Relevant bibliographies by topics / Serine hydrolases

Academic literature on the topic 'Serine hydrolases'

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Published: 8 June 2024

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

Journal articles on the topic "Serine hydrolases":

1

Nishioka, Tuguhiro, Makoto Iwata, Takuya Imaoka, Maiko Mutoh, Yoshihiro Egashira, Takashi Nishiyama, Takashi Shin, and Takao Fujii. "A Mono-2-Ethylhexyl Phthalate Hydrolase from a Gordonia sp. That Is Able To Dissimilate Di-2-Ethylhexyl Phthalate." Applied and Environmental Microbiology 72, no. 4 (April 2006): 2394–99. http://dx.doi.org/10.1128/aem.72.4.2394-2399.2006.

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ABSTRACT Gordonia sp. strain P8219, a strain able to decompose di-2-ethylhexyl phthalate, was isolated from machine oil-contaminated soil. Mono-2-ethylhexyl phthalate hydrolase was purified from cell extracts of this strain. This enzyme was a 32,164-Da homodimeric protein, and it effectively hydrolyzed monophthalate esters, such as monoethyl, monobutyl, monohexyl, and mono-2-ethylhexyl phthalate. The Km and V max values for mono-2-ethylhexyl phthalate were 26.9 ± 4.3 μM and 18.1 ± 0.9 μmol/min · mg protein, respectively. The deduced amino acid sequence of the enzyme exhibited less than 30% homology with those of meta-cleavage hydrolases which are serine hydrolases but exhibited no significant homology with the sequences of serine esterases. The pentapeptide motif GXSXG, which is conserved in serine hydrolases, was present in the sequence. The enzymatic properties and features of the primary structure suggested that this enzyme is a novel enzyme belonging to an independent group of serine hydrolases.
2

Jeremy Johnson, R., Andrew Bartels, Rachel Erkilla, Nicole Green, Steven Han, Nathaniel Holt, Melissa Jones, et al. "Proteopedia entry: Mammalian serine hydrolases." Biochemistry and Molecular Biology Education 43, no. 1 (November 18, 2014): 60–61. http://dx.doi.org/10.1002/bmb.20840.

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Botos, Istvan, and Alexander Wlodawer. "The expanding diversity of serine hydrolases." Current Opinion in Structural Biology 17, no. 6 (December 2007): 683–90. http://dx.doi.org/10.1016/j.sbi.2007.08.003.

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Tang, Shan, Adam T. Beattie, Lucie Kafkova, Gianluca Petris, Nicolas Huguenin-Dezot, Marc Fiedler, Matthew Freeman, and Jason W. Chin. "Mechanism-based traps enable protease and hydrolase substrate discovery." Nature 602, no. 7898 (February 16, 2022): 701–7. http://dx.doi.org/10.1038/s41586-022-04414-9.

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AbstractHydrolase enzymes, including proteases, are encoded by 2–3% of the genes in the human genome and 14% of these enzymes are active drug targets1. However, the activities and substrate specificities of many proteases—especially those embedded in membranes—and other hydrolases remain unknown. Here we report a strategy for creating mechanism-based, light-activated protease and hydrolase substrate traps in complex mixtures and live mammalian cells. The traps capture substrates of hydrolases, which normally use a serine or cysteine nucleophile. Replacing the catalytic nucleophile with genetically encoded 2,3-diaminopropionic acid allows the first step reaction to form an acyl-enzyme intermediate in which a substrate fragment is covalently linked to the enzyme through a stable amide bond2; this enables stringent purification and identification of substrates. We identify new substrates for proteases, including an intramembrane mammalian rhomboid protease RHBDL4 (refs. 3,4). We demonstrate that RHBDL4 can shed luminal fragments of endoplasmic reticulum-resident type I transmembrane proteins to the extracellular space, as well as promoting non-canonical secretion of endogenous soluble endoplasmic reticulum-resident chaperones. We also discover that the putative serine hydrolase retinoblastoma binding protein 9 (ref. 5) is an aminopeptidase with a preference for removing aromatic amino acids in human cells. Our results exemplify a powerful paradigm for identifying the substrates and activities of hydrolase enzymes.
5

Liu, Y., M. P. Patricelli, and B. F. Cravatt. "Activity-based protein profiling: The serine hydrolases." Proceedings of the National Academy of Sciences 96, no. 26 (December 21, 1999): 14694–99. http://dx.doi.org/10.1073/pnas.96.26.14694.

