{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,5]],"date-time":"2026-11-05T06:28:46Z","timestamp":1793860126110,"version":"4.6.1"},"reference-count":72,"publisher":"Springer Science and Business Media LLC","issue":"6","license":[{"start":{"date-parts":[[2026,9,12]],"date-time":"2026-09-12T00:00:00Z","timestamp":1789171200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2026,9,12]],"date-time":"2026-09-12T00:00:00Z","timestamp":1789171200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"funder":[{"DOI":"10.13039\/100020473","name":"Badan Riset dan Inovasi Nasional","doi-asserted-by":"publisher","award":["B-5647\/II.7.5\/RT.01.01\/4\/2025"],"award-info":[{"award-number":["B-5647\/II.7.5\/RT.01.01\/4\/2025"]}],"id":[{"id":"10.13039\/100020473","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Divers"],"DOI":"10.1007\/s11030-026-11731-y","type":"journal-article","created":{"date-parts":[[2026,9,12]],"date-time":"2026-09-12T15:36:30Z","timestamp":1789227390000},"page":"11135-11151","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Lipase ITB 2.1: a structure- and function-validated model for anti-obesity drug screening"],"prefix":"10.1007","volume":"30","author":[{"given":"Ilma Fauziah","family":"Ma\u2019ruf","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Teni","family":"Ernawati","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Faris","family":"Hermawan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Akhmaloka","family":"Akhmaloka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fida Madayanti","family":"Warganegara","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Made Puspasari","family":"Widhiastuty","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elvi","family":"Restiawaty","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hesti Lina","family":"Wiraswati","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ahmad","family":"Wibisana","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tjandrawati","family":"Mozef","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nur Akmalia","family":"Hidayati","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Titin","family":"Haryati","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dimas Frananta","family":"Simatupang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,9,12]]},"reference":[{"issue":"8","key":"11731_CR1","doi-asserted-by":"publisher","first-page":"794","DOI":"10.1056\/NEJMsr1606602","volume":"375","author":"B Lauby-Secretan","year":"2016","unstructured":"Lauby-Secretan B, Scoccianti C, Loomis D, Grosse Y, Bianchini F, Straif K (2016) Body fatness and cancer\u2013viewpoint of the IARC Working Group. N Engl J Med 375(8):794\u2013798. https:\/\/doi.org\/10.1056\/NEJMsr1606602","journal-title":"N Engl J Med"},{"key":"11731_CR2","doi-asserted-by":"publisher","first-page":"615375","DOI":"10.3389\/fonc.2020.615375","volume":"10","author":"T Scully","year":"2020","unstructured":"Scully T, Ettela A, LeRoith D, Gallagher EJ, Obesity (2020) Type 2 diabetes, and cancer risk. Front Oncol 10:615375. https:\/\/doi.org\/10.3389\/fonc.2020.615375","journal-title":"Front Oncol"},{"issue":"10113","key":"11731_CR3","doi-asserted-by":"publisher","first-page":"2627","DOI":"10.1016\/s0140-6736(17)32129-3","volume":"390","author":"NCD-RisC","year":"2017","unstructured":"NCD-RisC (2017) Worldwide trends in body-mass index, underweight, overweight, and obesity from 1975 to 2016: a pooled analysis of 2416 population-based measurement studies in 128\u00b79 million children, adolescents, and adults. Lancet 390(10113):2627\u20132642. https:\/\/doi.org\/10.1016\/s0140-6736(17)32129-3","journal-title":"Lancet"},{"key":"11731_CR4","unstructured":"WHO (2023) Noncommunicable diseases. https:\/\/www.who.int\/news-room\/fact-sheets\/detail\/noncommunicable-diseases"},{"key":"11731_CR5","unstructured":"IDF (2021) IDF Diabetes Atlas (10th ed.). https:\/\/diabetesatlas.org"},{"issue":"3","key":"11731_CR6","doi-asserted-by":"publisher","first-page":"209","DOI":"10.3322\/caac.21660","volume":"71","author":"H Sung","year":"2021","unstructured":"Sung H, Ferlay J, Siegel RL, Laversanne M, Soerjomataram I, Jemal A