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 μM zinc showed maximum activity. Recombinant TrzN contained 1 mole of Zn per mole of TrzN subunit. Maximally active TrzN was not affected by supplementation with most metals nor by EDTA, consistent with previous observations (E. Topp, W. M. Mulbry, H. Zhu, S. M. Nour, and D. Cuppels, Appl. Environ. Microbiol. 66:3134-3141, 2000) which had led to the conclusion that TrzN is not a metalloenzyme. Fully active native TrzN showed a loss of greater than 90% of enzyme activity and bound zinc when treated with the metal chelator 8-hydroxyquinoline-5-sulfonic acid. While exogenously added zinc or cobalt restored activity to metal-depleted TrzN, cobalt supported lower activity than did zinc. Iron, manganese, nickel, and copper did not support TrzN activity. Both Zn- and Co-TrzN showed different relative activities with different s-triazine substrates. Co-TrzN showed a visible absorption spectrum characteristic of other members of the amidohydrolase superfamily replaced with cobalt.
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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, carbonic anhydrase II, Zn2+ metalloenzyme ligands.
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Dissertations / Theses on the topic "Zinc metalloenzyme"

1

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. Significant sequence homology between the E. coli 5'-nucleotidase and members of the Ser/Thr protein phosphatase family in the catalytic site has lead to 5'-nucleotidase being included in this protein family. This thesis describes the development of a rapid purification methodology for milligram quantities of 5'-nucleotidase, and the investigation of a number of physical and biochemical properties of the enzyme with the aim of comparing these properties to those of certain catalytic site mutants. The molecular weight of the mature protein was estimated as 58219 daltons, with a specific activity for 5'-AMP, in the presence of 4 mM Co2+ and 13 mM Ca2+ at pH 6.0, of 730 mmol/min/mg. The presence of up to two zinc ions associated with the purified enzyme was observed using ICP-ES analysis, suggesting both metal ion binding sites are occupied by zinc in vivo, and some degree of displacement of zinc by cobalt could be observed. Mass spectrometry data, gathered at 60 and 70 mS orifice potential, suggested the presence of a small proportion of material with a mass 118 to 130 daltons greater than the main 5'-nucleotidase mass estimation. This study suggests that this mass difference, only evident at the lower orificepotential, is due to the presence of two zinc ions closely associated with 5'-nucleotidase. To account for the observed high level of activation of 5'-nucleotidase activity by particular divalent metal ions, this thesis describes a proposed model in which these divalent ions may displace the zinc ion at one of the metal ion binding sites. This displacement only occurs at one of the two metal ion binding sites, with the other metal binding site retaining the zinc ion already present. Studies with purified enzyme, each with a single amino acid substitution, lend support to this hypothesis and suggest the identity of the metal ion binding site at which displacement occurs. Seven key catalytic site residues (Asp-41, His-43, Asp-84, His-117, Glu-118, His-217 and His-252) were selected on the basis of sequence conservation within the Ser/Thr protein phosphatases and 5'-nucleotidases. X-ray crystallographic data published by others during this study implicated five of the selected residues (Asp-41, His-43, Asp-84, His-217 and His-252) directly in metal ion binding, including two residues from each metal ion binding site and one directly involved in both sites (Asp-84). The remaining two residues (His-117 and Glu-118) are highly conserved but were not thought to play direct roles in metal ion binding. The seven selected residues were modified by site-directed mutagenesis, and the effect of the amino acid substitutions upon the kinetic properties of 5'-nucleotidase activity was determined. Residues hypothesised to be involved in metal ion displacement, and subsequent activation of 5'-nucleotidase activity, were identified by reductions in metal ion affinity and increased levels of activation by cobalt compared to the wild type 5'-nucleotidase. This study suggests that the metal binding site, M2, that includes residues Asp-84, His-217 and His-252, is involved in metal ion displacement, while the other metal binding site, M1, is not. This, in turn, suggests the metal binding sites are functionally non-equivalent and kinetically distinct. No residues were identified in this study as playing significant roles in substrate binding, as there was no significant reduction observed in affinity for 5'-AMP observed in any of the catalytic site mutants.