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Ross, Matthew K., and Ran Wang. "Expanding the Toolkit for the Serine Hydrolases." Chemistry & Biology 22, no. 7 (July 2015): 808–9. http://dx.doi.org/10.1016/j.chembiol.2015.07.002.

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Hernáez, M. J., E. Andújar, J. L. Ríos, S. R. Kaschabek, W. Reineke, and E. Santero. "Identification of a Serine Hydrolase Which Cleaves the Alicyclic Ring of Tetralin." Journal of Bacteriology 182, no. 19 (October 1, 2000): 5448–53. http://dx.doi.org/10.1128/jb.182.19.5448-5453.2000.

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ABSTRACT A gene designated thnD, which is required for biodegradation of the organic solvent tetralin by Sphingomonas macrogoltabidus strain TFA, has been identified. Sequence comparison analysis indicated that thnD codes for a carbon-carbon bond serine hydrolase showing highest similarity to hydrolases involved in biodegradation of biphenyl. An insertion mutant defective in ThnD accumulates the ring fission product which results from the extradiol cleavage of the aromatic ring of dihydroxytetralin. The gene product has been purified and characterized. ThnD is an octameric thermostable enzyme with an optimum reaction temperature at 65°C. ThnD efficiently hydrolyzes the ring fission intermediate of the tetralin pathway and also 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, the ring fission product of the biphenylmeta-cleavage pathway. However, it is not active towards the equivalent intermediates of meta-cleavage pathways of monoaromatic compounds which have small substituents in C-6. When ThnD hydrolyzes the intermediate in the tetralin pathway, it cleaves a C-C bond comprised within the alicyclic ring of tetralin instead of cleaving a linear C-C bond, as all other known hydrolases ofmeta-cleavage pathways do. The significance of this activity of ThnD for the requirement of other activities to mineralize tetralin is discussed.
8

Bernhardt, Peter, Karl Hult, and Romas J. Kazlauskas. "Molecular Basis of Perhydrolase Activity in Serine Hydrolases." Angewandte Chemie International Edition 44, no. 18 (April 29, 2005): 2742–46. http://dx.doi.org/10.1002/anie.200463006.

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Bernhardt, Peter, Karl Hult, and Romas J. Kazlauskas. "Molecular Basis of Perhydrolase Activity in Serine Hydrolases." Angewandte Chemie 117, no. 18 (April 29, 2005): 2802–6. http://dx.doi.org/10.1002/ange.200463006.

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Patočka, Jiří, Kamil Kuča, and Daniel Jun. "Acetylcholinesterase and Butyrylcholinesterase – Important Enzymes of Human Body." Acta Medica (Hradec Kralove, Czech Republic) 47, no. 4 (2004): 215–28. http://dx.doi.org/10.14712/18059694.2018.95.

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The serine hydrolases and proteases are a ubiquitous group of enzymes that is fundamental to many critical lifefunctions. Human tissues have two distinct cholinesterase activities: acetylcholinesterase and butyrylcholinesterase. Acetylcholinesterase functions in the transmission of nerve impulses, whereas the physiological function of butyrylcholinesterase remains unknown. Acetylcholinesterase is one of the crucial enzymes in the central and peripheral nerve system. Organophosphates and carbamates are potent inhibitors of serine hydrolases and well suited probes for investigating the chemical reaction mechanism of the inhibition. Understanding the enzyme’s chemistry is essential in preventing and/or treating organophosphate and carbamate poisoning as well as designing new medicaments for cholinergic-related diseases like as Alzheimer’s disease.
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You might also be interested in the extended bibliographies on the topic 'Serine hydrolases' for particular source types:
Journal articles Dissertations / Theses

Dissertations / Theses on the topic "Serine hydrolases":

1

Fransson, Linda. "Enzyme substrate solvent interactions : a case study on serine hydrolases." Doctoral thesis, KTH, Biokemi, 2008. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-4867.

