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Journal articles on the topic 'Discovery of novel enzymes'

Author: Grafiati

Published: 5 June 2025

Last updated: 1 August 2025

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1

P, Keerthi, Lathif AK, and Nesaghi Amuthavel. "Enzyme Technology for Drug Discovery." Journal of Chemical Engineering & Process Technology 14, no. 14 (2023): 8. https://doi.org/10.35248/2157-7048.23.14.471.

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Enzymes are biochemical catalysts that facilitate chemical reactions under Physiological conditions. Currently enzymes are being employed in industrial biotechnology for numerous purposes for the production of novel and sustainable products at a speedy rate. Enzyme technology is the change of an enzyme's structure or catalytic activity in order to produce new metabolites or participate in new reaction pathways. Simultaneously, significant technical advancements are encouraging the chemical and pharmaceutical sectors to embrace enzyme technology, a movement fueled by worries about health, energ

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Buryska, Tomas, Lukas Daniel, Antonin Kunka, Jan Brezovsky, Jiri Damborsky, and Zbynek Prokop. "Discovery of Novel Haloalkane Dehalogenase Inhibitors." Applied and Environmental Microbiology 82, no. 6 (2016): 1958–65. http://dx.doi.org/10.1128/aem.03916-15.

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ABSTRACTHaloalkane dehalogenases (HLDs) have recently been discovered in a number of bacteria, including symbionts and pathogens of both plants and humans. However, the biological roles of HLDs in these organisms are unclear. The development of efficient HLD inhibitors serving as molecular probes to explore their function would represent an important step toward a better understanding of these interesting enzymes. Here we report the identification of inhibitors for this enzyme family using two different approaches. The first builds on the structures of the enzymes' known substrates and led to

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Dellafiora, Luca, Christoph Gonaus, Barbara Streit, et al. "An In Silico Target Fishing Approach to Identify Novel Ochratoxin A Hydrolyzing Enzyme." Toxins 12, no. 4 (2020): 258. http://dx.doi.org/10.3390/toxins12040258.

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Ochratoxin A (OTA), a mycotoxin that is of utmost concern in food and feed safety, is produced by fungal species that mainly belong to the Aspergillus and Penicillium genera. The development of mitigation strategies to reduce OTA content along the supply chains is key to ensuring safer production of food and feed. Enzyme-based strategies are among the most promising methods due to their specificity, efficacy, and multi-situ applicability. In particular, some enzymes are already known for hydrolyzing OTA into ochratoxin alpha (OTα) and phenylalanine (Phe), eventually resulting in detoxification

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Yi, Dong, Thomas Bayer, Christoffel P. S. Badenhorst, et al. "Recent trends in biocatalysis." Chemical Society Reviews 50, no. 14 (2021): 8003–49. http://dx.doi.org/10.1039/d0cs01575j.

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Technological developments enable the discovery of novel enzymes, the advancement of enzyme cascade designs and pathway engineering, moving biocatalysis into an era of technology integration, intelligent manufacturing and enzymatic total synthesis.

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Jung, Da-Woon, Woong-Hee Kim, and Darren R. Williams. "Chemical genetics and its application to moonlighting in glycolytic enzymes." Biochemical Society Transactions 42, no. 6 (2014): 1756–61. http://dx.doi.org/10.1042/bst20140201.

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Glycolysis is an ancient biochemical pathway that breaks down glucose into pyruvate to produce ATP. The structural and catalytic properties of glycolytic enzymes are well-characterized. However, there is growing appreciation that these enzymes participate in numerous moonlighting functions that are unrelated to glycolysis. Recently, chemical genetics has been used to discover novel moonlighting functions in glycolytic enzymes. In the present mini-review, we introduce chemical genetics and discuss how it can be applied to the discovery of protein moonlighting. Specifically, we describe the appl

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Celik, Cagla, Didar Tasdemir, Ayse Demirbas, et al. "Formation of functional nanobiocatalysts with a novel and encouraging immobilization approach and their versatile bioanalytical applications." RSC Advances 8, no. 45 (2018): 25298–303. http://dx.doi.org/10.1039/c8ra03250e.

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The discovery of functional organic–inorganic hybrid nanoflowers (FNFs) consisting of proteins/enzymes as the organic components and Cu(ii) ion as the inorganic component has made an enormous impact on enzyme immobilization studies.

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Kumari, Saroj. "Recent Trends in Omics-Based Enzyme Discovery to Combat Global Plastic Waste Crisis." Biotechnology Kiosk 3, no. 5 (2021): 4–12. http://dx.doi.org/10.37756/bk.21.3.5.1.