et al (2021) Global Cancer Statistics 2020: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries. CA Cancer J Clin 71(3):209\u2013249. https:\/\/doi.org\/10.3322\/caac.21660","journal-title":"CA Cancer J Clin"},{"key":"11731_CR7","doi-asserted-by":"publisher","first-page":"5832","DOI":"10.1038\/srep05832","volume":"4","author":"J Zhang","year":"2014","unstructured":"Zhang J, Zhao Y, Xu C, Hong Y, Lu H, Wu J et al (2014) Association between serum free fatty acid levels and nonalcoholic fatty liver disease: a cross-sectional study. Sci Rep 4:5832. https:\/\/doi.org\/10.1038\/srep05832","journal-title":"Sci Rep"},{"issue":"12","key":"11731_CR8","doi-asserted-by":"publisher","first-page":"1071","DOI":"10.1111\/obr.12318","volume":"16","author":"NM Aldekhail","year":"2015","unstructured":"Aldekhail NM, Logue J, McLoone P, Morrison DS (2015) Effect of orlistat on glycaemic control in overweight and obese patients with type 2 diabetes mellitus: a systematic review and meta-analysis of randomized controlled trials. Obes Rev 16(12):1071\u20131080. https:\/\/doi.org\/10.1111\/obr.12318","journal-title":"Obes Rev"},{"key":"11731_CR9","doi-asserted-by":"publisher","first-page":"110314","DOI":"10.1016\/j.biopha.2020.110314","volume":"128","author":"TT Liu","year":"2020","unstructured":"Liu TT, Liu XT, Chen QX, Shi Y (2020) Lipase inhibitors for obesity: a review. Biomed Pharmacother 128:110314. https:\/\/doi.org\/10.1016\/j.biopha.2020.110314","journal-title":"Biomed Pharmacother"},{"issue":"1","key":"11731_CR10","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1016\/j.cell.2009.11.027","volume":"140","author":"DK Nomura","year":"2010","unstructured":"Nomura DK, Long JZ, Niessen S, Hoover HS, Ng SW, Cravatt BF (2010) Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis. Cell 140(1):49\u201361. https:\/\/doi.org\/10.1016\/j.cell.2009.11.027","journal-title":"Cell"},{"issue":"1","key":"11731_CR11","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1620\/tjem.256.19","volume":"256","author":"X Gong","year":"2022","unstructured":"Gong X, Zheng X, Huang Y, Song W, Chen G, Chen T (2022) Monoacylglycerol lipase (MAGL) inhibition impedes the osteosarcoma progression by regulating epithelial mesenchymal transition. Tohoku J Exp Med 256(1):19\u201326. https:\/\/doi.org\/10.1620\/tjem.256.19","journal-title":"Tohoku J Exp Med"},{"issue":"3","key":"11731_CR12","doi-asserted-by":"publisher","first-page":"2850","DOI":"10.3892\/mmr.2016.4829","volume":"13","author":"M Ma","year":"2016","unstructured":"Ma M, Bai J, Ling Y, Chang W, Xie G, Li R et al (2016) Monoacylglycerol lipase inhibitor JZL184 regulates apoptosis and migration of colorectal cancer cells. Mol Med Rep 13(3):2850\u20132856. https:\/\/doi.org\/10.3892\/mmr.2016.4829","journal-title":"Mol Med Rep"},{"issue":"5","key":"11731_CR13","doi-asserted-by":"publisher","first-page":"787","DOI":"10.1158\/1535-7163.Mct-20-0589","volume":"20","author":"JL Pr\u00fcser","year":"2021","unstructured":"Pr\u00fcser JL, Ramer R, Wittig F, Ivanov I, Merkord J, Hinz B (2021) The monoacylglycerol lipase inhibitor JZL184 inhibits lung cancer cell invasion and metastasis via the CB(1) cannabinoid receptor. Mol Cancer Ther 20(5):787\u2013802. https:\/\/doi.org\/10.1158\/1535-7163.Mct-20-0589","journal-title":"Mol Cancer Ther"},{"issue":"9","key":"11731_CR14","doi-asserted-by":"publisher","first-page":"20774","DOI":"10.3390\/ijms160920774","volume":"16","author":"GM Borrelli","year":"2015","unstructured":"Borrelli GM, Trono D (2015) Recombinant lipases and phospholipases and their use as biocatalysts for industrial applications. Int J Mol Sci 16(9):20774\u201320840. https:\/\/doi.org\/10.3390\/ijms160920774","journal-title":"Int J Mol Sci"},{"issue":"4","key":"11731_CR15","doi-asserted-by":"publisher","first-page":"390","DOI":"10.1016\/s0958-1669(02)00341-5","volume":"13","author":"KE Jaeger","year":"2002","unstructured":"Jaeger KE, Eggert T (2002) Lipases for biotechnology. Curr Opin Biotechnol 13(4):390\u2013397. https:\/\/doi.org\/10.1016\/s0958-1669(02)00341-5","journal-title":"Curr Opin Biotechnol"},{"issue":"17","key":"11731_CR16","doi-asserted-by":"publisher","first-page":"9933","DOI":"10.3390\/ijms23179933","volume":"23","author":"CA