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Reaction rates and selectivities were measured for transacylation of fatty acid esters in solvents catalysed by Candida antarctica lipase B and by cutinase from Humicola insolens. With these enzymes classical water-based enzymology can be expanded to many different solvents allowing large variations in interaction energies between the enzymes, the substrates and the surrounding. Further ,hydrolysis reactions catalysed by Bacillus subtilis esterase 2 were investigated. Thermodynamics analyses revealed that the enzyme contribution to reaction rate acceleration compared to acid catalysis was purely entropic. On the other hand, studies of differences in activation entropy and enthalpy between enantiomers and between homologous esters showed that high substrate specificity was favoured by enthalpic stabilisation. Solvent was found to have a profound effect on enzyme catalysis, affecting both reaction rate and selectivity. Differences in substrate solubility will impact enzyme specificity since substrate binding is an equilibrium between enzyme-bound substrate and substrate in free solution. In addition, solven tmolecules were found to act as enzyme inhibitors, showing both competitive and non-competitive behaviour. In several homologous data series enthalpy-entropy compensation relationships were encountered. A possible extrathermodynamic relationship between enthalpy and entropy can easily be lost under co-varying errors propagated from the experiments. From the data in this thesis, one instance was found of a real enthalpy-entropy compensation that could be distinguished from statistical errors, while other examples could not be verified.
QC 20100722
2

Elahi, AEM Rubayet. "Proteome-wide Functional Profiling of Serine Hydrolases in the Human Malaria Parasite." Diss., Virginia Tech, 2019. http://hdl.handle.net/10919/90181.

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The serine hydrolase (SH) enzyme superfamily is one of the largest and most diverse enzyme classes in eukaryotes and prokaryotes. The most virulent human malaria parasite Plasmodium falciparum has over 40 predicted serine hydrolases (SH). Prior investigation on a few of these have suggested their critical role in parasite biology. The majority of the SHs in P. falciparum have not been functionally characterized. Investigation of these uncharacterized SHs will provide new insights into essential features of parasite metabolism and possibly lead to new antimalarial targets. In this study, we have employed activity-based protein profiling (ABPP) and liquid chromatography-tandem mass spectrometry (LC-MS/MS) to functionally characterize SHs. In our effort to profile plasmodial SHs using ABPP, we have identified a human erythrocyte SH, acylpeptide hydrolase (APEH) in the developing parasites. This finding is the first report of internalization of host hydrolytic enzyme by the parasite. Treatment of parasites with an APEH specific triazole urea inhibitor, AA74-1, caused growth inhibition in parasites with poor potency in the first replication cycle, however, the potency dramatically increased in the second cycle. We show that this unique growth inhibition profile is due to the inability of AA74-1 to inhibit parasite-internalized APEH in vivo. These findings suggest that internalization of active APEH by the parasite is essential for parasite survival. Lipases catalyze the hydrolysis of ester bonds of lipid species such as neutral lipids and phospholipids. Although roles of lipases in propagation, as well as virulence in various organisms, have been acknowledged, in P. falciparum lipases remain understudied. We combined LC-MS/MS with the SH-directed ABPP to identify lipases of SH superfamily in P. falciparum. We have identified 16 plasmodial SHs with putative lipase activity. Bioinformatics analysis of our identified lipases is consistent with our findings. We have screened a panel of various classes of SH inhibitors in a competitive ABPP. A plasmodial putative lipase was potently and specifically inhibited by human monoacylglycerol lipase inhibitor. This inhibition profile suggests it as a monoacylglycerol lipase which plays a role in releasing fatty acids from neutral lipid. This finding shows that how inhibitor screening can aid in building hypotheses on biological roles of an enzyme. Altogether, in this dissertation, we have presented a robust strategy of identifying and functionally characterizing SHs in P. falciparum, which opens the door to the discovery of new biological processes.
Doctor of Philosophy
Malaria contributed to nearly a half a million deaths in 2017. The vast majority of malaria-related deaths are due to the parasite Plasmodium falciparum. This parasite resides inside human red blood cells (erythrocytes) and grows rapidly during a 48 hour cycle. There are over 40 serine hydrolase (SH) superfamily proteins in the parasite. Biological functions of the majority of SHs in the parasite remains unknown. Study on these SHs will provide new insights into parasite biology, and possibly present new antimalarial drug targets. We used chemical biology techniques to identify and functionally characterize parasite SHs. In one study, we show the parasite intenalized a human erythrocyte SH, acylpeptide hydrolase (APEH). We used an APEH-specific inhibitor to investigate the biological significance of internalized APEH in parasite biology. Treatment of the parasite with the inhibitor resulted in parasite growth inhibition suggesting internalization of APEH is essential for parasite survival. Lipases are enzymes that aid in break down of lipids and have shown to be crucial for growth and pathogenicity in various organisms. Lipases and lipid catabolism remain understudied in the malaria parasite. We used mass spectrometry in our approach to identify 16 lipases in asexual parasites. We have also shown that screening with highly specific inhibitors can help in predicting biological function of a particular enzyme. In summary, in this body of work, we have presented an approach of studying SHs in the malaria parasite, which will provide new insights into parasite biology.
3

Galmés, Ordinas Miquel Àngel. "Molecular insights into the promiscuity of serine hydrolases. Towards a computationally guided protocol for the redesign of enzymes." Doctoral thesis, Universitat Jaume I, 2022. http://dx.doi.org/10.6035/14122.2022.725777.

