{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,19]],"date-time":"2026-01-19T11:21:37Z","timestamp":1768821697511,"version":"3.49.0"},"reference-count":37,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,5,1]],"date-time":"2025-05-01T00:00:00Z","timestamp":1746057600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001843","name":"Science and Engineering Research Board","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001843","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100014824","name":"Department of Pharmaceuticals, Ministry of Chemicals and Fertilizers, India","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100014824","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001409","name":"Department of Science and Technology, Ministry of Science and Technology, India","doi-asserted-by":"publisher","award":["CRG\/2022\/002746"],"award-info":[{"award-number":["CRG\/2022\/002746"]}],"id":[{"id":"10.13039\/501100001409","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Gene"],"published-print":{"date-parts":[[2025,5]]},"DOI":"10.1016\/j.gene.2025.149335","type":"journal-article","created":{"date-parts":[[2025,2,15]],"date-time":"2025-02-15T23:47:58Z","timestamp":1739663278000},"page":"149335","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":2,"special_numbering":"C","title":["Leishmania donovani homoserine dehydrogenase: Biochemical and structural characterization of a novel parasite specific enzyme of aspartate pathway"],"prefix":"10.1016","volume":"947","author":[{"given":"Sandra","family":"Lalchhuanawmi","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chandan","family":"Kumar Malik","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rajender","family":"Kumar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Swati","family":"Verma","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Prabha","family":"Garg","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sushma","family":"Singh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.gene.2025.149335_b0005","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1016\/j.cimid.2004.03.004","article-title":"Leishmaniasis: current situation and new perspectives","volume":"27","author":"Desjeux","year":"2004","journal-title":"Comp. Immunol. Microbiol. Infect. Dis."},{"key":"10.1016\/j.gene.2025.149335_b0010","unstructured":"J.A. Ruiz-Postigo, S. Jain, S. Madjou, A.N. Maia-Elkhoury, S. Valadas, S. Warusavithana, M. Osman, A. Yajima, Z. Lin, A. Beshah, Global leishmaniasis surveillance: 2021, assessing the impact of the COVID-19 pandemic, Wkly. Epidemiol. Rec. (2023) 575\u2013590."},{"key":"10.1016\/j.gene.2025.149335_b0015","doi-asserted-by":"crossref","DOI":"10.3389\/fmicb.2022.1052478","article-title":"Leishmaniasis: recent epidemiological studies in the Middle East","volume":"13","author":"Knight","year":"2023","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.gene.2025.149335_b0020","doi-asserted-by":"crossref","first-page":"1385","DOI":"10.1515\/pac-2018-1102","article-title":"Current and promising novel drug candidates against visceral leishmaniasis","volume":"91","author":"Reguera","year":"2019","journal-title":"Pure Appl. Chem."},{"key":"10.1016\/j.gene.2025.149335_b0025","doi-asserted-by":"crossref","first-page":"1590","DOI":"10.3390\/pharmaceutics14081590","article-title":"Metabolic pathways of Leishmania parasite: source of pertinent drug targets and potent drug candidates","volume":"14","author":"Jain","year":"2022","journal-title":"Pharmaceutics"},{"key":"10.1016\/j.gene.2025.149335_b0030","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1007\/s00726-014-1873-1","article-title":"Inhibitors of amino acids biosynthesis as antifungal agents","volume":"47","author":"Jastrz\u0119bowska","year":"2015","journal-title":"Amino Acids"},{"key":"10.1016\/j.gene.2025.149335_b0035","doi-asserted-by":"crossref","first-page":"950","DOI":"10.3390\/pathogens11080950","article-title":"Development of novel anti-leishmanials: the case for structure-based approaches","volume":"11","author":"Soni","year":"2022","journal-title":"Pathogens"},{"key":"10.1016\/j.gene.2025.149335_b0040","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12934-015-0275-8","article-title":"Determination of key enzymes for threonine synthesis through in vitro metabolic pathway analysis","volume":"14","author":"Zhang","year":"2015","journal-title":"Microb. Cell Fact."},{"key":"10.1016\/j.gene.2025.149335_b0045","doi-asserted-by":"crossref","first-page":"1905","DOI":"10.4014\/jmb.2004.04060","article-title":"Molecular and enzymatic features of homoserine dehydrogenase from Bacillus subtilis","volume":"30","author":"Nguyen","year":"2020","journal-title":"J. Microbiol. Biotechnol."