Godoy","year":"2022","unstructured":"Godoy CA, Pardo-Tamayo JS, Barbosa O (2022) Microbial lipases and their potential in the production of pharmaceutical building blocks. Int J Mol Sci 23(17):9933","journal-title":"Int J Mol Sci"},{"key":"11731_CR17","doi-asserted-by":"publisher","first-page":"1081","DOI":"10.13005\/bbra\/2545","volume":"14","author":"A Permana","year":"2017","unstructured":"Permana A, Warganegara F, Wahyuningrum D, Widhiastuty M, Akhmaloka A (2017) Heterologous expression and characterization of thermostable lipases from Geobacillus thermoleovorans PPD2 through Escherichia coli. Biosci Biotechnol Res Asia 14:1081\u20131088. https:\/\/doi.org\/10.13005\/bbra\/2545","journal-title":"Biosci Biotechnol Res Asia"},{"key":"11731_CR18","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1016\/j.jtbi.2015.03.035","volume":"374","author":"FI Khan","year":"2015","unstructured":"Khan FI, Govender A, Permaul K, Singh S, Bisetty K (2015) Thermostable chitinase II from Thermomyces lanuginosus SSBP: cloning, structure prediction and molecular dynamics simulations. J Theor Biol 374:107\u2013114. https:\/\/doi.org\/10.1016\/j.jtbi.2015.03.035","journal-title":"J Theor Biol"},{"key":"11731_CR19","doi-asserted-by":"publisher","DOI":"10.3390\/ijms20040884","author":"S Ali","year":"2019","unstructured":"Ali S, Khan FI, Mohammad T, Lan D, Hassan MI, Wang Y (2019) Identification and evaluation of inhibitors of lipase from Malassezia restricta using virtual high-throughput screening and molecular dynamics studies. Int J Mol Sci. https:\/\/doi.org\/10.3390\/ijms20040884","journal-title":"Int J Mol Sci"},{"issue":"7","key":"11731_CR20","doi-asserted-by":"publisher","first-page":"2295","DOI":"10.1093\/nar\/gkn072","volume":"36","author":"J Pei","year":"2008","unstructured":"Pei J, Kim BH, Grishin NV (2008) PROMALS3D: a tool for multiple protein sequence and structure alignments. Nucleic Acids Res 36(7):2295\u20132300. https:\/\/doi.org\/10.1093\/nar\/gkn072","journal-title":"Nucleic Acids Res"},{"issue":"7","key":"11731_CR21","doi-asserted-by":"publisher","first-page":"3022","DOI":"10.1093\/molbev\/msab120","volume":"38","author":"K Tamura","year":"2021","unstructured":"Tamura K, Stecher G, Kumar S (2021) MEGA11: molecular evolutionary genetics analysis version 11. Mol Biol Evol 38(7):3022\u20133027. https:\/\/doi.org\/10.1093\/molbev\/msab120","journal-title":"Mol Biol Evol"},{"issue":"2","key":"11731_CR22","doi-asserted-by":"publisher","first-page":"e17000","DOI":"10.1371\/journal.pone.0017000","volume":"6","author":"H Nacke","year":"2011","unstructured":"Nacke H, Th\u00fcrmer A, Wollherr A, Will C, Hodac L, Herold N et al (2011) Pyrosequencing-based assessment of bacterial community structure along different management types in German forest and grassland soils. PLoS ONE 6(2):e17000. https:\/\/doi.org\/10.1371\/journal.pone.0017000","journal-title":"PLoS ONE"},{"key":"11731_CR23","doi-asserted-by":"publisher","first-page":"763","DOI":"10.1007\/s00253-004-1568-8","volume":"64","author":"R Gupta","year":"2004","unstructured":"Gupta R, Gupta N, Rathi P (2004) Bacterial lipases: An overview of production, purification and biochemical properties. Appl Microbiol Biotechnol 64:763\u2013781. https:\/\/doi.org\/10.1007\/s00253-004-1568-8","journal-title":"Appl Microbiol Biotechnol"},{"issue":"1","key":"11731_CR24","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1093\/nar\/28.1.235","volume":"28","author":"HM Berman","year":"2000","unstructured":"Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H et al (2000) The protein data bank. Nucleic Acids Res 28(1):235\u2013242. https:\/\/doi.org\/10.1093\/nar\/28.1.235","journal-title":"Nucleic Acids Res"},{"issue":"13","key":"11731_CR25","doi-asserted-by":"publisher","first-page":"1605","DOI":"10.1002\/jcc.20084","volume":"25","author":"EF Pettersen","year":"2004","unstructured":"Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC et al (2004) UCSF Chimera\u2013a visualization system for exploratory research and analysis. J Comput Chem 25(13):1605\u20131612. https:\/\/doi.org\/10.1002\/jcc.20084","journal-title":"J