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Two serine hydrolases, Candida antarctica Lipase B (CALB) and para-nitrobenzyl (Bs2) esterase from Bacillus subtilis, were used as a model to study enzyme promiscuity through QM/MM methods and experimental enzymes kinetics. Both, the catalytic and the substrate promiscuity were studied. The hydrolysis of amides and the epoxidation of alkenes catalyzed by CALB were explored. Moreover, a computational scheme for the redesign of the Bs2 was also proposed. The electrostatic environment around the active site was analyzed and a map of structural determinants in the vicinity of the active site pocket was done using 3D Convolutional Neural Networks. The proposed computationally guided protocol for the mutagenesis of enzymes based on the detailed analysis of the electrostatic environment of two structurally aligned trajectories using rotation quaternions was applied. A new mutant variant of the Bs2 was suggested as an improved catalytic variant by combining the best electrostatic features of both enzymes.
Programa de Doctorat en Química Teòrica i Modelització Computacional
4

Kreuzer, Johannes Verfasser], Stephan A. [Akademischer Betreuer] Sieber, and Aymelt [Akademischer Betreuer] [Itzen. "The Natural Product Acivicin as a Tool for ABPP and the Activity of Serine Hydrolases in Uterine Fibroids / Johannes Kreuzer. Gutachter: Aymelt Itzen ; Stephan A. Sieber. Betreuer: Stephan A. Sieber." München : Universitätsbibliothek der TU München, 2015. http://d-nb.info/1071651544/34.

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5

Yedji, Rodrigue. "Perturbateurs endocriniens de type phtalate et poisson zèbre Danio rerio : approche chémoprotéomique pour l'identification des cibles et recherche de signatures d'exposition." Electronic Thesis or Diss., Université de Lorraine, 2022. http://www.theses.fr/2022LORR0106.

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Les esters de phtalate constituent une famille de composés synthétiques très répandue du fait de leurs usages comme plastifiants. Ils entrent dans la composition de plusieurs produits plastiques tels que les emballages, les jouets, les produits cosmétiques, certains systèmes de toiture en plastique, ainsi que les matériaux de décoration de meubles. Les phtalates ne sont pas liés de manière covalente à la matrice des polymères et sont donc facilement rejetés dans l'environnement, entraînant par conséquent une exposition animale et humaine. En absence de produits de substitutions non-toxiques, les composés de type phtalate restent encore largement utilisés dans l'industrie en dépit de la classification de certains d'entre eux dans la catégorie des substances présumées toxiques par l'European Chemicals Agency (ECHA), en tant que perturbateurs endocriniens. De plus, ils sont cancérigènes et tératogènes. L'effet délétère des esters de phtalates sur les organismes est établi mais le caractère multiple des effets observés montre que les mécanismes d'action des phtalates ne sont que très partiellement élucidés. Nous avons utilisé deux approches de protéomique ciblée pour tenter d'éclairer nos connaissances sur les mécanismes d'actions des esters de phtalate. Pour cela, le dibutyl phtalate (DBP) a été utilisé comme phtalate modèle, et le poisson zèbre (D. rerio) comme organisme modèle. L'utilisation de la première approche de protéomique ciblée, le profilage protéique basé sur l'affinité (affinity-based protein profiling, AfBPP) a permis de montrer la perturbation fonctionnelle de protéines par le DBP avec des sondes photoactivables issues de la synthèse de types aryle azide. L'optimisation des conditions de fixation des sondes diazirine (Diazirine 2) devrait nous permettre de disposer d'une sonde pouvant être utilisée pour identifier les cibles protéiques du DBP dans le protéome du poisson zèbre. La deuxième approche, le profilage basé sur l'activité des enzymes (activity-based protein profiling, ABPP) a permis d'utiliser une sonde réactive spécifique des hydrolases à sérine (SHs) pour cartographier pour la première fois des SHs actives dans le protéome du poisson zèbre. L'identification des SHs dérégulées en présence de DBP chez les larves de poisson zèbre a également été rapportée dans cette étude. Nos résultats globaux indiquent que les approches de protéomiques ciblées telles que l'ABPP ou l'AfBPP peuvent être un atout pour comprendre les mécanismes d'action liés aux xénobiotiques en écotoxicologie
Phthalate esters are a family of synthetic compounds widely used as plasticisers. They are used in a number of plastic products such as packaging, toys, cosmetics, plastic roofing system and furniture decoration materials. Phthalates are not covalently bonded to the polymer matrix and are therefore easily released into the environment, resulting in animal and human exposure. In the absence of non-toxic substitutes, phthalate compounds are still widely used in industry, despite the classification of some of them by the European Chemicals Agency (ECHA) as suspected toxic substances and as endocrine disruptors. In addition, they are carcinogenic and teratogenic. The deleterious effect of phthalate esters on organisms is established, but the multiple nature of the effects observed shows that the mechanisms of action of phthalates are only partially elucidated. We used two targeted proteomics approaches to shed light on the mechanisms of action of phthalate esters. Dibutyl phthalate (DBP) was used as a model phthalate and zebrafish (D. rerio) as a model organism. Using the first targeted proteomics approach, affinity-based protein profiling (AfBPP), the functional disruption of proteins by DBP with photoaffinity probes from aryl azide synthesis was demonstrated. Optimisation of the binding conditions for diazirine probes (Diazirine 2) should provide us with a probe that can be used to identify DBP protein targets in the zebrafish proteome. The second approach, activity-based protein profiling (ABPP), used a reactive probe specific for serine hydrolases (SHs) to map active SHs in the zebrafish proteome for the first time. The identification of deregulated SHs in the presence of DBP in zebrafish larvae was also reported in this study. Overall, our results indicate that targeted proteomics approaches such as ABPP or AfBPP can be an asset for understanding xenobiotic-related mechanisms of action in ecotoxicology
6

