{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T21:09:43Z","timestamp":1791925783166,"version":"4.3.4"},"reference-count":51,"publisher":"MDPI AG","issue":"13","license":[{"start":{"date-parts":[[2024,6,21]],"date-time":"2024-06-21T00:00:00Z","timestamp":1718928000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Universidad Popular Aut\u00f3noma del Estado de Puebla"},{"name":"Consejo de Ciencia y tecnolog\u00eda del Estado de Puebla"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The initial adoption of penicillin as an antibiotic marked the start of exploring other compounds essential for pharmaceuticals, yet resistance to penicillins and their side effects has compromised their efficacy. The N-terminal nucleophile (Ntn) amide-hydrolases S45 family plays a key role in catalyzing amide bond hydrolysis in various compounds, including antibiotics like penicillin and cephalosporin. This study comprehensively analyzes the structural and functional traits of the bacterial N-terminal nucleophile (Ntn) amide-hydrolases S45 family, covering penicillin G acylases, cephalosporin acylases, and D-succinylase. Utilizing structural bioinformatics tools and sequence analysis, the investigation delineates structurally conserved regions (SCRs) and substrate binding site variations among these enzymes. Notably, sixteen SCRs crucial for substrate interaction are identified solely through sequence analysis, emphasizing the significance of sequence data in characterizing functionally relevant regions. These findings introduce a novel approach for identifying targets to enhance the biocatalytic properties of N-terminal nucleophile (Ntn) amide-hydrolases, while facilitating the development of more accurate three-dimensional models, particularly for enzymes lacking structural data. Overall, this research advances our understanding of structure\u2013function relationships in bacterial N-terminal nucleophile (Ntn) amide-hydrolases, providing insights into strategies for optimizing their enzymatic capabilities.<\/jats:p>","DOI":"10.3390\/ijms25136850","type":"journal-article","created":{"date-parts":[[2024,6,21]],"date-time":"2024-06-21T12:27:33Z","timestamp":1718972853000},"page":"6850","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Exploring the Structurally Conserved Regions and Functional Significance in Bacterial N-Terminal Nucleophile (Ntn) Amide-Hydrolases"],"prefix":"10.3390","volume":"25","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0545-8232","authenticated-orcid":false,"given":"Israel","family":"Quiroga","sequence":"first","affiliation":[{"name":"Department of Life and Health Sciences, Universidad Popular Aut\u00f3noma del Estado de Puebla, 13 Poniente No. 1927, Barrio de Santiago, Puebla 72410, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0002-8783-0770","authenticated-orcid":false,"given":"Juan Andr\u00e9s","family":"Hern\u00e1ndez-Gonz\u00e1lez","sequence":"additional","affiliation":[{"name":"Department of Life and Health Sciences, Universidad Popular Aut\u00f3noma del Estado de Puebla, 13 Poniente No. 1927, Barrio de Santiago, Puebla 72410, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0410-0415","authenticated-orcid":false,"given":"Elizabeth","family":"Bautista-Rodr\u00edguez","sequence":"additional","affiliation":[{"name":"Department of Life and Health Sciences, Universidad Popular Aut\u00f3noma del Estado de Puebla, 13 Poniente No. 1927, Barrio de Santiago, Puebla 72410, Mexico"},{"name":"Department of Health Sciences, Universidad Aut\u00f3noma de Tlaxcala, Sur 11, Barrio de Guardia, Zacatelco 90070, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5333-3069","authenticated-orcid":false,"given":"Alfredo C.","family":"Ben\u00edtez-Rojas","sequence":"additional","affiliation":[{"name":"Department of Life and Health Sciences, Universidad Popular Aut\u00f3noma del Estado de Puebla, 13 Poniente No. 1927, Barrio de Santiago, Puebla 72410, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,6,21]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"3825","DOI":"10.1007\/s00253-016-7399-6","article-title":"A Breakthrough in Enzyme Technology to Fight Penicillin Resistance\u2014Industrial Application of Penicillin Amidase","volume":"100","author":"Buchholz","year":"2016","journal-title":"Appl. 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