EnzymesPub Date : 2024-01-01Epub Date: 2024-06-08DOI: 10.1016/bs.enz.2024.05.011
Katrina J Holly, Molly S Youse, Daniel P Flaherty
{"title":"Enterococci carbonic anhydrase inhibition.","authors":"Katrina J Holly, Molly S Youse, Daniel P Flaherty","doi":"10.1016/bs.enz.2024.05.011","DOIUrl":"https://doi.org/10.1016/bs.enz.2024.05.011","url":null,"abstract":"<p><p>Carbonic anhydrase metalloenzymes are encoded in genomes throughout all kingdoms of life with a conserved function catalyzing the reversible conversion of CO<sub>2</sub> to bicarbonate. Carbonic anhydrases have been well-investigated in humans, but are still relatively understudied in bacterial organisms, including Enterococci. Studies over the past decade have presented bacterial carbonic anhydrases as potential drug targets, with some chemical scaffolds potently inhibiting the Enterococcus carbonic anhydrases in vitro and displaying antimicrobial efficacy against Enterococcus organisms. While carbonic anhydrases in Enterococci still have much to be explored, hypotheses may be drawn from similar Gram-positive organisms for which known information exists about carbonic anhydrase function and relevance. Within this chapter is reported information and rational hypotheses regarding the subcellar locations, potential physiological roles, essentiality, structures, and kinetics of carbonic anhydrases in Enterococci.</p>","PeriodicalId":39097,"journal":{"name":"Enzymes","volume":"55 ","pages":"283-311"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142120830","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
EnzymesPub Date : 2024-01-01Epub Date: 2024-07-26DOI: 10.1016/bs.enz.2024.07.001
Vincenzo Massimiliano Vivenzio, Davide Esposito, Simona Maria Monti, Giuseppina De Simone
{"title":"Bacterial α-CAs: a biochemical and structural overview.","authors":"Vincenzo Massimiliano Vivenzio, Davide Esposito, Simona Maria Monti, Giuseppina De Simone","doi":"10.1016/bs.enz.2024.07.001","DOIUrl":"https://doi.org/10.1016/bs.enz.2024.07.001","url":null,"abstract":"<p><p>Carbonic anhydrases belonging to the α-class are widely distributed in bacterial species. These enzymes have been isolated from bacteria with completely different characteristics including both Gram-negative and Gram-positive strains. α-CAs show a considerable similarity when comparing the biochemical, kinetic and structural features, with only small differences which reflect the diverse role these enzymes play in Nature. In this chapter, we provide a comprehensive overview on bacterial α-CA data, with a highlight to their potential biomedical and biotechnological applications.</p>","PeriodicalId":39097,"journal":{"name":"Enzymes","volume":"55 ","pages":"31-63"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142120824","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
EnzymesPub Date : 2024-01-01Epub Date: 2024-08-23DOI: 10.1016/bs.enz.2024.05.002
Andrea Angeli
{"title":"Bacterial γ-carbonic anhydrases.","authors":"Andrea Angeli","doi":"10.1016/bs.enz.2024.05.002","DOIUrl":"https://doi.org/10.1016/bs.enz.2024.05.002","url":null,"abstract":"<p><p>Carbonic anhydrases (CAs) are a ubiquitous family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide to bicarbonate and protons, playing pivotal roles in a variety of biological processes including respiration, calcification, acid-base balance, and CO<sub>2</sub> fixation. Recent studies have expanded the understanding of CAs, particularly the γ-class from diverse biological sources such as pathogenic bacteria, extremophiles, and halophiles, revealing their unique structural adaptations and functional mechanisms that enable operation under extreme environmental conditions. This chapter discusses the comprehensive catalytic mechanism and structural insights from X-ray crystallography studies, highlighting the molecular adaptations that confer stability and activity to these enzymes in harsh environments. It also explores the modulation mechanism of these enzymes, detailing how different modulators interact with the active site of γ-CAs. Comparative analyzes with other CA classes elucidate the evolutionary trajectories and functional diversifications of these enzymes. The synthesis of this knowledge not only sheds light on the fundamental aspects of CA biology but also opens new avenues for therapeutic and industrial applications, particularly in designing targeted inhibitors for pathogenic bacteria and developing biocatalysts for industrial processes under extreme conditions. The continuous advancement in structural biology promises further insights into this enzyme family, potentially leading to novel applications in medical and environmental biotechnology.</p>","PeriodicalId":39097,"journal":{"name":"Enzymes","volume":"55 ","pages":"93-120"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142120826","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