},{"key":"10.1016\/j.gene.2025.149335_b0050","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.bbrep.2015.07.006","article-title":"Structural insight into activation of homoserine dehydrogenase from the archaeon Sulfolobus tokodaii via reduction","volume":"3","author":"Tomonaga","year":"2015","journal-title":"Biochem. Biophys. Reports"},{"key":"10.1016\/j.gene.2025.149335_b0055","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1007\/s00425-008-0772-7","article-title":"Polyamines: essential factors for growth and survival","volume":"228","author":"Kusano","year":"2008","journal-title":"Planta"},{"key":"10.1016\/j.gene.2025.149335_b0060","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1111\/mmi.12351","article-title":"The threonine degradation pathway of the Trypanosoma brucei procyclic form: the main carbon source for lipid biosynthesis is under metabolic control","volume":"90","author":"Millerioux","year":"2013","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.gene.2025.149335_b0065","doi-asserted-by":"crossref","first-page":"9065","DOI":"10.3390\/ijms22169065","article-title":"Reconstruction of the diaminopimelic acid pathway to promote L-lysine production in Corynebacterium glutamicum","volume":"22","author":"Liu","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.gene.2025.149335_b0070","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1016\/j.jmii.2016.03.001","article-title":"Candida albicans Hom6 is a homoserine dehydrogenase involved in protein synthesis and cell adhesion","volume":"50","author":"Tsai","year":"2017","journal-title":"J. Microbiol. Immunol. Infect."},{"key":"10.1016\/j.gene.2025.149335_b0075","doi-asserted-by":"crossref","first-page":"3825","DOI":"10.1016\/j.bmc.2004.05.009","article-title":"New phenolic inhibitors of yeast homoserine dehydrogenase","volume":"12","author":"Ejim","year":"2004","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.gene.2025.149335_b0080","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1016\/j.chembiol.2003.09.015","article-title":"Enzyme-assisted suicide: molecular basis for the antifungal activity of 5-hydroxy-4-oxonorvaline by potent inhibition of homoserine dehydrogenase","volume":"10","author":"Jacques","year":"2003","journal-title":"Chem. Biol."},{"key":"10.1016\/j.gene.2025.149335_b0085","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1016\/j.ijbiomac.2019.09.209","article-title":"Structural exploration of glutamine synthetase from Leishmania donovani: Insights from in silico and in vitro analysis","volume":"146","author":"Kumar","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.gene.2025.149335_b0090","doi-asserted-by":"crossref","first-page":"1658","DOI":"10.1093\/bioinformatics\/btl158","article-title":"Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences","volume":"22","author":"Li","year":"2006","journal-title":"Bioinformatics"},{"key":"10.1016\/j.gene.2025.149335_b0095","doi-asserted-by":"crossref","first-page":"3022","DOI":"10.1093\/molbev\/msab120","article-title":"MEGA11: molecular evolutionary genetics analysis version 11","volume":"38","author":"Tamura","year":"2021","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.gene.2025.149335_b0100","doi-asserted-by":"crossref","unstructured":"H. Ashkenazy, S. Abadi, E. Martz, O. Chay, I. Mayrose, T. Pupko, N. Ben-Tal, ConSurf 2016: an improved methodology to estimate and visualize evolutionary conservation in macromolecules, Nucleic Acids Res. 44 (2016) W344\u2013W350.","DOI":"10.1093\/nar\/gkw408"},{"key":"10.1016\/j.gene.2025.149335_b0105","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.gene.2025.149335_b0110","doi-asserted-by":"crossref","first-page":"2785","DOI":"10.1002\/jcc.21256","article-title":"AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility","volume":"30","author":"Morris","year":"2009","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.gene.2025.149335_b0115","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera\u2014a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.gene.2025.149335_b0120","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1002\/minf.201200128","article-title":"Molecular modeling and active site binding mode characterization of aspartate \u03b2\u2010semialdehyde dehydrogenase family","volume":"32","author":"Kumar","year":"2013","journal-title":"Mol. Inform."