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The worldwide rapidly increasing amount of plastic waste is considered a major concern in the environmental crisis today. Recycling post-consumer plastics is believed to be a viable approach to mitigate the global plastic waste challenge. Plastic recycling is considered attractive due to the reason that it could help achieve waste valorization while meeting the goals of environmental quality standards. To this end, the current research efforts are heavily focused towards developing innovative technologies for new enzyme discoveries for effective plastic waste management. Recent research has sh

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Yan, Junjun, Peng Chen, Yan Zeng, et al. "The Characterization and Modification of a Novel Bifunctional and Robust Alginate Lyase Derived from Marinimicrobium sp. H1." Marine Drugs 17, no. 10 (2019): 545. http://dx.doi.org/10.3390/md17100545.

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Alginase lyase is an important enzyme for the preparation of alginate oligosaccharides (AOS), that possess special biological activities and is widely used in various fields, such as medicine, food, and chemical industry. In this study, a novel bifunctional alginate lyase (AlgH) belonging to the PL7 family was screened and characterized. The AlgH exhibited the highest activity at 45 °C and pH 10.0, and was an alkaline enzyme that was stable at pH 6.0–10.0. The enzyme showed no significant dependence on metal ions, and exhibited unchanged activity at high concentration of NaCl. To determine the

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Reisky, Lukas, Vishnu S. T. Srinivasamurthy, Chris P. S. Badenhorst, Simon P. Godehard, and Uwe T. Bornscheuer. "A Novel High-Throughput Assay Enables the Direct Identification of Acyltransferases." Catalysts 9, no. 1 (2019): 64. http://dx.doi.org/10.3390/catal9010064.

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Acyltransferases are enzymes that are capable of catalyzing the transesterification of non-activated esters in an aqueous environment and therefore represent interesting catalysts for applications in various fields. However, only a few acyltransferases have been identified so far, which can be explained by the lack of a simple, broadly applicable high-throughput assay for the identification of these enzymes from large libraries. Here, we present the development of such an assay that is based on the enzymatic formation of oligocarbonates from dimethyl carbonate and 1,6-hexanediol. In contrast t

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Robin, Frédéric, Julien Delmas, Elisabete Machado, Bernadette Bouchon, Luísa Peixe, and Richard Bonnet. "Characterization of the Novel CMT Enzyme TEM-154." Antimicrobial Agents and Chemotherapy 55, no. 3 (2010): 1262–65. http://dx.doi.org/10.1128/aac.01359-10.

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ABSTRACTTEM-154, identified in Portugal in 2004, associated the substitutions observed in the extended-spectrum β-lactamase (ESBL) TEM-12 and in the inhibitor-resistant penicillinase (IRT) TEM-33. This enzyme exhibited hydrolytic activity against ceftazidime and a low level of resistance to clavulanic acid. Surprisingly, the substitution Met69Leu enhanced the catalytic efficiency of oxyimino β-lactams conferred by the substitution Arg164Ser. Its discovery confirms the dissemination of the complex mutant group of TEM enzymes in European countries.

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Krupová, M., M. Gebauer, N. Schulten, H. Gül, M. Ren, and L. Schada Von Borzyskowski. "Discovery and characterization of novel enzymes for Nylon-6 upcycling." New Biotechnology 85 (March 2025): 216–17. https://doi.org/10.1016/j.nbt.2024.08.038.

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12

Tort, Olivia, Sebastián Tanco, Cecilia Rocha, et al. "The cytosolic carboxypeptidases CCP2 and CCP3 catalyze posttranslational removal of acidic amino acids." Molecular Biology of the Cell 25, no. 19 (2014): 3017–27. http://dx.doi.org/10.1091/mbc.e14-06-1072.

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The posttranslational modification of carboxy-terminal tails of tubulin plays an important role in the regulation of the microtubule cytoskeleton. Enzymes responsible for deglutamylating tubulin have been discovered within a novel family of mammalian cytosolic carboxypeptidases. The discovery of these enzymes also revealed the existence of a range of other substrates that are enzymatically deglutamylated. Only four of six mammalian cytosolic carboxypeptidases had been enzymatically characterized. Here we complete the functional characterization of this protein family by demonstrating that CCP2

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Hushpulian, Dmitry M., Irina N. Gaisina, Sergey V. Nikulin, et al. "HIGH THROUGHPUT SCREENING IN DRUG DISCOVERY: PROBLEMS AND SOLUTIONS." Lomonosov chemistry journal 65, no. 2, 2024 (2024): 96–112. http://dx.doi.org/10.55959/su0579-9384-2-2024-65-2-96-112.

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World-wide introduction of high throughput screening (HTS) methods in drug discovery research did not result in the increased number of novel medications on the market. We discuss novel trends in drug discovery that came from the understanding that majority of diseases are multifactorial and that one enzyme has many protein substrates. Hence, new approaches are focused on development of drugs, which (1) trigger survival pathways to return the organism to homeostatic balance, and (2) inhibit enzymes modifying histones or transcription factors not at the active site, but by displacement of prote

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Memon, Safyan Aman, Kinaan Aamir Khan, and Hammad Naveed. "HECNet: a hierarchical approach to enzyme function classification using a Siamese Triplet Network." Bioinformatics 36, no. 17 (2020): 4583–89. http://dx.doi.org/10.1093/bioinformatics/btaa536.