EnzymesPub Date : 2024-01-01Epub Date: 2024-07-05DOI: 10.1016/bs.enz.2024.06.006
Alessio Nocentini
{"title":"Sulfonamide inhibitors of bacterial carbonic anhydrases.","authors":"Alessio Nocentini","doi":"10.1016/bs.enz.2024.06.006","DOIUrl":"https://doi.org/10.1016/bs.enz.2024.06.006","url":null,"abstract":"<p><p>The increasing prevalence of antibiotic-resistant bacteria necessitates the exploration of novel therapeutic targets. Bacterial carbonic anhydrases (CAs) have been known for decades, but only in the past ten years they have garnered significant interest as drug targets to develop antibiotics having a diverse mechanism of action compared to the clinically used drugs. Significant progress has been made in the field in the past three years, with the validation in vivo of CAs from Neisseria gonorrhoeae, and vancomycin-resistant enterococci as antibiotic targets. This chapter compiles the state-of-the-art research on sulfonamide derivatives described as inhibitors of all known bacterial CAs. A section delves into the mechanisms of action of sulfonamide compounds with the CA classes identified in pathogenic bacteria, specifically α, β, and γ classes. Therefore, the inhibitory profiling of the bacterial CAs with classical and clinically used sulfonamide compounds is reported and analyzed. Another section covers various other series of sulfonamide CA inhibitors studied for the development of new antibiotics. By synthesizing current research findings, this chapter highlights the potential of sulfonamide inhibitors as a novel class of antibacterial agents and paves the way for future drug design strategies.</p>","PeriodicalId":39097,"journal":{"name":"Enzymes","volume":"55 ","pages":"143-191"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142120836","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
EnzymesPub Date : 2024-01-01Epub Date: 2024-09-07DOI: 10.1016/bs.enz.2024.05.005
Luigi Pisano, Martina Turco, Claudiu T Supuran
{"title":"Biomedical applications of tyrosinases and tyrosinase inhibitors.","authors":"Luigi Pisano, Martina Turco, Claudiu T Supuran","doi":"10.1016/bs.enz.2024.05.005","DOIUrl":"https://doi.org/10.1016/bs.enz.2024.05.005","url":null,"abstract":"<p><p>Tyrosinase is involved in several human diseases, among which hypopigmentation and depigmentation conditions (vitiligo, idiopathic guttate hypomelanosis, pityriasis versicolor, pityriasis alba) and hyperpigmentations (melasma, lentigines, post-inflammatory and periorbital hyperpigmentation, cervical idiopathic poikiloderma and acanthosis nigricans). There are increasing evidences that tyrosinase plays a relevant role in the formation and progression of melanoma, a difficult to treat skin tumor. Hydroquinone, azelaic acid and tretinoin (all-trans-retinoic acid) are clinically used in the management of some hyperpigmentations, whereas many novel chemotypes acting as tyrosinase inhibitors with potential antimelanoma action are being investigated. Kojic acid, hydroquinone, its glycosylated derivative arbutin, or the resorcinol derivative rucinol are used in cosmesis in creams as skin whitening agents, whereas no antimelanoma tyrosinase inhibitor reached clinical trials so far, although thiamidol is a recently approved new tyrosinase inhibitor for the treatment of melasma. Kojic acid and vitamin C are used for avoiding vegetable/food oxidative browning due to the tyrosinase-catalyzed reactions, whereas bacterial enzymes show potential in biotechnological applications, for the production of mixed melanins, for protein cross-linking reactions, for producing phenol(s) biosensors, of for the production of L-DOPA, an anti-Parkinson's disease drug.</p>","PeriodicalId":39097,"journal":{"name":"Enzymes","volume":"56 ","pages":"261-280"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142297667","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