Hamberg, Anders. "Serine Hydrolase Selectivity : Kinetics and applications in organic and analytical chemistry." Doctoral thesis, KTH, Biokemi, 2010. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-12831.

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The substrate selectivities for different serine hydrolases were utilized in various applications, presented in papers I-VI. The articles are discussed in the thesis in view of the kinetics of the enzyme catalysis involved. In paper I the enantioselectivities towards a range of secondary alcohols were reversed for Candida antarctica lipase B by site directed mutagenesis. The thermodynamic components of the enantioselectivity were determined for the mutated variant of the lipase. In papers II-III Candida antarctica lipase B was engineered for selective monoacylation using two different approaches. A variant of the lipase created for substrate assisted catalysis (paper II) and three different variants with mutations which decreased the volume of the active site (paper III) were evaluated. Enzyme kinetics for the different variants were measured and translated into activation energies for comparison of the approaches. In papers IV and V three different enzymes were used for rapid analysis of enantiomeric excess and conversion of O-acylated cyanohydrins synthesized by a defined protocol. Horse liver alcohol dehydrogenase, Candida antarctica lipase B and pig liver esterase were sequentially added to a solution containing the O-acylated cyanohydrin. Each enzyme caused a drop in absorbance from oxidation of NADH to NAD+. The product yield and enantiomeric excess was calculated from the relative differences in absorbance. In paper VI a method for C-terminal peptide sequencing was developed based on conventional Carboxypeptidase Y digestion combined with matrix assisted laser desorption/ionization mass spectrometry. An alternative nucleophile was used to obtain a stable peptide ladder and improve sequence coverage.
QC20100629
7

Hamon, Nadège. "Synthese de nucleosides en serie carbocyclique à visée antivirale." Thesis, Montpellier 2, 2010. http://www.theses.fr/2010MON20087/document.