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Abstract Motivation Understanding an enzyme’s function is one of the most crucial problem domains in computational biology. Enzymes are a key component in all organisms and many industrial processes as they help in fighting diseases and speed up essential chemical reactions. They have wide applications and therefore, the discovery of new enzymatic proteins can accelerate biological research and commercial productivity. Biological experiments, to determine an enzyme’s function, are time-consuming and resource expensive. Results In this study, we propose a novel computational approach to predict

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15

Hubert, Catherine B., and Sarah M. Barry. "New chemistry from natural product biosynthesis." Biochemical Society Transactions 44, no. 3 (2016): 738–44. http://dx.doi.org/10.1042/bst20160063.

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Catalysts are a vital part of synthetic chemistry. However, there are still many important reactions for which catalysts have not been developed. The use of enzymes as biocatalysts for synthetic chemistry is growing in importance due to the drive towards sustainable methods for producing both bulk chemicals and high value compounds such as pharmaceuticals, and due to the ability of enzymes to catalyse chemical reactions with excellent stereoselectivity and regioselectivity. Such challenging transformations are a common feature of natural product biosynthetic pathways. In this mini-review, we d

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Herbert, Josephine, Angela H. Beckett, and Samuel C. Robson. "A Review of Cross-Disciplinary Approaches for the Identification of Novel Industrially Relevant Plastic-Degrading Enzymes." Sustainability 14, no. 23 (2022): 15898. http://dx.doi.org/10.3390/su142315898.

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The large-scale global use of plastics has led to one of the greatest environmental issues of the 21st century. The incredible durability of these polymers, whilst beneficial for a wide range of purposes, makes them hard to break down. True recycling of plastics is difficult and expensive, leading to accumulation in the environment as waste. Recently, a new field of research has developed, aiming to use natural biological processes to solve this man-made problem. Incredibly, some microorganisms are able to produce enzymes with the capacity to chemically break down plastic polymers into their m

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De Beul, Emma, Alana Jongbloet, Jorick Franceus, and Tom Desmet. "Discovery of a Kojibiose Hydrolase by Analysis of Specificity-Determining Correlated Positions in Glycoside Hydrolase Family 65." Molecules 26, no. 20 (2021): 6321. http://dx.doi.org/10.3390/molecules26206321.

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The Glycoside Hydrolase Family 65 (GH65) is an enzyme family of inverting α-glucoside phosphorylases and hydrolases that currently contains 10 characterized enzyme specificities. However, its sequence diversity has never been studied in detail. Here, an in-silico analysis of correlated mutations was performed, revealing specificity-determining positions that facilitate annotation of the family’s phylogenetic tree. By searching these positions for amino acid motifs that do not match those found in previously characterized enzymes from GH65, several clades that may harbor new functions could be

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Rolf, Jascha, Katrin Rosenthal, and Stephan Lütz. "Application of Cell-Free Protein Synthesis for Faster Biocatalyst Development." Catalysts 9, no. 2 (2019): 190. http://dx.doi.org/10.3390/catal9020190.

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Cell-free protein synthesis (CFPS) has become an established tool for rapid protein synthesis in order to accelerate the discovery of new enzymes and the development of proteins with improved characteristics. Over the past years, progress in CFPS system preparation has been made towards simplification, and many applications have been developed with regard to tailor-made solutions for specific purposes. In this review, various preparation methods of CFPS systems are compared and the significance of individual supplements is assessed. The recent applications of CFPS are summarized and the potent

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COLLINGRIDGE, PETER W., ROBERT W. B. BROWN, and MICHAEL L. GINGER. "Moonlighting enzymes in parasitic protozoa." Parasitology 137, no. 9 (2010): 1467–75. http://dx.doi.org/10.1017/s0031182010000259.

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SUMMARYEnzymes moonlight in a non-enzymatic capacity in a diverse variety of cellular processes. The discovery of these non-enzymatic functions is generally unexpected, and moonlighting enzymes are known in both prokaryotes and eukaryotes. Importantly, this unexpected multi-functionality indicates that caution might be needed on some occasions in interpreting phenotypes that result from the deletion or gene-silencing of some enzymes, including some of the best known enzymes from classic intermediary metabolism. Here, we provide an overview of enzyme moonlighting in parasitic protists. Unequivo

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Magalhães, Rita P., Jorge M. Cunha, and Sérgio F. Sousa. "Perspectives on the Role of Enzymatic Biocatalysis for the Degradation of Plastic PET." International Journal of Molecular Sciences 22, no. 20 (2021): 11257. http://dx.doi.org/10.3390/ijms222011257.