Comput Chem"},{"issue":"7873","key":"11731_CR26","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","volume":"596","author":"J Jumper","year":"2021","unstructured":"Jumper J, Evans R, Pritzel A, Green T, Figurnov M, Ronneberger O et al (2021) Highly accurate protein structure prediction with AlphaFold. Nature 596(7873):583\u2013589. https:\/\/doi.org\/10.1038\/s41586-021-03819-2","journal-title":"Nature"},{"issue":"8","key":"11731_CR27","doi-asserted-by":"publisher","first-page":"3891","DOI":"10.1021\/acs.jcim.1c00203","volume":"61","author":"J Eberhardt","year":"2021","unstructured":"Eberhardt J, Santos-Martins D, Tillack AF, Forli S, AutoDock (2021) Vina 1.2.0: new docking methods, expanded force field, and python bindings. J Chem Inf Model 61(8):3891\u20133898. https:\/\/doi.org\/10.1021\/acs.jcim.1c00203","journal-title":"J Chem Inf Model"},{"issue":"1","key":"11731_CR28","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1186\/s13321-019-0362-7","volume":"11","author":"EW Bell","year":"2019","unstructured":"Bell EW, Zhang Y (2019) DockRMSD: an open-source tool for atom mapping and RMSD calculation of symmetric molecules through graph isomorphism. J Cheminform 11(1):40. https:\/\/doi.org\/10.1186\/s13321-019-0362-7","journal-title":"J Cheminform"},{"key":"11731_CR29","unstructured":"Schr\u00f6dinger L (2015) The PyMOL Molecular Graphics System, Version 3.1.0. https:\/\/www.pymol.org\/"},{"issue":"3","key":"11731_CR30","doi-asserted-by":"publisher","first-page":"435","DOI":"10.1021\/ct700301q","volume":"4","author":"B Hess","year":"2008","unstructured":"Hess B, Kutzner C, van der Spoel D, Lindahl E (2008) GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4(3):435\u2013447. https:\/\/doi.org\/10.1021\/ct700301q","journal-title":"J Chem Theory Comput"},{"issue":"25","key":"11731_CR31","doi-asserted-by":"publisher","first-page":"2135","DOI":"10.1002\/jcc.23354","volume":"34","author":"J Huang","year":"2013","unstructured":"Huang J, MacKerell AD Jr. (2013) CHARMM36 all-atom additive protein force field: validation based on comparison to NMR data. J Comput Chem 34(25):2135\u20132145. https:\/\/doi.org\/10.1002\/jcc.23354","journal-title":"J Comput Chem"},{"issue":"12","key":"11731_CR32","doi-asserted-by":"publisher","first-page":"3155","DOI":"10.1021\/ci3003649","volume":"52","author":"K Vanommeslaeghe","year":"2012","unstructured":"Vanommeslaeghe K, Raman EP, MacKerell AD Jr (2012) Automation of the CHARMM General Force Field (CGenFF) II: assignment of bonded parameters and partial atomic charges. J Chem Inf Model 52(12):3155\u20133168. https:\/\/doi.org\/10.1021\/ci3003649","journal-title":"J Chem Inf Model"},{"issue":"1","key":"11731_CR33","doi-asserted-by":"publisher","first-page":"014101","DOI":"10.1063\/1.2408420","volume":"126","author":"G Bussi","year":"2007","unstructured":"Bussi G, Donadio D, Parrinello M (2007) Canonical sampling through velocity rescaling. J Chem Phys 126(1):014101. https:\/\/doi.org\/10.1063\/1.2408420","journal-title":"J Chem Phys"},{"issue":"11","key":"11731_CR34","doi-asserted-by":"publisher","first-page":"114107","DOI":"10.1063\/5.0020514","volume":"153","author":"M Bernetti","year":"2020","unstructured":"Bernetti M, Bussi G (2020) Pressure control using stochastic cell rescaling. J Chem Phys 153(11):114107. https:\/\/doi.org\/10.1063\/5.0020514","journal-title":"J Chem Phys"},{"issue":"12","key":"11731_CR35","doi-asserted-by":"publisher","first-page":"10089","DOI":"10.1063\/1.464397","volume":"98","author":"T Darden","year":"1993","unstructured":"Darden T, York D, Pedersen L (1993) Particle mesh Ewald: An N\u22c5log(N) method for Ewald sums in large systems. J Chem Phys 98(12):10089\u201310092. https:\/\/doi.org\/10.1063\/1.464397","journal-title":"J Chem Phys"},{"key":"11731_CR36","first-page":"8","volume":"11","author":"MP Widhiastuty","year":"2011","unstructured":"Widhiastuty MP, Febriani F, Moeis M, Akhmaloka A, Warganegara F (2011) Cloning, homological analysis and expression of Lipase gene from hot spring isolate. Int J Integr Biology 11:8\u201313","journal-title":"Int J Integr