{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,10]],"date-time":"2026-03-10T14:58:49Z","timestamp":1773154729391,"version":"3.50.1"},"reference-count":23,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2020,8,18]],"date-time":"2020-08-18T00:00:00Z","timestamp":1597708800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["ZE 542\/12\u20102"],"award-info":[{"award-number":["ZE 542\/12\u20102"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["analyticalsciencejournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Biotech &amp; Bioengineering"],"published-print":{"date-parts":[[2020,12]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Protein lipoylation is essential for the function of many key enzymes but barely studied kinetically. Here, the two\u2010step reaction cascade of H protein lipoylation catalyzed by the multifunctional enzyme lipoate\u2013protein ligase A (LplA) was quantitatively and differentially studied. We discovered new phenomena and unusual kinetics of the cascade: (a) the speed of the first reaction is faster than the second one by two orders of magnitude, leading to high accumulation of the intermediate lipoyl\u2010AMP (Lip\u2010AMP); (b) Lip\u2010AMP is hydrolyzed, but only significantly at the presence of H protein and in competition with the lipoylation; (c) both the lipoylation of H protein and its hydrolysis is enhanced by the apo and lipoylated forms of H protein and a mutant without the lipoylation site. A conceptual mechanistic model is proposed to explain these experimental observations in which conformational change of LplA upon interaction with H protein and competitive nucleophilic attacks play key roles.<\/jats:p>","DOI":"10.1002\/bit.27526","type":"journal-article","created":{"date-parts":[[2020,8,4]],"date-time":"2020-08-04T11:00:47Z","timestamp":1596538847000},"page":"3677-3687","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":14,"title":["Activation and competition of lipoylation of H protein and its hydrolysis in a reaction cascade catalyzed by the multifunctional enzyme lipoate\u2013protein ligase A"],"prefix":"10.1002","volume":"117","author":[{"given":"Xinyi","family":"Zhang","sequence":"first","affiliation":[{"name":"Beijing Advanced Innovation Center for Soft Matter Science and Engineering Beijing University of Chemical Technology Beijing 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Institute of Plant Protection Chinese Academy of Agricultural Sciences Beijing China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9768-7096","authenticated-orcid":false,"given":"An\u2010Ping","family":"Zeng","sequence":"additional","affiliation":[{"name":"Beijing Advanced Innovation Center for Soft Matter Science and Engineering Beijing University of Chemical Technology Beijing China"},{"name":"Institute of Bioprocess and Biosystems Engineering Hamburg University of Technology Hamburg 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