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Plastics are highly durable and widely used materials. Current methodologies of plastic degradation, elimination, and recycling are flawed. In recent years, biodegradation (the usage of microorganisms for material recycling) has grown as a valid alternative to previously used methods. The evolution of bioengineering techniques and the discovery of novel microorganisms and enzymes with degradation ability have been key. One of the most produced plastics is PET, a long chain polymer of terephthalic acid (TPA) and ethylene glycol (EG) repeating monomers. Many enzymes with PET degradation activity

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Ziemert, Nadine, Keishi Ishida, Philippe Quillardet, et al. "Microcyclamide Biosynthesis in Two Strains of Microcystis aeruginosa: from Structure to Genes and Vice Versa." Applied and Environmental Microbiology 74, no. 6 (2008): 1791–97. http://dx.doi.org/10.1128/aem.02392-07.

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ABSTRACT Comparative analysis of related biosynthetic gene clusters can provide new insights into the versatility of these pathways and allow the discovery of new natural products. The freshwater cyanobacterium Microcystis aeruginosa NIES298 produces the cytotoxic peptide microcyclamide. Here, we provide evidence that the cyclic hexapeptide is formed by a ribosomal pathway through the activity of a set of processing enzymes closely resembling those recently shown to be involved in patellamide biosynthesis in cyanobacterial symbionts of ascidians. Besides two subtilisin-type proteases and a het

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Luis, Ana S., and Eric C. Martens. "Interrogating gut bacterial genomes for discovery of novel carbohydrate degrading enzymes." Current Opinion in Chemical Biology 47 (December 2018): 126–33. http://dx.doi.org/10.1016/j.cbpa.2018.09.012.

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Kwon, Yong-Chan, Kyung-Ho Lee, Ho-Cheol Kim та ін. "Cloning-Independent Expression and Analysis of ω-Transaminases by Use of a Cell-Free Protein Synthesis System". Applied and Environmental Microbiology 76, № 18 (2010): 6295–98. http://dx.doi.org/10.1128/aem.00029-10.

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ABSTRACT Herewith we report the expression and screening of microbial enzymes without involving cloning procedures. Computationally predicted putative ω-transaminase (ω-TA) genes were PCR amplified from the bacterial colonies and expressed in a cell-free protein synthesis system for subsequent analysis of their enzymatic activity and substrate specificity. Through the cell-free expression analysis of the putative ω-TA genes, a number of enzyme-substrate pairs were identified in a matter of hours. We expect that the proposed strategy will provide a universal platform for bridging the informatio

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Maitlo, Majid Ali, Anwar Hussain Phulpoto, Muneer Ahmed Qazi, Sadam Hussain Shaikh, Sham Lal, and Nisar Ahmed Kanhar. "Biocatalytic Strategies for Environmental Pollutant Degradation: Advancing Enzymatic and Molecular Innovations." Journal of Microbiological Sciences 3, no. 01 (2024): 66–81. https://doi.org/10.38211/jms.2024.03.121.

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Biocatalytic approaches, leveraging enzymatic and molecular mechanisms, offer sustainable solutions for degrading environmental pollutants. This review explores the role of microbial enzyme transforming persistent contaminants such as polycyclic aromatic hydrocarbons, dyes, and endocrine disruptors into less harmful compounds. The specificity and efficiency of these enzymes make them effective in various environmental matrices. Advancements in enzyme immobilization techniques have enhanced their stability and reusability, addressing challenges related to operational conditions and cost-effecti

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Yuan, Yifeng, Rémi Zallot, Tyler L. Grove, et al. "Discovery of novel bacterial queuine salvage enzymes and pathways in human pathogens." Proceedings of the National Academy of Sciences 116, no. 38 (2019): 19126–35. http://dx.doi.org/10.1073/pnas.1909604116.

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Queuosine (Q) is a complex tRNA modification widespread in eukaryotes and bacteria that contributes to the efficiency and accuracy of protein synthesis. Eukaryotes are not capable of Q synthesis and rely on salvage of the queuine base (q) as a Q precursor. While many bacteria are capable of Q de novo synthesis, salvage of the prokaryotic Q precursors preQ0 and preQ1 also occurs. With the exception of Escherichia coli YhhQ, shown to transport preQ0 and preQ1, the enzymes and transporters involved in Q salvage and recycling have not been well described. We discovered and characterized 2 Q salvag

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H, Javid. "Short Note on Biotechnological Application of Halophilic Enzymes." Open Access Journal of Microbiology & Biotechnology 6, no. 3 (2021): 1–5. http://dx.doi.org/10.23880/oajmb-16000200.

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Evolution of life in extreme environments entails wide adaptations. Amongst these environments, those with high salt concentration are abodes to so-called halophilic microorganisms. The unique key properties of halophilic proteins not only enable them to survive in hostile and precluding environments, but also make their enzymes as precious biocatalysts in pharmaceutical, fine chemical processes, industries, food processing, detergents, waste treatments, etc., where harsh conditions prevent favorable reactions by normal enzymes. Unfortunately, due to lack of deep knowledge and proper equipment

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McCormack, J. G. "Applying science to drug discovery." Biochemical Society Transactions 34, no. 2 (2006): 238–42. http://dx.doi.org/10.1042/bst0340238.