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Les analogues nucléosidiques constituent une famille importante d'agents thérapeutiques dans le traitement de maladies d'origine virale. Parmi ces composés, les nucléosides carbocycliques possèdent des propriétés biologiques intéressantes. Le premier chapitre de cette thèse est consacrée à la famille des neplanocines qui sont des carbonucleosides naturels. Nous avons détaillé l'interaction de ces composés avec leur principale cible, la S-adénosylhomocystéine hydrolase, ainsi que les différentes approches de synthèses de ces carbonucléosides et de leurs énantioméres avant de passer en revue leurs activités biologiques. Nous avons présenté dans le deuxième chapitre la première synthèse énantiosélective de la (éD)-néplanocine B. Le troisième chapitre est quant à lui axé sur la mise au point d'une synthèse de 3 '-halo-5'-norcarbonucléosides phosphonates ainsi qu’à l'évaluation de leurs activités antivirales
Nucleosides analogues constitute an important family of therapeutic agents in the treatment of viral diseases. Among these compounds, carbocyclic nucleosides have interesting biological properties. The first chapter of this thesis is dedicated to a family of natural carbonucleosides, the neplanocins. We have presented their mode of action against S-adenosylhomocysteine hydrolase, as well as various syntheses of natural neplanocins and their enantiomers before reviewing their biological activities. In the second chapter, we described the first enantioselective synthesis of (¨D)-neplanocine B. The third chapter is devoted to the development of the synthesis of 3 '-halo-5¡¯-norcarbonucleosides phosphonates as well as the evaluation of their antiviral activities
8

Ambrose, Timothy James William. "Serine hydrolase activity and roles for monoacylglycerol lipase in innate immunity and intestinal inflammation." Thesis, University of Oxford, 2018. http://ora.ox.ac.uk/objects/uuid:f7a12796-ae8f-4121-ab1a-26778261ac78.

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Detection of evolutionarily conserved pathogen motifs by pattern recognition receptors (PRRs), particularly on dendritic cells (DCs), is crucial for adequate immune responses. Defects in DC function are known to be associated with inflammatory bowel disease (IBD). The endocannabinoid system (ECS) is the system through which exocannabinoids such as Δ9-tetrahydrocannabinol and cannabidiol signal. Regarding inflammation, cannabinoids generally exert anti-inflammatory effects, including on experimental colitis. However, most work has been performed in animal models and less is known about the function of this system in human immune cells, particularly DCs. Monoacylglycerol lipase (MGLL) is the key enzyme for hydrolysis of the endocannabinoid 2-arachidonoylglycerol, and a member of the serine hydrolase enzyme superfamily. This thesis defines the activity of serine hydrolase enzymes for the first time in human DCs upon stimulation by NOD2/TLR2 ligands using activity-based protein profiling (ABPP). MGLL is shown to be ubiquitously upregulated upon stimulation of DCs and in monocyte-derived macrophages. Through pharmacological inhibition studies, MGLL is demonstrated to regulate cellular and secreted lipids, not limited to endocannabinoids. However, overall DC function is independent of this enzyme suggesting that the effects of lipid modulation may be on bystander cells. Challenging the current literature, MGLL inhibition with a novel inhibitor worsens murine Citrobacter rodentium colitis. Finally, ABPP demonstrates a rich serine hydrolome in colonic tissue from human IBD with many enzymes previously undefined in this disease. Gene expression of ECS components suggests the enzymes ABHD12 and DAGLα/β may be potential markers of field change in IBD.
9

Ho, Cherry Pei-Yee. "Evaluation of a Serine Hydrolase Inhibitor JZL184 as an Immunomodulator against Avian Pathogenic Escherichia Coli O78 in Chickens." Thesis, Mississippi State University, 2018. http://pqdtopen.proquest.com/#viewpdf?dispub=10788360.

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Studies with the serine hydrolase inhibitor JZL184 have suggested that enhanced 2-arachidonoylglycerol signaling could be strategized to stimulate innate immune cells to combat invading pathogens and improve host defense by prompting the systemic release of proinflammatory cytokines. Although the neurochemical effects of JZL184 were found to cultivate within 30 min in mice, its immune-regulating effects have been studied much later and its effects on chickens have not been clear. To explore the modulations in the chickens’ immune responses, we studied the effects of intraperitoneal injections of JZL184 in APEC O78-infected chickens on pathogenicity, histopathology, and IL-1β levels. The pathogenicity of the strain was assessed by isolating bacteria from livers, blood, air sacs, and hearts at 8, 28, and 56 h post-infection (p.i.). Air sacs, livers, and hearts were examined for histopathological changes at 8, 28, and 56 h p.i. Serum samples were collected at 8, 28, and 56 h p.i. and analyzed with a chicken IL-1β ELISA kit. Liver and spleen samples were homogenized for detection of serine hydrolases and carboxylesterases. Our work showed that 10 mg/kg and 40 mg/kg of JZL184 did not reduce the severity and progression of lesions produced in chickens challenged with 108 CFU of E. coli O78. The JZL184 treatments made colibacillosis lesions in the E. coli O78-challenged chickens worse and we did not find evidence of the injections increasing the serum cytokine levels of IL-1β at our sampling times.

