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One of the most widely applied lipases in the manufacturing industry is <jats:italic>Candida antarctica<\/jats:italic> lipase B (<jats:styled-content style=\"fixed-case\">CALB<\/jats:styled-content>). Here, we report the biochemical and structural characterization of a novel <jats:styled-content style=\"fixed-case\">CALB<\/jats:styled-content>\u2010like lipase from an important human pathogen\u2014<jats:italic>Aspergillus fumigatus<\/jats:italic> (<jats:styled-content style=\"fixed-case\">AFLB<\/jats:styled-content>), which has high sn\u20101,3\u2010specificity toward triolein. <jats:styled-content style=\"fixed-case\">AFLB<\/jats:styled-content> crystal structure displays a <jats:styled-content style=\"fixed-case\">CALB<\/jats:styled-content>\u2010like catalytic domain and hosts a unique tightly closed \u2018lid\u2019 domain that contains a disulfide bridge, as well as an extra N\u2010terminal subdomain composed of residues 1\u2013128 (including the helix \u03b11\u2013\u03b15 located above the active site). To gain insight into the function of this novel lid and N\u2010terminal subdomain, we constructed and characterized a series of mutants in these two domains. Deleting the protruding bulk lid's residues, replacing the bulk and tight lid with a small and loose lid from <jats:styled-content style=\"fixed-case\">CALB<\/jats:styled-content>, or breaking the disulfide bridge increased the affinity of <jats:styled-content style=\"fixed-case\">CALB<\/jats:styled-content> for glyceride substrates and improved its catalytic activity, along with the loss of enzyme fold stability and thermostability. N\u2010terminal truncation mutants revealed that the N\u2010terminal peptide (residues 1\u201359) is a strong inhibitor of <jats:styled-content style=\"fixed-case\">AFLB<\/jats:styled-content> binding to lipid films. This peptide thus limits <jats:styled-content style=\"fixed-case\">AFLB<\/jats:styled-content>'s penetration power and specific activity, revealing a unique enzyme activity regulatory mechanism. Our findings on the functional and structural properties of <jats:styled-content style=\"fixed-case\">AFLB<\/jats:styled-content> provide a better understanding of the functions of the <jats:styled-content style=\"fixed-case\">CALB<\/jats:styled-content>\u2010like lipases and pave the way for its future protein engineering.<\/jats:p><\/jats:sec><jats:sec><jats:title>Database<\/jats:title><jats:p>Structural data are available in the Protein Data Bank under the accession numbers <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.rcsb.org\/pdb\/search\/structidSearch.do?structureId=6IDY\">6IDY<\/jats:ext-link>.<\/jats:p><\/jats:sec>","DOI":"10.1111\/febs.14814","type":"journal-article","created":{"date-parts":[[2019,3,25]],"date-time":"2019-03-25T17:51:47Z","timestamp":1553536307000},"page":"2366-2380","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["Structure and characterization of <i>Aspergillus fumigatus<\/i> lipase B with a unique, oversized regulatory subdomain"],"prefix":"10.1111","volume":"286","author":[{"given":"Weiqian","family":"Huang","sequence":"first","affiliation":[{"name":"School of Bioscience and Bioengineering South China University of Technology Guangzhou China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dongming","family":"Lan","sequence":"additional","affiliation":[{"name":"School of Food Science and Engineering South China University of Technology Guangzhou China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Grzegorz M.","family":"Popowicz","sequence":"additional","affiliation":[{"name":"Institute of Structural Biology Helmholtz Zentrum M\u00fcnchen Neuherberg Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Krzysztof M.","family":"Zak","sequence":"additional","affiliation":[{"name":"Institute of Structural Biology Helmholtz Zentrum M\u00fcnchen Neuherberg 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