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Scientists and science in the pharmaceutical industry rely heavily on the more academically orientated basic research carried out at Universities, for first of all training, but also as a source of new ideas and approaches to drug discovery. Progress in the discovery and development of novel therapeutics benefits from a healthy alliance with, and the output from, more basic research institutions, and the reverse is also true, with many advances in understanding of physiological and pathological processes being as the result of the application of novel targeted molecules. To illustrate this, so

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Ganley, Jack G., and Emily R. Derbyshire. "Linking Genes to Molecules in Eukaryotic Sources: An Endeavor to Expand Our Biosynthetic Repertoire." Molecules 25, no. 3 (2020): 625. http://dx.doi.org/10.3390/molecules25030625.

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The discovery of natural products continues to interest chemists and biologists for their utility in medicine as well as facilitating our understanding of signaling, pathogenesis, and evolution. Despite an attenuation in the discovery rate of new molecules, the current genomics and transcriptomics revolution has illuminated the untapped biosynthetic potential of many diverse organisms. Today, natural product discovery can be driven by biosynthetic gene cluster (BGC) analysis, which is capable of predicting enzymes that catalyze novel reactions and organisms that synthesize new chemical structu

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Franceus, Jorick, and Tom Desmet. "Sucrose Phosphorylase and Related Enzymes in Glycoside Hydrolase Family 13: Discovery, Application and Engineering." International Journal of Molecular Sciences 21, no. 7 (2020): 2526. http://dx.doi.org/10.3390/ijms21072526.

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Sucrose phosphorylases are carbohydrate-active enzymes with outstanding potential for the biocatalytic conversion of common table sugar into products with attractive properties. They belong to the glycoside hydrolase family GH13, where they are found in subfamily 18. In bacteria, these enzymes catalyse the phosphorolysis of sucrose to yield α-glucose 1-phosphate and fructose. However, sucrose phosphorylases can also be applied as versatile transglucosylases for the synthesis of valuable glycosides and sugars because their broad promiscuity allows them to transfer the glucosyl group of sucrose

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Guebitz, Georg M., Felice Quartinello, and Doris Ribitsch. "ENZYME BASED RECYCLING PROCESSES." Detritus, no. 20 (September 14, 2022): 13–16. http://dx.doi.org/10.31025/2611-4135/2022.15214.

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Novel strategies allowing environmentally friendly recycling of plastics are strongly needed. Enzymes have shown high potential, especially for the recovery of building blocks from multilayer materials which will be discussed in this paper. It has been shown that enzymes can specifically hydrolyze and solubilize certain components of blended packaging materials or mixed wastes. This allows a step—wise recovery of valuable building blocks which can be used for re-synthesis or for bioproduction (e.g. recovered glucose). However, despite the high potential of biocatalysts, even more efficient enz

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Chang, Te-Sheng. "Functional Approaches to Discover New Compounds via Enzymatic Modification: Predicted Data Mining Approach and Biotransformation-Guided Purification." Molecules 30, no. 10 (2025): 2228. https://doi.org/10.3390/molecules30102228.

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In the field of biotechnology, natural compounds isolated from medicinal plants are highly valued; however, their discovery, purification, biofunctional characterization, and biochemical validation have historically involved time-consuming and laborious processes. Two innovative approaches have emerged to more efficiently discover new bioactive substances: the predicted data mining approach (PDMA) and biotransformation-guided purification (BGP). The PDMA is a computational method that predicts biotransformation potential, identifying potential substrates for specific enzymes from numerous cand

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Marblestone, Jeffrey G., K. G. Suresh Kumar, Michael J. Eddins, et al. "Novel Approach for Characterizing Ubiquitin E3 Ligase Function." Journal of Biomolecular Screening 15, no. 10 (2010): 1220–28. http://dx.doi.org/10.1177/1087057110380456.

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The ubiquitin-proteasome system is central to the regulation of numerous cellular events, and dysregulation may lead to disease pathogenesis. E3 ubiquitin ligases typically function in concert with E1 and E2 enzymes to recruit specific substrates, thereby coordinating their ubiquitylation and subsequent proteasomal degradation or cellular activity. E3 ligases have been implicated in a wide range of pathologies, and monitoring their activity in a rapid and cost-effective manner would be advantageous in drug discovery. The relative lack of high-throughput screening (HTS)–compliant E3 ligase assa

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Visvanathan, Ramya, Tadanobu Utsuki, Daniel E. Beck та ін. "A novel micellular fluorogenic substrate for quantitating the activity of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma (PLCγ) enzymes". PLOS ONE 19, № 3 (2024): e0299541. http://dx.doi.org/10.1371/journal.pone.0299541.