},{"key":"10.1016\/j.gene.2025.149335_b0125","doi-asserted-by":"crossref","first-page":"1082","DOI":"10.1080\/07391102.2014.929535","article-title":"Shape-based virtual screening, docking, and molecular dynamics simulations to identify Mtb-ASADH inhibitors","volume":"33","author":"Kumar","year":"2015","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.gene.2025.149335_b0130","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1038\/73359","article-title":"Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases","volume":"7","author":"DeLaBarre","year":"2000","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.gene.2025.149335_b0135","doi-asserted-by":"crossref","first-page":"1216","DOI":"10.1107\/S1399004715004617","article-title":"Structural basis for the catalytic mechanism of homoserine dehydrogenase","volume":"71","author":"Navratna","year":"2015","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"10.1016\/j.gene.2025.149335_b0140","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1074\/jbc.M109.068882","article-title":"Threonine-insensitive Homoserine Dehydrogenase from Soybean genomic organization, kinetic mechanism, and in vivo activity","volume":"285","author":"Schroeder","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.gene.2025.149335_b0150","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-018-24063-1","article-title":"Inhibition of homoserine dehydrogenase by formation of a cysteine-NAD covalent complex","volume":"8","author":"Ogata","year":"2018","journal-title":"Sci. Rep."},{"key":"10.1016\/j.gene.2025.149335_b0155","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/j.procbio.2022.01.019","article-title":"Characterization of a novel type homoserine dehydrogenase with high oxidation activity from Arthrobacter nicotinovorans","volume":"114","author":"Liang","year":"2022","journal-title":"Process Biochem."},{"key":"10.1016\/j.gene.2025.149335_b0160","doi-asserted-by":"crossref","DOI":"10.1016\/j.pep.2021.105909","article-title":"Biochemical characterization and redesign of the coenzyme specificity of a novel monofunctional NAD+-dependent homoserine dehydrogenase from the human pathogen Neisseria gonorrhoeae","volume":"186","author":"Tang","year":"2021","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.gene.2025.149335_b0165","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1002\/bkcs.11929","article-title":"Biochemical characterization of homoserine dehydrogenase from Pseudomonas aeruginosa","volume":"41","author":"Kim","year":"2020","journal-title":"Bull. Korean Chem. Soc."},{"key":"10.1016\/j.gene.2025.149335_b0170","doi-asserted-by":"crossref","first-page":"5779","DOI":"10.1016\/S0021-9258(18)62720-6","article-title":"Homoserine dehydrogenase of Rhodospirillum rubrum: II. purification and characterization of the enzyme","volume":"245","author":"Datta","year":"1970","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.gene.2025.149335_b0175","doi-asserted-by":"crossref","first-page":"5332","DOI":"10.1016\/S0021-9258(19)63351-X","article-title":"Threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. kinetic and spectroscopic effects upon binding of serine and threonine","volume":"252","author":"Costrejean","year":"1977","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.gene.2025.149335_b0180","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1093\/jb\/mvy094","article-title":"The crystal structure of homoserine dehydrogenase complexed with l-homoserine and NADPH in a closed form","volume":"165","author":"Akai","year":"2019","journal-title":"J. Biochem."},{"key":"10.1016\/j.gene.2025.149335_b0185","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1111\/j.1744-7348.2006.00074.x","article-title":"Lysine and threonine biosynthesis in sorghum seeds: characterisation of aspartate kinase and homoserine dehydrogenase isoenzymes","volume":"149","author":"Ferreira","year":"2006","journal-title":"Ann. Appl. Biol."},{"key":"10.1016\/j.gene.2025.149335_b0190","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1093\/oxfordjournals.jbchem.a123427","article-title":"Inhibition of homoserine dehydrogenase I by L-serine in Escherichia coli","volume":"109","author":"Hama","year":"1991","journal-title":"J. Biochem."}],"container-title":["Gene"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0378111925001234?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0378111925001234?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,2,27]],"date-time":"2025-02-27T18:13:46Z","timestamp":1740680026000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0378111925001234"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,5]]},"references-count":37,"alternative-id":["S0378111925001234"],"URL":"https:\/\/doi.org\/10.1016\/j.gene.2025.149335","relation":{},"ISSN":["0378-1119"],"issn-type":[{"value":"0378-1119","type":"print"}],"subject":[],"published":{"date-parts":[[2025,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Leishmania donovani homoserine dehydrogenase: Biochemical and structural characterization of a novel parasite specific enzyme of aspartate pathway","name":"articletitle","label":"Article Title"},{"value":"Gene","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.gene.2025.149335","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"149335"}}