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Here, we investigated the wild\u2010type pLG72, the R30K variant associated with schizophrenia susceptibility, and the K62E variant. The protein conformation, oligomeric state, ligand\u2010, and hDAAO\u2010binding properties are only slightly modified by the substitutions. All pLG72 variants inhibit hDAAO and lead to an increase in cellular (<jats:sc>d\/d<\/jats:sc>+<jats:sc>l<\/jats:sc>)\u2010serine. However, the R30K pLG72 is significantly more prone to degradation than the R30 and the K62E variants in a cell system, thus possessing a lower ability to interact\/inhibit hDAAO. This links R30K pLG72 with the hyperactivity of hDAAO, the decreased <jats:sc>d<\/jats:sc>\u2010serine level, and NMDAR hypofunction observed in schizophrenia\u2010affected patients.<\/jats:p>","DOI":"10.1002\/1873-3468.12585","type":"journal-article","created":{"date-parts":[[2017,2,6]],"date-time":"2017-02-06T19:03:01Z","timestamp":1486407781000},"page":"646-655","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["Elucidating the role of the pLG72 R30K substitution in schizophrenia susceptibility"],"prefix":"10.1002","volume":"591","author":[{"given":"Silvia","family":"Sacchi","sequence":"first","affiliation":[{"name":"Department of Biotechnology and Life Sciences Universit\u00e0 degli Studi dell'Insubria Varese Italy"},{"name":"The Protein Factory Politecnico di Milano and Universit\u00e0 degli Studi dell'Insubria 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