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The activities of the phospholipase C gamma (PLCγ) 1 and 2 enzymes are essential for numerous cellular processes. Unsurprisingly, dysregulation of PLCγ1 or PLCγ2 activity is associated with multiple maladies including immune disorders, cancers, and neurodegenerative diseases. Therefore, the modulation of either of these two enzymes has been suggested as a therapeutic strategy to combat these diseases. To aid in the discovery of PLCγ family enzyme modulators that could be developed into therapeutic agents, we have synthesized a high-throughput screening-amenable micellular fluorogenic substrate

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Damada, Pedro H., and Marco W. Fraaije. "Identification of Five Robust Novel Ene-Reductases from Thermophilic Fungi." Catalysts 14, no. 11 (2024): 764. http://dx.doi.org/10.3390/catal14110764.

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Ene-reductases (ERs) are enzymes known for catalyzing the asymmetric hydrogenation of activated alkenes. Among these, old yellow enzyme (OYE) ERs have been the most extensively studied for biocatalytic applications due to their dependence on NADH or NADPH as electron donors. These flavin-containing enzymes are highly enantio- and stereoselective, making them attractive biocatalysts for industrial use. To discover novel thermostable OYE-type ERs, we explored genomes of thermophilic fungi. Five genes encoding ERs were selected and expressed in Escherichia coli, namely AtOYE (from Aspergillus the

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Eniyan, Kandasamy, Jyoti Rani, Srinivasan Ramachandran, Rahul Bhat, Inshad Ali Khan, and Urmi Bajpai. "Screening of Antitubercular Compound Library Identifies Inhibitors of Mur Enzymes in Mycobacterium tuberculosis." SLAS DISCOVERY: Advancing the Science of Drug Discovery 25, no. 1 (2019): 70–78. http://dx.doi.org/10.1177/2472555219881148.

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The rapid rise in the emergence of multidrug-resistant (MDR) and extensively drug-resistant (XDR) strains of Mycobacterium tuberculosis (Mtb) mandates the discovery of novel tuberculosis (TB) drugs. Mur enzymes, which are identified as essential proteins in Mtb and catalyze the cytoplasmic steps in the peptidoglycan biosynthetic pathway, are considered potential drug targets. However, none of the clinical drugs have yet been developed against these enzymes. Hence, the aim of this study was to identify novel inhibitors of Mur enzymes in Mycobacterium tuberculosis. We screened an antitubercular

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Jarman, Michael, S. Elaine Barrie, John J. Deadman, John Houghton, Raymond McCague, and Martin G. Rowlands. "Hydroxyperfluoroazobenzenes: novel inhibitors of enzymes of androgen biosynthesis." Journal of Medicinal Chemistry 33, no. 9 (1990): 2452–55. http://dx.doi.org/10.1021/jm00171a019.

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Tupec, Michal, Aleš Buček, Irena Valterová, and Iva Pichová. "Biotechnological potential of insect fatty acid-modifying enzymes." Zeitschrift für Naturforschung C 72, no. 9-10 (2017): 387–403. http://dx.doi.org/10.1515/znc-2017-0031.

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AbstractThere are more than one million described insect species. This species richness is reflected in the diversity of insect metabolic processes. In particular, biosynthesis of secondary metabolites, such as defensive compounds and chemical signals, encompasses an extraordinarily wide range of chemicals that are generally unparalleled among natural products from other organisms. Insect genomes, transcriptomes and proteomes thus offer a valuable resource for discovery of novel enzymes with potential for biotechnological applications. Here, we focus on fatty acid (FA) metabolism-related enzym

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Zeeman, Samuel C., Thierry Delatte, Gaëlle Messerli, et al. "Starch breakdown: recent discoveries suggest distinct pathways and novel mechanisms." Functional Plant Biology 34, no. 6 (2007): 465. http://dx.doi.org/10.1071/fp06313.

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The aim of this article is to provide an overview of current models of starch breakdown in leaves. We summarise the results of our recent work focusing on Arabidopsis, relating them to other work in the field. Early biochemical studies of starch containing tissues identified numerous enzymes capable of participating in starch degradation. In the non-living endosperms of germinated cereal seeds, starch breakdown proceeds by the combined actions of α-amylase, limit dextrinase (debranching enzyme), β-amylase and α-glucosidase. The activities of these enzymes and the regulation of some of the resp

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Harada, Masamitsu, Jun Nagai, Riho Kurata, et al. "Establishment of Novel High-Standard Chemiluminescent Assay for NTPase in Two Protozoans and Its High-Throughput Screening." Marine Drugs 18, no. 3 (2020): 161. http://dx.doi.org/10.3390/md18030161.