EnzymesPub Date : 2024-01-01Epub Date: 2024-09-10DOI: 10.1016/bs.enz.2024.06.005
Fosca Errante, Lucrezia Sforzi, Claudiu T Supuran, Anna Maria Papini, Paolo Rovero
{"title":"Peptide and peptidomimetic tyrosinase inhibitors.","authors":"Fosca Errante, Lucrezia Sforzi, Claudiu T Supuran, Anna Maria Papini, Paolo Rovero","doi":"10.1016/bs.enz.2024.06.005","DOIUrl":"10.1016/bs.enz.2024.06.005","url":null,"abstract":"<p><p>Melanin, which is produced by melanocytes and spread over keratinocytes, is responsible for human skin browning. There are several processes involved in melanogenesis, mostly prompted by enzymatic activities. Tyrosinase (TYR), a copper containing metalloenzyme, is considered the main actor in melanin production, as it catalyzes two crucial steps that modify tyrosine residues in dopaquinone. For this reason, TYR inhibition has been exploited as a possible mechanism of modulation of hyper melanogenesis. There are various types of molecules used to block TYR activity, principally used as skin whitening agents in cosmetic products, e.g., tretinoin, hydroquinone, azelaic acid, kojic acid, arbutin and peptides. Peptides are highly valued for their versatile nature, making them promising candidates for various functions. Their specificity often leads to excellent safety, tolerability, and efficacy in humans, which can be considered their primary advantage over traditional small molecules. There are several examples of tyrosinase inhibitor peptides (TIPs) operating as possible hypo-pigmenting agents, which can be classified according to their origin: natural, hybrid or synthetically produced. Moreover, the possibility of variating their backbones, introducing non-canonical amino acids or modifying one or more peptide bond(s), to obtain peptidomimetic molecules, is an added value to avoid or delay proteolytic activity, while the possibility of conjugation with other bioactive peptides or organic moieties can bring other specific activity leading to dual-functional peptides.</p>","PeriodicalId":39097,"journal":{"name":"Enzymes","volume":"56 ","pages":"135-189"},"PeriodicalIF":0.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142297673","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
EnzymesPub Date : 2023-01-01Epub Date: 2023-09-27DOI: 10.1016/bs.enz.2023.09.001
Fuyuhiko Tamanoi
{"title":"History of The Enzymes: 1950-2023.","authors":"Fuyuhiko Tamanoi","doi":"10.1016/bs.enz.2023.09.001","DOIUrl":"10.1016/bs.enz.2023.09.001","url":null,"abstract":"<p><p>Since its publication in 1950, the series \"The Enzymes\" has been established as an important reference book for researchers and students in the field of enzymology, biochemistry and biophysics and medical research. A number of scientists have served as a series editor for the Enzymes. Topics covered range from characterizations of various enzymes, biochemical processes and medical applications. This chapter provides an overview of the history of The Enzymes.</p>","PeriodicalId":39097,"journal":{"name":"Enzymes","volume":"54 ","pages":"3-11"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72015664","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
EnzymesPub Date : 2023-01-01Epub Date: 2023-04-21DOI: 10.1016/bs.enz.2023.03.003
Jonatan Caroli, Andrea Mattevi
{"title":"The NPAC-LSD2 complex in nucleosome demethylation.","authors":"Jonatan Caroli, Andrea Mattevi","doi":"10.1016/bs.enz.2023.03.003","DOIUrl":"10.1016/bs.enz.2023.03.003","url":null,"abstract":"<p><p>NPAC is a transcriptional co-activator widely associated with the H3K36me3 epigenetic marks present in the gene bodies. NPAC plays a fundamental role in RNA polymerase progression, and its depletion downregulates gene transcription. In this chapter, we review the current knowledge on the functional and structural features of this multi-domain protein. NPAC (also named GLYR1 or NP60) contains a PWWP motif, a chromatin binder and epigenetic reader that is proposed to weaken the DNA-histone contacts facilitating polymerase passage through the nucleosomes. The C-terminus of NPAC is a catalytically inactive dehydrogenase domain