catalytiques associent les propriétés de reconnaissance des anticorps aux propriétés de catalyse des enzymes. Différentes approches ont été envisagées pour leur faire mimer les enzymes : analogues d'états de transition, copie du site actif par le réseau idiotypique, ingénierie des protéines. De nombreuses enzymes s'associent avec des métaux pour assurer leurs fonctions. Le zinc est un élément intéressant dans ce cas car retrouvé dans plus de 300 enzymes. Ces sites de fixation étant bien caractérisés, ils ont pu semir de modèle en biotechnologie dans l'ingénierie des protéines. L'
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Patil, Vishal. "Design and synthesis of small molecule inhibitors of zinc metalloenzymes." Diss., Georgia Institute of Technology, 2011. http://hdl.handle.net/1853/45859.

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Histone deacetylases (HDACs) are a class of enzymes that play a crucial role in DNA expression by removing an acetyl group from the ɛ-N-acetyl lysine residue on histone proteins. Out of 18 isoforms of HDAC enzymes which are classified into 4 classes, only 11 of them are metalloenzymes that require zinc for its catalytic activity. HDACs are considered promising target for drug development in cancer and other parasitic diseases due to their role in gene expression. Histone deacetylase inhibitors (HDACi) can cause cell cycle arrest, and induce differentiation or apotosis. While HDACi shows promis
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Salter, Michael H. "The study of models for zinc(II) metalloenzymes in aqueous solution /." Electronic version (PDF), 2003. http://dl.uncw.edu/etd/2003/salterm/michaelsalter.html.

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Pérez, Olmo Cristina. "Polar tris(pyrazolyl)borates for the modeling of zinc metalloenzymes in aqueous solution." [S.l.] : [s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=975035436.

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Camberlein, Virgyl. "Target-guided synthesis of metalloenzymes ligands with therapeutic applications." Thesis, Université de Lille (2022-....), 2022. http://www.theses.fr/2022ULILS004.

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La synthèse guidée par la cible de ligands protéiques est une stratégie innovante pour découvrir des composés bioactifs. En particulier, la Kinetic Target-Guided Synthesis (KTGS) and the Dynamic Combinatorial Chemistry (DCC) ont permis, ces dernières années, de découvrir des ligands originaux pour des cibles thérapeutiques mal explorées, ce qui a permis de lancer des projets de découverte de médicaments. Ce projet de thèse vise à utiliser la KTGS pour découvrir, puis optimiser des ligands de deux classes de métalloenzymes que sont les aminopeptidases du réticulum endoplasmiques (ERAP) et l’éla
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Debela, Mekdes Haile Mariam. "Crystal structures of the human tissue kallikreins 4, 5, 7, 10, characterisation of their substrate specificity and analysis of their various zinc inhibition mechanisms." München Verl. Dr. Hut, 2007. http://d-nb.info/988422395/04.

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Book chapters on the topic "Zinc metalloenzyme"

1

HaeggstrÖM, J. Z., A. Wetterholm, and B. Samuelsson. "Leukotriene A4 Hydrolase: A Zinc Metalloenzyme with Dual Enzymatic Activities." In Eicosanoids and Other Bioactive Lipids in Cancer, Inflammation and Radiation Injury, 39–42. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-3520-1_9.

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Breksa, Andrew P., and Timothy A. Garrow. "Betaine-Homocysteine S-Methyltransferase is an Abundant Zinc Metalloenzyme in Liver." In Trace Elements in Man and Animals 10, 1013–15. New York, NY: Springer US, 2002. http://dx.doi.org/10.1007/0-306-47466-2_311.

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Kamp, Marc Willem. "Zinc-Dependent Metalloenzymes – Computational Studies." In Encyclopedia of Biophysics, 2795–96. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_273.

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Jordan, Matthew R., Matias Villarruel Dujovne, Daiana A. Capdevila, and David P. Giedroc. "Metal ion homeostasis: Metalloenzyme paralogs in the bacterial adaptative response to zinc restriction." In Reference Module in Chemistry, Molecular Sciences and Chemical Engineering. Elsevier, 2022. http://dx.doi.org/10.1016/b978-0-12-823144-9.00161-8.

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"ZINC SITES IN METALLOENZYMES." In Handbook on Metalloproteins, 947–48. CRC Press, 2001. http://dx.doi.org/10.1201/9781482270822-102.

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"ZINC SITES IN METALLOENZYMES 951." In Handbook on Metalloproteins, 993–1022. CRC Press, 2001. http://dx.doi.org/10.1201/9781482270822-108.

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Berreau, Lisa M. "Kinetic and mechanistic studies of the reactivity of Zn–OHn (n=1 or 2) species in small molecule analogs of zinc-containing metalloenzymes." In Advances in Physical Organic Chemistry, 79–181. Elsevier, 2006. http://dx.doi.org/10.1016/s0065-3160(06)41002-9.

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Reports on the topic "Zinc metalloenzyme"

1

Balch, William. Purification and characterization of dihydroorotase from Clostridium oroticum, a zinc-containing metalloenzyme. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.1687.

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