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Toxoplasma gondii is a major protozoan parasite and infects human and many other warm-blooded animals. The infection leads to Toxoplasmosis, a serious issue in AIDS patients, organ transplant recipients and pregnant women. Neospora caninum, another type of protozoa, is closely related to Toxoplasma gondii. Infections of the protozoa in animals also causes serious diseases such as Encephalomyelitis and Myositis-Polyradiculitis in dogs or abortion in cows. Both Toxoplasma gondii and Neospora caninum have similar nucleoside triphosphate hydrolases (NTPase), NcNTPase and TgNTPase-I in Neospora can

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Franceus, Jorik, and Tom Desmet. "Sucrose Phosphorylase and Related Enzymes in Glycoside Hydrolase Family 13: Discovery, Application and Engineering." International Journal of Molecular Sciences 21, no. 7 (2020): 2526. https://doi.org/10.3390/ijms21072526.

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<strong>Abstract</strong> Sucrose phosphorylases are carbohydrate-active enzymes with outstanding potential for the biocatalytic conversion of common table sugar into products with attractive properties. They belong to the glycoside hydrolase family GH13, where they are found in subfamily 18. In bacteria, these enzymes catalyse the phosphorolysis of sucrose to yield alpha-glucose 1-phosphate and fructose. However, sucrose phosphorylases can also be applied as versatile transglucosylases for the synthesis of valuable glycosides and sugars because their broad promiscuity allo

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Mehta, Kunal, Mihir Khambete, Arundhati Abhyankar, and Abdelwahab Omri. "Anti-Tuberculosis Mur Inhibitors: Structural Insights and the Way Ahead for Development of Novel Agents." Pharmaceuticals 16, no. 3 (2023): 377. http://dx.doi.org/10.3390/ph16030377.

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Mur enzymes serve as critical molecular devices for the synthesis of UDP-MurNAc-pentapeptide, the main building block of bacterial peptidoglycan polymer. These enzymes have been extensively studied for bacterial pathogens such as Escherichia coli and Staphylococcus aureus. Various selective and mixed Mur inhibitors have been designed and synthesized in the past few years. However, this class of enzymes remains relatively unexplored for Mycobacterium tuberculosis (Mtb), and thus offers a promising approach for drug design to overcome the challenges of battling this global pandemic. This review

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Slama, Houda Ben, Ali Chenari Bouket, Faizah N. Alenezi, et al. "Potentials of Endophytic Fungi in the Biosynthesis of Versatile Secondary Metabolites and Enzymes." Forests 12, no. 12 (2021): 1784. http://dx.doi.org/10.3390/f12121784.

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World population growth and modernization have engendered multiple environmental problems: the propagation of humans and crop diseases and the development of multi-drug-resistant fungi, bacteria and viruses. Thus, a considerable shift towards eco-friendly products has been seen in medicine, pharmacy, agriculture and several other vital sectors. Nowadays, studies on endophytic fungi and their biotechnological potentials are in high demand due to their substantial, cost-effective and eco-friendly contributions in the discovery of an array of secondary metabolites. For this review, we provide a b

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Brandish, Philip E., Chi-Sung Chiu, Jonathan Schneeweis, et al. "A Cell-Based Ultra-High-Throughput Screening Assay for Identifying Inhibitors of D-Amino Acid Oxidase." Journal of Biomolecular Screening 11, no. 5 (2006): 481–87. http://dx.doi.org/10.1177/1087057106288181.

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Enzymes are often considered less “druggable” targets than ligand-regulated proteins such as G-protein-coupled receptors, ion channels, or other hormone receptors. Reasons for this include cellular location (intracellular vs. cell surface), typically lower affinities for the binding of small molecules compared to ligand-specific receptors, and binding (catalytic) sites that are often charged or highly polar. A practical drawback to the discovery of compounds targeting enzymes is that screening of compound libraries is typically carried out in cell-free activity assays using purified protein in

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Schaeffer, Marie, Joerg Schroeder, Anja R. Heckeroth, et al. "Identification of Lead Compounds Targeting the Cathepsin B-Like Enzyme of Eimeria tenella." Antimicrobial Agents and Chemotherapy 56, no. 3 (2011): 1190–201. http://dx.doi.org/10.1128/aac.05528-11.

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ABSTRACTCysteine peptidases have been implicated in the development and pathogenesis ofEimeria. We have identified a single-copy cathepsin B-like cysteine peptidase gene in the genome database ofEimeria tenella(EtCatB). Molecular modeling of the predicted protein suggested that it differs significantly from host enzymes and could be a good drug target. EtCatB was expressed and secreted as a soluble, active, glycosylated mature enzyme fromPichia pastoris. Biochemical characterization of the recombinant enzyme confirmed that it is cathepsin B-like. Screening of a focused library against the enzy

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Olmeda, Isidoro, Francisco Paredes-Martínez, Ramón Sendra, Patricia Casino, Isabel Pardo, and Sergi Ferrer. "Biochemical and Structural Characterization of a Novel Psychrophilic Laccase (Multicopper Oxidase) Discovered from Oenococcus oeni 229 (ENOLAB 4002)." International Journal of Molecular Sciences 25, no. 15 (2024): 8521. http://dx.doi.org/10.3390/ijms25158521.