10

Kornahrens, Anne. "Methodology development and synthesis of a biologically relevant natural product and targeted scaffold discovery for serine hydrolase inhibition." Thesis, University of Oxford, 2016. https://ora.ox.ac.uk/objects/uuid:4cf5026f-e421-4b0b-9f62-707622f780b7.

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The phenomenal potential of synthetic chemistry to influence small molecule therapeutic development represents my overarching theme. The goal of designing or discovering a novel clinical candidate or biological target can be achieved through a variety of avenues available to synthetic organic chemists. The potential of natural product total synthesis and inhibitor development as impactful projects were pursued with the use and development of methodology. The natural product streptonigrin, a potent antitumor antibiotic, showed promise in clinical trials ultimately terminated in the 1970s. The underexplored mechanism of action prompted a reexamination of this potential therapeutic. The Donohoe group successfully designed a modular total synthesis accessing streptonigrin in 11 steps and 14% yield. The introduction of an asymmetric Suzuki-Miyaura reaction yielded a key intermediate in 42% ee and 65% yield, which represents the first example of purely synthetic access to enantioenriched late-stage streptonigrin analogues. The "hydrogen-borrowing" method allows the functionalization of ketones with methanol and transition metal catalysts, but examples lacked application to further α-functionalization. The successful development of a novel "interrupted- hydrogen-borrowing" method allowed the use of iridium and methanol to trap the reactive enone intermediates by preventing the subsequent "hydrogen returning". Thus, this enabled these reactive intermediates to be subjected to a 1,4-conjugate addition with a nucleophilic ketone enolate and subsequent cyclization and oxidation to form highly substituted pyridines from simple ketones. The exploration of serine hydrolases, an important mammalian enzyme class with a large portion still uncharacterized, requires inhibitors with new chemotypes that can covalently and irreversibly bind. The small library of urea- and carbamate- containing scaffolds with varied aromatic backbone substitutions was subjected to activity-based protein profiling to allow expedient examination of the whole serine hydrolase family. The predicted strong electronic effect of the p-substituent was confirmed, modulating the reactivity of the electrophilic urea or carbamate moiety. MudPIT analysis of a subset supported the demonstrated reactivity profile and identified the uncharacterized serine hydrolase PNPLA4 as a selective target of one inhibitor. This potent and selective inhibition was verified by in vitro and in cell assays and validates this chemotype as a family of serine hydrolase inhibitors.
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Books on the topic "Serine hydrolases":

1

Barrett, Alan J., John N. Abelson, and Melvin I. Simon. Proteolytic Enzymes: Serine and Cysteine Peptidases. Elsevier Science & Technology Books, 1994.

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Proteolytic Enzymes: Serine and Cysteine Peptidases, Volume 244 (Methods in Enzymology). Academic Press, 1994.

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(Editor), John N. Abelson, Melvin I. Simon (Editor), and Alan J. Barrett (Editor), eds. Proteolytic Enzymes: Serine and Cysteine Peptidases, Volume 244 (Methods in Enzymology). Academic Press, 1994.

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Barrett, Alan J., John N. Abelson, and Melvin I. Simon. Proteolytic Enzymes: Aspartic and Metallo Peptidases. Elsevier Science & Technology Books, 1995.

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5

Tiezzi, Antonio, Elisa Ovidi, and Tomasz M. Karpiński, eds. New Findings from Natural Substances. BENTHAM SCIENCE PUBLISHERS, 2022. http://dx.doi.org/10.2174/97898150514211220101.

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Abstract:
New Findings from Natural Substances present the state-of-the-art and future prospects for the application of biomolecules in the pharmaceutical, agricultural, food and industrial sectors. The book presents eight reviews contributed by more than twenty experts on interesting natural substances, and plant sources, that serve as sources of natural remedies for a variety of ailments. The reviews in the book cover the use of herbs like Heliotropium and Astragalus. Additional health benefits of extracts from essential oils, Caenorhabditis elegans, and olive oil, as well as the medicinal use of rosmarinic acid and hydrolates. The contributions highlight a range of pharmacological agents from natural sources that have anti-cancer, anti-inflammatory, cardioprotective and neuroprotective effects. The contents are presented in a simple and organized style. The book will broaden the knowledge about biological products for a variety of readers - generalists, students and researchers, alike.

Book chapters on the topic "Serine hydrolases":

1

Schomburg, Dietmar, and Ida Schomburg. "L-serine-phosphatidylethanolamine phosphatidyltransferase 2.7.8.29." In Class 2–3.2 Transferases, Hydrolases, 447. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36240-8_99.