Biology"},{"issue":"2","key":"11731_CR37","doi-asserted-by":"publisher","first-page":"393","DOI":"10.1111\/j.1574-6968.1999.tb08754.x","volume":"179","author":"D Lee","year":"1999","unstructured":"Lee D, Koh Y, Kim K, Kim B, Choi H, Kim D et al (1999) Isolation and characterization of a thermophilic lipase from bacillus thermoleovorans ID-1. FEMS Microbiol Lett 179(2):393\u2013400. https:\/\/doi.org\/10.1111\/j.1574-6968.1999.tb08754.x","journal-title":"FEMS Microbiol Lett"},{"key":"11731_CR38","doi-asserted-by":"publisher","first-page":"135","DOI":"10.22207\/JPAM.11.1.18","volume":"11","author":"N Husin","year":"2017","unstructured":"Husin N, Nurbaiti S, Warganegara F, Akhmaloka A (2017) Heterologous expression of gene encoded thermostable lipase and lipolytic activity. J Pure Appl Microbiol 11:135\u2013139. https:\/\/doi.org\/10.22207\/JPAM.11.1.18","journal-title":"J Pure Appl Microbiol"},{"issue":"5","key":"11731_CR39","doi-asserted-by":"publisher","first-page":"1762","DOI":"10.1021\/acs.jchemed.0c01184","volume":"98","author":"MF Candela","year":"2021","unstructured":"Candela MF, Arenas NE, Caicedo O, Malag\u00f3n A (2021) Inhibition of lipase by orlistat: kinetics combined with in silico approaches to visualize interactions. J Chem Educ 98(5):1762\u20131767. https:\/\/doi.org\/10.1021\/acs.jchemed.0c01184","journal-title":"J Chem Educ"},{"key":"11731_CR40","doi-asserted-by":"publisher","DOI":"10.1007\/s00284-024-03904-5","author":"H Shah","year":"2024","unstructured":"Shah H, Chengnan Z, Khan S, Patil P, Li W, Xu Y et al (2024) Comprehensive insights into microbial lipases: unveiling structural dynamics, catalytic mechanism, and versatile applications. Curr Microbiol. https:\/\/doi.org\/10.1007\/s00284-024-03904-5","journal-title":"Curr Microbiol"},{"issue":"1","key":"11731_CR41","doi-asserted-by":"publisher","first-page":"5469","DOI":"10.1038\/s41598-020-62427-8","volume":"10","author":"K Kitadokoro","year":"2020","unstructured":"Kitadokoro K, Tanaka M, Hikima T, Okuno Y, Yamamoto M, Kamitani S (2020) Crystal structure of pathogenic Staphylococcus aureus lipase complex with the anti-obesity drug orlistat. Sci Rep 10(1):5469. https:\/\/doi.org\/10.1038\/s41598-020-62427-8","journal-title":"Sci Rep"},{"issue":"11","key":"11731_CR42","doi-asserted-by":"publisher","first-page":"394","DOI":"10.1007\/s00284-024-03904-5","volume":"81","author":"H Shah","year":"2024","unstructured":"Shah H, Zhang C, Khan S, Patil PJ, Li W, Xu Y et al (2024) Comprehensive insights into microbial lipases: unveiling structural dynamics, catalytic mechanism, and versatile applications. Curr Microbiol 81(11):394. https:\/\/doi.org\/10.1007\/s00284-024-03904-5","journal-title":"Curr Microbiol"},{"issue":"Pt 1","key":"11731_CR43","doi-asserted-by":"publisher","first-page":"177","DOI":"10.1042\/bj3430177","volume":"343","author":"JL Arpigny","year":"1999","unstructured":"Arpigny JL, Jaeger KE (1999) Bacterial lipolytic enzymes: classification and properties. Biochem J 343(Pt 1):177\u2013183","journal-title":"Biochem J"},{"issue":"1","key":"11731_CR44","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1111\/j.1574-6976.2002.tb00599.x","volume":"26","author":"UT Bornscheuer","year":"2002","unstructured":"Bornscheuer UT (2002) Microbial carboxyl esterases: classification, properties and application in biocatalysis. FEMS Microbiol Rev 26(1):73\u201381. https:\/\/doi.org\/10.1111\/j.1574-6976.2002.tb00599.x","journal-title":"FEMS Microbiol Rev"},{"key":"11731_CR45","doi-asserted-by":"publisher","first-page":"627","DOI":"10.1016\/S0734-9750(01)00086-6","volume":"19","author":"R Sharma","year":"2002","unstructured":"Sharma R, Chisti Y, Banerjee U (2002) Production, purification, characterization, and applications of lipases. Biotechnol Adv 19:627\u2013662. https:\/\/doi.org\/10.1016\/S0734-9750(01)00086-6","journal-title":"Biotechnol Adv"},{"key":"11731_CR46","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1016\/j.plipres.2014.12.001","volume":"57","author":"R Gupta","year":"2015","unstructured":"Gupta R, Kumari A, Syal P, Singh Y (2015) Molecular and functional diversity of yeast and fungal lipases: their role in biotechnology and cellular