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Recently, prokaryotic laccases from lactic acid bacteria (LAB), which can degrade biogenic amines, were discovered. A laccase enzyme has been cloned from Oenococcus oeni, a very important LAB in winemaking, and it has been expressed in Escherichia coli. This enzyme has similar characteristics to those previously isolated from LAB as the ability to oxidize canonical substrates such as 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), 2,6-dimethoxyphenol (2,6-DMP), and potassium ferrocyanide K4[Fe(CN6)], and non-conventional substrates as biogenic amines. However, it presents some di

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Sartaj, Km, Alok Patel, Leonidas Matsakas, and Ramasare Prasad. "Unravelling Metagenomics Approach for Microbial Biofuel Production." Genes 13, no. 11 (2022): 1942. http://dx.doi.org/10.3390/genes13111942.

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Renewable biofuels, such as biodiesel, bioethanol, and biobutanol, serve as long-term solutions to fossil fuel depletion. A sustainable approach feedstock for their production is plant biomass, which is degraded to sugars with the aid of microbes-derived enzymes, followed by microbial conversion of those sugars to biofuels. Considering their global demand, additional efforts have been made for their large-scale production, which is ultimately leading breakthrough research in biomass energy. Metagenomics is a powerful tool allowing for functional gene analysis and new enzyme discovery. Thus, th

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Kadian, Kavita, Yash Gupta, Harsh Vardhan Singh, Prakasha Kempaiah, and Manmeet Rawat. "Apicoplast Metabolism: Parasite’s Achilles’ Heel." Current Topics in Medicinal Chemistry 18, no. 22 (2019): 1987–97. http://dx.doi.org/10.2174/1568026619666181130134742.

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Malaria continues to impinge heavily on mankind, with five continents still under its clasp. Widespread and rapid emergence of drug resistance in the Plasmodium parasite to current therapies accentuate the quest for novel drug targets and antimalarial compounds. Plasmodium parasites, maintain a non-photosynthetic relict organelle known as Apicoplast. Among the four major pathways of Apicoplast, biosynthesis of isoprenoids via Methylerythritol phosphate (MEP) pathway is the only indispensable function of Apicoplast that occurs during different stages of the malaria parasite. Moreover, the human

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Miao, Qin, Xiaoling Zhang, Yitong Wang, et al. "Characterization of Novel Pectinolytic Enzymes Derived from the Efficient Lignocellulose Degradation Microbiota." Biomolecules 12, no. 10 (2022): 1388. http://dx.doi.org/10.3390/biom12101388.

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Diverse pectinolytic enzymes are widely applied in the food, papermaking, and other industries, and they account for more than 25% of the global industrial enzyme demands. Efficient lignocellulose degradation microbiota are reservoirs of pectinolytic enzymes and other lignocellulose-degrading genes. Metagenomics has been widely used to discover new pectinolytic enzymes. Here, we used a metagenomic strategy to characterize pectinolytic genes from one efficient lignocellulose-degrading microbiota derived from pulp and paper wastewater treatment microbiota. A total of 23 predicted full-length GH2

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Ferraris, Davide M., Edoardo L. M. Gelardi, Silvia Garavaglia, Riccardo Miggiano, and Menico Rizzi. "Targeting NAD-dependent dehydrogenases in drug discovery against infectious diseases and cancer." Biochemical Society Transactions 48, no. 2 (2020): 693–707. http://dx.doi.org/10.1042/bst20191261.

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Dehydrogenases are oxidoreductase enzymes that play a variety of fundamental functions in the living organisms and have primary roles in pathogen survival and infection processes as well as in cancer development. We review here a sub-set of NAD-dependent dehydrogenases involved in human diseases and the recent advancements in drug development targeting pathogen-associated NAD-dependent dehydrogenases. We focus also on the molecular aspects of the inhibition process listing the structures of the most relevant molecules targeting this enzyme family. Our aim is to review the most impacting findin

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Ariaeenejad, Shohreh, Javad Gharechahi, Mehdi Foroozandeh Shahraki, et al. "Precision enzyme discovery through targeted mining of metagenomic data." Natural Products and Bioprospecting 14, no. 1 (2024). http://dx.doi.org/10.1007/s13659-023-00426-8.

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AbstractMetagenomics has opened new avenues for exploring the genetic potential of uncultured microorganisms, which may serve as promising sources of enzymes and natural products for industrial applications. Identifying enzymes with improved catalytic properties from the vast amount of available metagenomic data poses a significant challenge that demands the development of novel computational and functional screening tools. The catalytic properties of all enzymes are primarily dictated by their structures, which are predominantly determined by their amino acid sequences. However, this aspect h

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