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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. Significant sequence homology between the E. coli 5'-nucleotidase and members of the Ser/Thr protein phosphatase family in the catalytic site has lead to 5'-nucleotidase being included in this protein family. This thesis describes the development of a rapid purification methodology for milligram quantities of 5'-nucleotidase, and the investigation of a number of physical and biochemical properties of the enzyme with the aim of comparing these properties to those of certain catalytic site mutants. The molecular weight of the mature protein was estimated as 58219 daltons, with a specific activity for 5'-AMP, in the presence of 4 mM Co2+ and 13 mM Ca2+ at pH 6.0, of 730 mmol/min/mg. The presence of up to two zinc ions associated with the purified enzyme was observed using ICP-ES analysis, suggesting both metal ion binding sites are occupied by zinc in vivo, and some degree of displacement of zinc by cobalt could be observed. Mass spectrometry data, gathered at 60 and 70 mS orifice potential, suggested the presence of a small proportion of material with a mass 118 to 130 daltons greater than the main 5'-nucleotidase mass estimation. This study suggests that this mass difference, only evident at the lower orificepotential, is due to the presence of two zinc ions closely associated with 5'-nucleotidase. To account for the observed high level of activation of 5'-nucleotidase activity by particular divalent metal ions, this thesis describes a proposed model in which these divalent ions may displace the zinc ion at one of the metal ion binding sites. This displacement only occurs at one of the two metal ion binding sites, with the other metal binding site retaining the zinc ion already present. Studies with purified enzyme, each with a single amino acid substitution, lend support to this hypothesis and suggest the identity of the metal ion binding site at which displacement occurs. Seven key catalytic site residues (Asp-41, His-43, Asp-84, His-117, Glu-118, His-217 and His-252) were selected on the basis of sequence conservation within the Ser/Thr protein phosphatases and 5'-nucleotidases. X-ray crystallographic data published by others during this study implicated five of the selected residues (Asp-41, His-43, Asp-84, His-217 and His-252) directly in metal ion binding, including two residues from each metal ion binding site and one directly involved in both sites (Asp-84). The remaining two residues (His-117 and Glu-118) are highly conserved but were not thought to play direct roles in metal ion binding. The seven selected residues were modified by site-directed mutagenesis, and the effect of the amino acid substitutions upon the kinetic properties of 5'-nucleotidase activity was determined. Residues hypothesised to be involved in metal ion displacement, and subsequent activation of 5'-nucleotidase activity, were identified by reductions in metal ion affinity and increased levels of activation by cobalt compared to the wild type 5'-nucleotidase. This study suggests that the metal binding site, M2, that includes residues Asp-84, His-217 and His-252, is involved in metal ion displacement, while the other metal binding site, M1, is not. This, in turn, suggests the metal binding sites are functionally non-equivalent and kinetically distinct. No residues were identified in this study as playing significant roles in substrate binding, as there was no significant reduction observed in affinity for 5'-AMP observed in any of the catalytic site mutants.
Thesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Biomolecular and Biomedical Sciences
Science, Environment, Engineering and Technology
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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'approche que nous proposons est basée sur la biosynthèse de nove du site de fixation du zinc catalique. Pour cela, nous nous appuyons sur les règles de reconnaissance de l'IDA-Zn (Il) par les protéines (IMAC). L'immunisation d'un animal contre l'IDA-Zn(ll) devrait produire des anticorps présentant au niveau de leur paratope une structure de ligands capable de fixer un ion métallique dans une conformation catalytique. Pour développer ce type d'anticorps, une nouvelle méthode ELISA a d'abord été développée. L'utilisation d'un présentateur dIhaptène non protéique (le PEG bifonctionalisé) nous permet d'éviter toute réaction croisée avec la protéine de trans ort utilisée pour l'immunisation. Les anticorps anti-IDA-Zn(ll) ont ensuite été réalisés selon deux tech¬niques. D'abord la méthode des hybridomes nous a permis d'isoler à partir de 1152 clones 14 clones présentant de bonnes affinités. Ensuite, le répertoire immunologique de la souris immunisée contre l'IDA-Zn(ll) a été exprimé en banque de phages (banque de scFv). L'avantage d'une telle banque réside dans l'expression de tout le répertoire immunologique de la souris immunisée, ce qui offre la possibilité de "screener" des spécificités plus vastes vis-à-vis d'autres métaux, chélates métalliques ou d'autres antigènes. Enfin, la production de ces anticorps anti-chélate métallique à grande échelle nous a fait apparaître la nécessité de développer une méthode de purification douce, respectueuse de la structure tridimensionnelle des anticorps. Une méthode, faisant appel au ligand pseudobiospécifique l'histidine, a été développée au laboratoire. Pour valider son utilisation aux anticorps catalytiques, nous avons décidé de l'appliquer à la purification des anticorps catalytiques naturels présents dans le sérum des malades afteints de maladies auto-immunes. Les résultats sont comparés avec les méthodes classiques protéine A et protéine G, en termes de pureté des fractions et d'activité catalytique.