physiology. Prog Lipid Res 57:40\u201354. https:\/\/doi.org\/10.1016\/j.plipres.2014.12.001","journal-title":"Prog Lipid Res"},{"key":"11731_CR47","doi-asserted-by":"publisher","first-page":"1142536","DOI":"10.3389\/fmicb.2023.1142536","volume":"14","author":"A Kumar","year":"2023","unstructured":"Kumar A, Verma V, Dubey VK, Srivastava A, Garg SK, Singh VP et al (2023) Industrial applications of fungal lipases: a review. Front Microbiol 14:1142536. https:\/\/doi.org\/10.3389\/fmicb.2023.1142536","journal-title":"Front Microbiol"},{"issue":"6","key":"11731_CR48","doi-asserted-by":"publisher","first-page":"632","DOI":"10.1016\/j.biotechadv.2011.04.005","volume":"29","author":"P Fickers","year":"2011","unstructured":"Fickers P, Marty A, Nicaud JM (2011) The lipases from Yarrowia lipolytica: genetics, production, regulation, biochemical characterization and biotechnological applications. Biotechnol Adv 29(6):632\u2013644. https:\/\/doi.org\/10.1016\/j.biotechadv.2011.04.005","journal-title":"Biotechnol Adv"},{"issue":"20","key":"11731_CR49","doi-asserted-by":"publisher","first-page":"3506","DOI":"10.1111\/febs.14211","volume":"284","author":"Z Zhao","year":"2017","unstructured":"Zhao Z, Hou S, Lan D, Wang X, Liu J, Khan FI et al (2017) Crystal structure of a lipase from Streptomyces sp. strain W007\u2014implications for thermostability and regiospecificity. Febs j 284(20):3506\u20133519. https:\/\/doi.org\/10.1111\/febs.14211","journal-title":"Febs j"},{"issue":"2","key":"11731_CR50","doi-asserted-by":"publisher","first-page":"259","DOI":"10.1016\/j.bbrc.2017.04.103","volume":"488","author":"D Lan","year":"2017","unstructured":"Lan D, Xu H, Xu J, Dubin G, Liu J, Iqbal Khan F et al (2017) Malassezia globosa MgMDL2 lipase: crystal structure and rational modification of substrate specificity. Biochem Biophys Res Commun 488(2):259\u2013265. https:\/\/doi.org\/10.1016\/j.bbrc.2017.04.103","journal-title":"Biochem Biophys Res Commun"},{"key":"11731_CR51","doi-asserted-by":"publisher","DOI":"10.3389\/fbioe.2017.00016","author":"FI Khan","year":"2017","unstructured":"Khan FI, Lan D, Durrani R, Huan W, Zhao Z, Wang Y (2017) The lid domain in lipases: structural and functional determinant of enzymatic properties. Front Bioeng Biotechnol. https:\/\/doi.org\/10.3389\/fbioe.2017.00016","journal-title":"Front Bioeng Biotechnol"},{"key":"11731_CR52","doi-asserted-by":"publisher","first-page":"166","DOI":"10.1016\/j.molcatb.2006.01.018","volume":"39","author":"F Secundo","year":"2006","unstructured":"Secundo F, Carrea G, Tarabiono C, Gatti-Lafranconi P, Brocca S, Lotti M et al (2006) The lid is a structural and functional determinant of lipase activity and selectivity. J Mol Catal B-enzymatic 39:166\u2013170. https:\/\/doi.org\/10.1016\/j.molcatb.2006.01.018","journal-title":"J Mol Catal B-enzymatic"},{"issue":"6557","key":"11731_CR53","doi-asserted-by":"publisher","first-page":"871","DOI":"10.1126\/science.abj8754","volume":"373","author":"M Baek","year":"2021","unstructured":"Baek M, DiMaio F, Anishchenko I, Dauparas J, Ovchinnikov S, Lee GR et al (2021) Accurate prediction of protein structures and interactions using a three-track neural network. Science 373(6557):871\u2013876. https:\/\/doi.org\/10.1126\/science.abj8754","journal-title":"Science"},{"key":"11731_CR54","doi-asserted-by":"publisher","first-page":"116505","DOI":"10.1016\/j.molliq.2021.116505","volume":"335","author":"S Li","year":"2021","unstructured":"Li S, Hu X, Pan J, Gong D, Zhang G (2021) Mechanistic insights into the inhibition of pancreatic lipase by apigenin: inhibitory interaction, conformational change and moleculhfcaar docking studies. J Mol Liq 335:116505. https:\/\/doi.org\/10.1016\/j.molliq.2021.116505","journal-title":"J Mol Liq"},{"key":"11731_CR55","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1016\/j.jcis.2016.10.058","volume":"488","author":"R Xin","year":"2017","unstructured":"Xin R, Khan FI, Zhao Z, Zhang Z, Yang B, Wang Y (2017) A comparative study on kinetics and substrate specificities of Phospholipase A(1) with Thermomyces lanuginosus lipase. J Colloid Interface Sci 488:149\u2013154. https:\/\/doi.org\/10.1016\/j.jcis.2016.10.058","journal-title":"J