{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,26]],"date-time":"2025-09-26T13:16:33Z","timestamp":1758892593544,"version":"3.44.0"},"reference-count":37,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2020,8,1]],"date-time":"2020-08-01T00:00:00Z","timestamp":1596240000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,8,1]],"date-time":"2020-08-01T00:00:00Z","timestamp":1596240000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"name":"Key Laboratory of Fermentation Engineering (Ministry of Education) of China"},{"DOI":"10.13039\/501100012590","name":"Opening Project of Shanghai Key Laboratory of New Drug Design","doi-asserted-by":"publisher","award":["17DZ2271000"],"award-info":[{"award-number":["17DZ2271000"]}],"id":[{"id":"10.13039\/501100012590","id-type":"DOI","asserted-by":"publisher"}]},{"name":"China and the National Natural Science Foundation of China","award":["31801489"],"award-info":[{"award-number":["31801489"]}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Enzyme and Microbial Technology"],"published-print":{"date-parts":[[2020,8]]},"DOI":"10.1016\/j.enzmictec.2020.109548","type":"journal-article","created":{"date-parts":[[2020,4,7]],"date-time":"2020-04-07T17:14:19Z","timestamp":1586279659000},"page":"109548","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":8,"special_numbering":"C","title":["Characterization and rational design for substrate specificity of a prolyl endopeptidase from Stenotrophomonas maltophilia"],"prefix":"10.1016","volume":"138","author":[{"given":"Junjie","family":"Yu","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Junjie","family":"Wu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dewei","family":"Xie","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lei","family":"Du","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ya-Jie","family":"Tang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4666-4019","authenticated-orcid":false,"given":"Jingli","family":"Xie","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dongzhi","family":"Wei","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"10113","key":"10.1016\/j.enzmictec.2020.109548_bib0005","doi-asserted-by":"crossref","first-page":"2610","DOI":"10.1016\/S0140-6736(17)32298-5","article-title":"Stretching the carotid sinus to treat resistant hypertension","volume":"390","author":"Courand","year":"2017","journal-title":"Lancet"},{"issue":"3","key":"10.1016\/j.enzmictec.2020.109548_bib0010","doi-asserted-by":"crossref","first-page":"1842","DOI":"10.1006\/bbrc.1994.2402","article-title":"Human type 2 angiotensin II receptor gene: Cloned, mapped to the X chromosome, and its mRNA is expressed in the human lung","volume":"203","author":"Koike","year":"1994","journal-title":"Biochem. Biophys. Res. Commun"},{"issue":"5","key":"10.1016\/j.enzmictec.2020.109548_bib0015","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1042\/cs1000481","article-title":"Angiotensin receptors: Distribution, signalling and function","volume":"100","author":"Dinh","year":"2001","journal-title":"Clin. Sci."},{"issue":"10","key":"10.1016\/j.enzmictec.2020.109548_bib0020","doi-asserted-by":"crossref","first-page":"5230","DOI":"10.1039\/C8FO01146J","article-title":"Isolation, purification and the anti-hypertensive effect of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from Ruditapes philippinarum fermented with Bacillus natto","volume":"9","author":"Chen","year":"2018","journal-title":"Food Funct"},{"issue":"9","key":"10.1016\/j.enzmictec.2020.109548_bib0025","doi-asserted-by":"crossref","first-page":"5230","DOI":"10.1039\/C9FO01531K","article-title":"Effect of a multi-frequency counter-current S-type ultrasound pretreatment on the defatted corn germ protein: enzymatic hydrolysis, ACE inhibitory activity and structural characterization","volume":"10","author":"Musa","year":"2019","journal-title":"Food Funct"},{"issue":"2","key":"10.1016\/j.enzmictec.2020.109548_bib0030","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1038\/ki.1989.190","article-title":"Efficacy and variability of the antiproteinuric effect of ACE inhibition by lisinopril","volume":"36","author":"Heeg","year":"1989","journal-title":"Kidney Int."