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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 promising antitumor effects, their mechanism of action and selectivity against cancer cells have not been adequately defined yet. In addition, low oral bioavailability, short half-life time, bone marrow toxicity, and cardiotoxicity limit their use in clinic. Therefore, there is considerable interest in developing compounds with selectivity and specificity towards individual family members of HDACs. The prototypical pharmacophore for HDAC inhibitors consist of a metal-binding moiety that coordinates to the catalytic metal ion within the HDAC active site, a capping group that interacts with the residues at the entrance of the active site and a linker that appropriately positions the metal-binding moiety and capping group for interactions in the active site. It has been shown that modification of cap, cap linking moiety, linker or zinc binding group (ZBG) shows promises of superior potency and isoform selectivity. My thesis research involves manipulating different aspects of the pharmacophoric model to yield not only more potent, selective, and effective drugs but also to help understand the biology of HDAC isoforms. In addition, I was successful in extending studies on HDAC isoforms to other zinc metalloenzymes such as leishmanolysin (gp63) and spliceosome associated zinc-metalloenzymes to understand biology of these zinc metalloenzymes by developing potent and selective small molecule inhibitors. This will aid in improvement of existing therapeutics for treatment of cancer, leishmania, malaria and other genetic disorders.
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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’élastase LasB de la bactérie Pseudomonas aeruginosa. Les ERAPs (1 et 2) participent au processus de maturation des antigènes. Ces enzymes clivent les précurseurs peptidiques en peptides antigéniques matures afin que ceux-ci disposent d’une taille optimale pour leur complexation au complexe majeur d’histocompatibilité de classe I et ainsi initient ou non la réponse immunitaire adaptative. Les niveaux d’expression de ces protéases ainsi que des polymorphismes d’un seul nucléotide ont été associé au développement de cancers et de maladies auto-immunes. Ainsi, la modulation de ces enzymes permettrait de lutter contre les pathologies associées au système immunitaire. P. aeruginosa est une bactérie Gram negative dotée d’une virulence et d’une résistance aux antimicrobiens remarquable. Aujourd’hui, la résistance aux antibiotiques représente un enjeu de santé publique majeur et il y a un besoin urgent en nouvelles thérapeutiques. Afin de satisfaire ce besoin, de nouvelles stratégies sont apparues comme celle consistant à cibler la virulence des bactéries afin de « désarmer » celles-ci. LasB représente une cible thérapeutique de choix de par sa localisation extracellulaire et ses implications physiopathologiques (colonisation, invasion, évasion à la réponse immunitaire, formation de biofilm, etc.). Bien qu'il y ait un besoin médical évident non satisfait dans ces deux aires thérapeutiques, aucun modulateur des ERAPs ni de LasB n'a atteint le marché. Ainsi, l’utilisation de la stratégie KTGS suivie de phases d’optimisation nous ont permis d’identifier et optimiser de nouvelles familles de ligands de ces enzymes. Ces composés peuvent être considérés comme des leads prometteurs puisqu’ils présentent des affinités nanomolaires pour leurs cibles respectives, des profils de sélectivité et de toxicité ainsi que des propriétés physicochimiques remarquables
Target-guided synthesis of protein ligands is an innovative strategy to discover bioactive compounds. In particular, the Kinetic Target-Guided Synthesis (KTGS) and the Dynamic Combinatorial Chemistry (DCC) have allowed, in recent years, the discovery of novel ligands for poorly explored therapeutic targets, which has enabled drug-discovery projects. This thesis project aims at using KTGS to discover and optimize ligands for two classes of metalloenzymes, namely endoplasmic reticulum aminopeptidases (ERAPs) and elastase LasB from the bacterium Pseudomonas aeruginosa. ERAPs (1 and 2) are involved in the process of antigen maturation. These enzymes cleave peptide precursors into mature antigenic peptides so that they have an optimal size for their complexation to the major histocompatibility complex of class I and thus initiate or not the adaptive immune response. The expression levels of these proteases as well as single nucleotide polymorphisms have been associated with the development of cancers and autoimmune diseases. Thus, the modulation of these enzymes would allow to fight against pathologies associated with the immune system. P. aeruginosa is a Gram-negative bacterium with remarkable virulence and antimicrobial resistance. Today, antibiotic resistance represents a major public health issue and there is an urgent need for new therapeutics. In order to meet this need, new strategies have emerged such as targeting the virulence of bacteria to "disarm" them. LasB represents a therapeutic target of choice due to its extracellular localization and its physiopathological implications (colonization, invasion, evasion of immune response, biofilm formation, etc.). Although there is a clear unmet medical need in these two therapeutic areas, no modulator of ERAPs or LasB has reached the market. Thus, the use of the KTGS strategy followed by optimization phases allowed us to identify and optimize new families of ligands for these enzymes. These compounds can be considered as promising lead compounds since they present nanomolar affinities for their respective targets, selectivity and toxicity profiles as well as remarkable physicochemical properties
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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"

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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"

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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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