Colloid Interface Sci"},{"issue":"4","key":"11731_CR56","doi-asserted-by":"publisher","first-page":"855","DOI":"10.1002\/prot.26776","volume":"93","author":"F Ozhelvaci","year":"2025","unstructured":"Ozhelvaci F, Steczkiewicz K (2025) \u03b1\/\u03b2 hydrolases: toward unraveling entangled classification. Proteins 93(4):855\u2013870. https:\/\/doi.org\/10.1002\/prot.26776","journal-title":"Proteins"},{"issue":"3","key":"11731_CR57","doi-asserted-by":"publisher","first-page":"197","DOI":"10.1093\/protein\/5.3.197","volume":"5","author":"DL Ollis","year":"1992","unstructured":"Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J, Sussman JL (1992) The \u03b1\/\u03b2 hydrolase fold. Protein Eng Des Sel 5(3):197\u2013211","journal-title":"Protein Eng Des Sel"},{"issue":"26","key":"11731_CR58","doi-asserted-by":"publisher","first-page":"8708","DOI":"10.1074\/jbc.RA119.011809","volume":"295","author":"VD Pham","year":"2020","unstructured":"Pham VD, To TA, Gagn\u00e9-Thivierge C, Couture M, Lag\u00fce P, Yao D et al (2020) Structural insights into the putative bacterial acetylcholinesterase ChoE and its substrate inhibition mechanism. J Biol Chem 295(26):8708\u20138724. https:\/\/doi.org\/10.1074\/jbc.RA119.011809","journal-title":"J Biol Chem"},{"issue":"1","key":"11731_CR59","doi-asserted-by":"publisher","first-page":"111","DOI":"10.1186\/s43094-025-00862-y","volume":"11","author":"HK Nivatya","year":"2025","unstructured":"Nivatya HK, Singh A, Kumar N, Sonam, Sharma L, Singh V et al (2025) Assessing molecular docking tools: understanding drug discovery and design. Future J Pharm Sci 11(1):111. https:\/\/doi.org\/10.1186\/s43094-025-00862-y","journal-title":"Future J Pharm Sci"},{"key":"11731_CR60","unstructured":"NCBI (2026) PubChem Compound Summary for CID 3034010, Orlistat. https:\/\/pubchem.ncbi.nlm.nih.gov\/compound\/Orlistat"},{"issue":"11","key":"11731_CR61","doi-asserted-by":"publisher","first-page":"2122","DOI":"10.1002\/pro.493","volume":"19","author":"S Rehm","year":"2010","unstructured":"Rehm S, Trodler P, Pleiss J (2010) Solvent-induced lid opening in lipases: a molecular dynamics study. Protein Sci 19(11):2122\u20132130. https:\/\/doi.org\/10.1002\/pro.493","journal-title":"Protein Sci"},{"key":"11731_CR62","doi-asserted-by":"publisher","first-page":"295","DOI":"10.13005\/bbra\/2632","volume":"15","author":"D Herasari","year":"2018","unstructured":"Herasari D, Hertadi R, Warganegara F, Akhmaloka A (2018) Stability and mobility of lid lipmnk in acetonitrile by molecular dynamics simulations approach. Biosci Biotechnol Res Asia 15:295\u2013299. https:\/\/doi.org\/10.13005\/bbra\/2632","journal-title":"Biosci Biotechnol Res Asia"},{"key":"11731_CR63","volume-title":"Hydrogen bonds in proteins: role and strength","author":"RE Hubbard","year":"2010","unstructured":"Hubbard RE, Kamran Haider M (2010) Hydrogen bonds in proteins: role and strength. Wiley"},{"key":"11731_CR64","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1016\/j.jtbi.2015.03.035","volume":"374","author":"K Faez Iqbal","year":"2015","unstructured":"Faez Iqbal K, Algasan G, Kugen P, Suren S, Krishna B (2015) Thermostable chitinase II from Thermomyces lanuginosus SSBP: cloning, structure prediction and molecular dynamics simulations. J Theor Biol 374:107\u2013114. https:\/\/doi.org\/10.1016\/j.jtbi.2015.03.035","journal-title":"J Theor Biol"},{"key":"11731_CR65","doi-asserted-by":"crossref","unstructured":"Grewal S, Deswal G, Grewal AS, Guarve K (2025) Chapter Eight - Molecular dynamics simulations: Insights into protein and protein ligand interactions. In: Narayan CV, Verma S, Grewal AS, Singh N, Nimesh H (eds) Advances in Pharmacology. Academic, pp 139\u2013162","DOI":"10.1016\/bs.apha.2025.01.007"},{"issue":"10","key":"11731_CR66","doi-asserted-by":"publisher","first-page":"2123","DOI":"10.1080\/07391102.2016.1206837","volume":"35","author":"FI Khan","year":"2017","unstructured":"Khan FI, Nizami B, Anwer R, Gu K-R, Bisetty K, Hassan MI et al (2017) Structure prediction and functional analyses of a thermostable lipase obtained from Shewanella putrefaciens. J Biomol Struct Dynamics 