that forms a stable and rigid tetramer acting as an oligomerization module for the formation of co-transcriptional multimeric complexes. The PWWP and dehydrogenase domains are connected by a long, mostly disordered, linker that comprises putative sites for protein and DNA interactions. A short dodecapeptide sequence (residues 214-225) forms the binding site for LSD2, a flavin-dependent lysine-specific histone demethylase. This stretch of residues binds on the surface of LSD2 and facilitates the capture and processing of the H3 tail in the nucleosome context, thus promoting the H3K4me1/2 epigenetic mark removal. LSD2 is associated with other two chromatin modifiers, G9a and NSD3. The LSD2-G9a-NSD3 complex modifies the pattern of the post translational modifications deposited on histones, thus converting the relaxed chromatin into a transcriptionally refractory state after the RNA polymerase passage. NPAC is a scaffolding factor that organizes and coordinates the epigenetic activities required for optimal transcription elongation.</p>","PeriodicalId":39097,"journal":{"name":"Enzymes","volume":"53 ","pages":"97-111"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41157659","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
EnzymesPub Date : 2023-01-01Epub Date: 2023-07-31DOI: 10.1016/bs.enz.2023.07.002
Howard T Jacobs
{"title":"A century of mitochondrial research, 1922-2022.","authors":"Howard T Jacobs","doi":"10.1016/bs.enz.2023.07.002","DOIUrl":"10.1016/bs.enz.2023.07.002","url":null,"abstract":"<p><p>Although recognized earlier as subcellular entities by microscopists, mitochondria have been the subject of functional studies since 1922, when their biochemical similarities with bacteria were first noted. In this overview I trace the history of research on mitochondria from that time up to the present day, focussing on the major milestones of the overlapping eras of mitochondrial biochemistry, genetics, pathology and cell biology, and its explosion into new areas in the past 25 years. Nowadays, mitochondria are considered to be fully integrated into cell physiology, rather than serving specific functions in isolation.</p>","PeriodicalId":39097,"journal":{"name":"Enzymes","volume":"54 ","pages":"37-70"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72015659","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
EnzymesPub Date : 2023-01-01Epub Date: 2023-07-28DOI: 10.1016/bs.enz.2023.07.001
Lee Bardwell, Jeremy Thorner
{"title":"Mitogen-activated protein kinase (MAPK) cascades-A yeast perspective.","authors":"Lee Bardwell, Jeremy Thorner","doi":"10.1016/bs.enz.2023.07.001","DOIUrl":"10.1016/bs.enz.2023.07.001","url":null,"abstract":"<p><p>Discovery of the class of protein kinase now dubbed a mitogen (or messenger)-activated protein kinase (MAPK) is an illustrative example of how disparate lines of investigation can converge and reveal an enzyme family universally conserved among eukaryotes, from single-celled microbes to humans. Moreover, elucidation of the circuitry controlling MAPK function defined a now overarching principle in enzyme regulation-the concept of an activation cascade mediated by sequential phosphorylation events. Particularly ground-breaking for this field of exploration were the contributions of genetic approaches conducted using several model organisms, but especially the budding yeast Saccharomyces cerevisiae. Notably, examination of how haploid yeast cells respond to their secreted peptide mating pheromones was crucial in pinpointing genes encoding MAPKs and their upstream activators. Fully contemporaneous biochemical analysis of the activities elicited upon stimulation of mammalian cells by insulin and other growth- and differentiation-inducing factors lead eventually to the demonstration that components homologous to those in yeast were involved. Continued studies of these pathways in yeast were integral to other foundational discoveries in MAPK signaling, including the roles of tethering, scaffolding and docking interactions.</p>","PeriodicalId":39097,"journal":{"name":"Enzymes","volume":"54 ","pages":"137-170"},"PeriodicalIF":0.0,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72015666","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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