},{"issue":"5","key":"10.1016\/j.enzmictec.2020.109548_bib0035","doi-asserted-by":"crossref","first-page":"303","DOI":"10.2165\/00129784-200707050-00001","article-title":"ACE inhibition in hypertension: Focus on perindopril","volume":"7","author":"Cockcroft","year":"2007","journal-title":"Am. J. Cardiovasc. Drugs"},{"issue":"4","key":"10.1016\/j.enzmictec.2020.109548_bib0040","doi-asserted-by":"crossref","first-page":"777","DOI":"10.3168\/jds.S0022-0302(95)76689-9","article-title":"Purification and characterization of angiotensin I-converting enzyme inhibitors from sour milk","volume":"78","author":"Nakamura","year":"1989","journal-title":"J. Dairy Sci."},{"issue":"4","key":"10.1016\/j.enzmictec.2020.109548_bib0045","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1111\/j.1365-2621.2000.tb16049.x","article-title":"Classification and antihypertensive activity of angiotensin I-converting enzyme inhibitory peptides derived from food proteins","volume":"65","author":"Fujita","year":"2000","journal-title":"J. Food Sci"},{"issue":"5","key":"10.1016\/j.enzmictec.2020.109548_bib0050","doi-asserted-by":"crossref","first-page":"898","DOI":"10.1016\/j.procbio.2014.02.007","article-title":"In vitro, and in vivo, ACE inhibitory of pistachio hydrolysates and in silico, mechanism of identified peptide binding with ACE","volume":"49","author":"Li","year":"2014","journal-title":"Process Biochem"},{"issue":"4","key":"10.1016\/j.enzmictec.2020.109548_bib0055","doi-asserted-by":"crossref","first-page":"1056","DOI":"10.1110\/ps.03498604","article-title":"Trypsin specificity as elucidated by LIE calculations, X-ray structures, and association constant measurements","volume":"13","author":"Leiros","year":"2004","journal-title":"Protein Sci."},{"year":"1992","series-title":"Specificity of proteolysis","author":"Keil","key":"10.1016\/j.enzmictec.2020.109548_bib0060"},{"issue":"2","key":"10.1016\/j.enzmictec.2020.109548_bib0065","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/S0092-8674(00)81416-6","article-title":"Prolyl oligopeptidase: An unusual beta-propeller domain regulates proteolysis","volume":"94","author":"F\u00fcl\u00f6p","year":"1998","journal-title":"Cell"},{"issue":"4","key":"10.1016\/j.enzmictec.2020.109548_bib0070","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1152\/ajpgi.00034.2006","article-title":"Highly efficient gluten degradation with a newly identified prolyl endoprotease: Implications for celiac disease","volume":"291","author":"Stepniak","year":"2006","journal-title":"Am. J. Physiol.-Gastroint. Liver Physiol."},{"issue":"1","key":"10.1016\/j.enzmictec.2020.109548_bib0075","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1136\/gut.2006.111609","article-title":"Efficient degradation of gluten by a prolyl endoprotease in a gastrointestinal model: Implications for coeliac disease","volume":"57","author":"Mitea","year":"2008","journal-title":"Gut"},{"issue":"10","key":"10.1016\/j.enzmictec.2020.109548_bib0080","doi-asserted-by":"crossref","first-page":"4786","DOI":"10.1016\/S0021-9258(19)85566-7","article-title":"Proline-specific endopeptidase from Flavobacterium, purification and properties","volume":"255","author":"Yoshimoto","year":"1980","journal-title":"J. Biol. Chem."},{"issue":"8","key":"10.1016\/j.enzmictec.2020.109548_bib0085","doi-asserted-by":"crossref","first-page":"2454","DOI":"10.1128\/jb.174.8.2454-2459.1992","article-title":"Proline-specific endopeptidases from microbial sources: Isolation of an enzyme from a Xanthomonas sp","volume":"174","author":"Szwajcer-Dey","year":"1992","journal-title":"J. Bacteriol"},{"issue":"60","key":"10.1016\/j.enzmictec.2020.109548_bib0090","doi-asserted-by":"crossref","first-page":"790","DOI":"10.1093\/oxfordjournals.jbchem.a124120","article-title":"Prolyl endopeptidase from Aeromonas hydrophila: Cloning, sequencing, and expression of the enzyme gene and characterization of the expressed enzyme","volume":"113","author":"Kanatani","year":"1993","journal-title":"J. Biochem."