35(10):2123\u20132135. https:\/\/doi.org\/10.1080\/07391102.2016.1206837","journal-title":"J Biomol Struct Dynamics"},{"key":"11731_CR67","doi-asserted-by":"publisher","first-page":"139","DOI":"10.1016\/j.jbiotec.2014.07.446","volume":"187","author":"DE Stephens","year":"2014","unstructured":"Stephens DE, Khan FI, Singh P, Bisetty K, Singh S, Permaul K (2014) Creation of thermostable and alkaline stable xylanase variants by DNA shuffling. J Biotechnol 187:139\u2013146. https:\/\/doi.org\/10.1016\/j.jbiotec.2014.07.446","journal-title":"J Biotechnol"},{"issue":"31","key":"11731_CR68","doi-asserted-by":"publisher","first-page":"2839","DOI":"10.2174\/1568026621666211105095731","volume":"21","author":"FI Khan","year":"2021","unstructured":"Khan FI, Ali S, Chen W, Anjum F, Shafie A, Hassan MI et al (2021) High-resolution MD simulation studies to get mechanistic insights into the urea-induced denaturation of human sphingosine kinase 1. Curr Top Med Chem 21(31):2839\u20132850. https:\/\/doi.org\/10.2174\/1568026621666211105095731","journal-title":"Curr Top Med Chem"},{"key":"11731_CR69","doi-asserted-by":"publisher","first-page":"1171","DOI":"10.1016\/j.ijbiomac.2020.05.168","volume":"161","author":"S Qausain","year":"2020","unstructured":"Qausain S, Khan FI, Lai D, Hassan MI, Basheeruddin M, Ahmed N et al (2020) Mechanistic insights into the urea-induced denaturation of a non-seleno thiol specific antioxidant human peroxiredoxin 6. Int J Biol Macromol 161:1171\u20131180. https:\/\/doi.org\/10.1016\/j.ijbiomac.2020.05.168","journal-title":"Int J Biol Macromol"},{"key":"11731_CR70","doi-asserted-by":"publisher","first-page":"1496","DOI":"10.1016\/j.ijbiomac.2020.07.280","volume":"161","author":"FI Khan","year":"2020","unstructured":"Khan FI, Gupta P, Roy S, Azum N, Alamry KA, Asiri AM et al (2020) Mechanistic insights into the urea-induced denaturation of human sphingosine kinase 1. Int J Biol Macromol 161:1496\u20131505. https:\/\/doi.org\/10.1016\/j.ijbiomac.2020.07.280","journal-title":"Int J Biol Macromol"},{"key":"11731_CR71","doi-asserted-by":"publisher","DOI":"10.3390\/ijms241310684","author":"S Wang","year":"2023","unstructured":"Wang S, Khan FI (2023) Investigation of molecular interactions mechanism of pembrolizumab and PD-1. Int J Mol Sci. https:\/\/doi.org\/10.3390\/ijms241310684","journal-title":"Int J Mol Sci"},{"key":"11731_CR72","doi-asserted-by":"publisher","first-page":"e0119264","DOI":"10.1371\/journal.pone.0119264","volume":"10","author":"L Mart\u00ednez","year":"2015","unstructured":"Mart\u00ednez L (2015) Automatic identification of mobile and rigid substructures in molecular dynamics simulations and fractional structural fluctuation analysis. PLoS ONE 10:e0119264. https:\/\/doi.org\/10.1371\/journal.pone.0119264","journal-title":"PLoS ONE"}],"container-title":["Molecular Diversity"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11030-026-11731-y.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s11030-026-11731-y","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11030-026-11731-y.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,11,5]],"date-time":"2026-11-05T06:02:26Z","timestamp":1793858546000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s11030-026-11731-y"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,12]]},"references-count":72,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2026,12]]}},"alternative-id":["11731"],"URL":"https:\/\/doi.org\/10.1007\/s11030-026-11731-y","relation":{},"ISSN":["1573-501X"],"issn-type":[{"value":"1573-501X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,12]]},"assertion":[{"value":"23 March 2026","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"31 August 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"12 September 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","label":"Competing interests","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"Declaration of generatif AI and AI-assisted technologies in the writing process.","order":2,"name":"Ethics","label":"Declaration of generative AI and AI-assisted technologies in the writing process","group":{"name":"EthicsHeading","label":"Declarations"}}]}}