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Schomburg, Dietmar, and Ida Schomburg. "D-alanine-d-serine ligase 6.3.2.35." In Class 3.4–6 Hydrolases, Lyases, Isomerases, Ligases, 687–89. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36260-6_93.

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Schomburg, Dietmar, and Ida Schomburg. "O-phospho-l-serine-tRNA ligase 6.1.1.27." In Class 3.4–6 Hydrolases, Lyases, Isomerases, Ligases, 651–60. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36260-6_84.

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Baggelaar, Marc P., and Mario Van der Stelt. "Competitive ABPP of Serine Hydrolases: A Case Study on DAGL-Alpha." In Methods in Molecular Biology, 161–69. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6439-0_12.

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Deng, Shiping, and Inna Popova. "Carbohydrate Hydrolases." In SSSA Book Series, 185–209. Madison, WI, USA: American Society of Agronomy, Crop Science Society of America, and Soil Science Society of America, 2015. http://dx.doi.org/10.2136/sssabookser9.c9.

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Ding, Shi-You, William S. Adney, Todd B. Vinzant, Stephen R. Decker, John O. Baker, Steven R. Thomas, and Michael E. Himmel. "Glycoside Hydrolase Gene Cluster ofAcidothermus cellulolyticus." In ACS Symposium Series, 332–60. Washington, DC: American Chemical Society, 2003. http://dx.doi.org/10.1021/bk-2003-0855.ch020.

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Hong, Tram Ngoc, and Renier A. L. van der Hoorn. "DIGE-ABPP by Click Chemistry: Pairwise Comparison of Serine Hydrolase Activities from the Apoplast of Infected Plants." In Methods in Molecular Biology, 183–94. Totowa, NJ: Humana Press, 2014. http://dx.doi.org/10.1007/978-1-62703-986-4_15.

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Moris-Varas, Francisco, Laura Hartman, Amit Shah, and David C. Demirjian. "Screening of Hydrolase Libraries Using pH-Shift Reagents: Rapid Evaluation of Enantioselectivity." In ACS Symposium Series, 41–54. Washington, DC: American Chemical Society, 2001. http://dx.doi.org/10.1021/bk-2001-0776.ch003.

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Chou, Yat-Chen, William S. Adney, Stephen R. Decker, John O. Baker, Glenna Kunkel, David W. Templeton, and Michael E. Himmel. "Cloning and Heterologous Expression of the Gene Encoding a Family 7 Glycosyl Hydrolase fromPenicillium funiculosum." In ACS Symposium Series, 170–93. Washington, DC: American Chemical Society, 2004. http://dx.doi.org/10.1021/bk-2004-0889.ch010.

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McCleary, Barry V. "Comparison of Endolytic Hydrolases That Depolymerize 1,4-β-D-Mannan, 1,5-α-L-Arabinan, and 1,4-β-D-Galactan." In ACS Symposium Series, 437–49. Washington, DC: American Chemical Society, 1991. http://dx.doi.org/10.1021/bk-1991-0460.ch034.

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Conference papers on the topic "Serine hydrolases":

1

Rüedi, P., W. Ganci, and U. Ringeisen. "Synthesis of Rigid Acetylcholine Mimics as Inhibitors of Serine Hydrolases." In The 1st International Electronic Conference on Synthetic Organic Chemistry. Basel, Switzerland: MDPI, 1997. http://dx.doi.org/10.3390/ecsoc-1-02032.

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Rüedi, P., S. Furegati, A. Linden, G. Przibille, and D. Rentsch. "Synthesis, ee-Determination and Absolute Configuration of Chiral Organophosphorus Inhibitors of Serine Hydrolases." In The 1st International Electronic Conference on Synthetic Organic Chemistry. Basel, Switzerland: MDPI, 1997. http://dx.doi.org/10.3390/ecsoc-1-02031.

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Sajic, Tatjana, Stephan Arni, Walter Weder, Rudolf Aebersold, and Sven Hillinger. "Abstract 4934: Modified SWATH MS analysis of serine hydrolase activity in lung adenocarcinoma." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-4934.

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Sajic, Tatjana, Stephan Arni, Walter Weder, Rudolf Aebersold, and Sven Hillinger. "Abstract 4934: Modified SWATH MS analysis of serine hydrolase activity in lung adenocarcinoma." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-4934.

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