},{"issue":"1","key":"10.1016\/j.enzmictec.2020.109548_bib0095","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1006\/abbi.1998.0836","article-title":"Prolyl endopeptidase from Sphingomonas capsulata: Isolation and characterization of the enzyme and nucleotide sequence of the gene","volume":"358","author":"Kabashima","year":"1998","journal-title":"Arch. Biochem. Biophys"},{"issue":"4","key":"10.1016\/j.enzmictec.2020.109548_bib0100","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1016\/S0032-9592(02)00180-2","article-title":"Purification and characterization of a hydrophobic amino acid specific endopeptidase from Halobacterium halobium S9 with potential","volume":"38","author":"Capiralla","year":"2002","journal-title":"Process Biochem"},{"issue":"6","key":"10.1016\/j.enzmictec.2020.109548_bib0105","doi-asserted-by":"crossref","first-page":"3025","DOI":"10.1128\/AEM.71.6.3025-3032.2005","article-title":"Identification of endopeptidase genes from the genomic sequence of Lactobacillus helveticus CNRZ32 and the role of these genes in hydrolysis of model bitter peptides","volume":"71","author":"Sridhar","year":"2005","journal-title":"Appl. Environ. Microbiol"},{"issue":"6","key":"10.1016\/j.enzmictec.2020.109548_bib0110","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1002\/bit.20643","article-title":"Fermentation, purification, formulation, and pharmacological evaluation of a prolyl endopeptidase from Myxococcus xanthus: Implications for celiac sprue therapy","volume":"92","author":"Gass","year":"2005","journal-title":"Biotechnol. Bioeng"},{"issue":"20","key":"10.1016\/j.enzmictec.2020.109548_bib0115","doi-asserted-by":"crossref","first-page":"7944","DOI":"10.1021\/jf0506535","article-title":"Effective prevention of chill-haze in beer using an acid proline-specific endoprotease from Aspergillus niger","volume":"53","author":"Lopez","year":"2005","journal-title":"J. Agric. Food Chem"},{"key":"10.1016\/j.enzmictec.2020.109548_bib0120","article-title":"Purification of a prolyl endopeptidase from Aspergillus oryzae and evaluation of its ability to digest gluten","volume":"237","author":"Riggle","year":"2009","journal-title":"Abstracts of Papers of the American Chemical Society"},{"issue":"10","key":"10.1016\/j.enzmictec.2020.109548_bib0125","doi-asserted-by":"crossref","first-page":"3599","DOI":"10.1073\/pnas.0408286102","article-title":"Structural and mechanistic analysis of two prolyl endopeptidases: Role of interdomain dynamics in catalysis and specificity","volume":"102","author":"Shan","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"1","key":"10.1016\/j.enzmictec.2020.109548_bib0130","doi-asserted-by":"crossref","first-page":"2456","DOI":"10.1038\/s41598-017-02550-1","article-title":"Dynamics and ligand-induced conformational changes in human prolyl oligopeptidase analyzed by hydrogen\/deuterium exchange mass spectrometry","volume":"7","author":"Tsirigotaki","year":"2017","journal-title":"Sci. Rep."},{"issue":"12","key":"10.1016\/j.enzmictec.2020.109548_bib0135","doi-asserted-by":"crossref","first-page":"1616","DOI":"10.1021\/acs.biochem.9b00031","article-title":"Crystal structure and conformational dynamics of Pyrococcus furiosus prolyl oligopeptidase","volume":"58","author":"Ellis-Guardiola","year":"2019","journal-title":"Biochem."},{"issue":"3","key":"10.1016\/j.enzmictec.2020.109548_bib0140","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1093\/embo-reports\/kvd048","article-title":"Catalysis of serine oligopeptidases is controlled by a gating filter mechanism","volume":"1","author":"F\u00fcl\u00f6p","year":"2000","journal-title":"EMBO Rep"},{"issue":"7","key":"10.1016\/j.enzmictec.2020.109548_bib0145","doi-asserted-by":"crossref","first-page":"1428","DOI":"10.1002\/prot.24511","article-title":"Decoding the structural events in substrate-gating mechanism of eukaryotic prolyl oligopeptidase using normal mode analysis and molecular dynamics simulations","volume":"82","author":"Kaushik","year":"2014","journal-title":"Proteins"},{"issue":"28","key":"10.1016\/j.enzmictec.2020.109548_bib0150","doi-asserted-by":"crossref","first-page":"21487","DOI":"10.1074\/jbc.M109.092692","article-title":"Induced-fit mechanism for prolyl endopeptidase","volume":"285","author":"Li","year":"2010","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.enzmictec.2020.109548_bib0155","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1007\/s10295-013-1378-z","article-title":"Purification and characterization of a prolyl endopeptidase isolated from Aspergillus oryzae","volume":"41","author":"Kang","year":"2013","journal-title":"J. Ind. Microbiol. Biotechnol."},{"issue":"40","key":"10.1016\/j.enzmictec.2020.109548_bib0160","doi-asserted-by":"crossref","first-page":"7546","DOI":"10.1021\/acs.jafc.6b02482","article-title":"Characterization of a novel \u03b1-L-arabinofuranosidase from Ruminococcus albus 7 and rational design for its thermostability","volume":"64","author":"Yang","year":"2016","journal-title":"J. Agric. Food Chem"},{"issue":"6","key":"10.1016\/j.enzmictec.2020.109548_bib0165","doi-asserted-by":"crossref","first-page":"1359","DOI":"10.1021\/acs.jafc.7b04294","article-title":"Antihypertensive effects, molecular docking study and isothermal titration calorimetry assay of the angiotensin I-converting enzyme inhibitory peptides from Chlorella vulgaris","volume":"66","author":"Xie","year":"2018","journal-title":"J. Agric. Food Chem."},{"key":"10.1016\/j.enzmictec.2020.109548_bib0170","first-page":"1","article-title":"Identification and characterization of a serious multidrug resistant Stenotrophomonas maltophilia strain in China","volume":"2015","author":"Zhao","year":"2015","journal-title":"J. Biomed. Biotechnol"},{"issue":"3","key":"10.1016\/j.enzmictec.2020.109548_bib0175","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1007\/s00018-006-6317-y","article-title":"Prolyl endopeptidases","volume":"64","author":"Gass","year":"2007","journal-title":"Cell. Mol. Life Sci."},{"issue":"20","key":"10.1016\/j.enzmictec.2020.109548_bib0180","doi-asserted-by":"crossref","first-page":"11234","DOI":"10.1021\/jf202902r","article-title":"Inhibition strength of short peptides derived from an ACE inhibitory peptide","volume":"59","author":"Terashima","year":"2011","journal-title":"J. Agric. Food Chem."},{"year":"2008","series-title":"Determining the specificity of pepsin for proteolytic digestion","author":"Palashoff","key":"10.1016\/j.enzmictec.2020.109548_bib0185"}],"container-title":["Enzyme and Microbial Technology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141022920300417?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141022920300417?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,26]],"date-time":"2025-09-26T01:40:17Z","timestamp":1758850817000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141022920300417"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,8]]},"references-count":37,"alternative-id":["S0141022920300417"],"URL":"https:\/\/doi.org\/10.1016\/j.enzmictec.2020.109548","relation":{},"ISSN":["0141-0229"],"issn-type":[{"type":"print","value":"0141-0229"}],"subject":[],"published":{"date-parts":[[2020,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Characterization and rational design for substrate specificity of a prolyl endopeptidase from Stenotrophomonas maltophilia","name":"articletitle","label":"Article Title"},{"value":"Enzyme and Microbial Technology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.enzmictec.2020.109548","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"109548"}}