{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T01:57:47Z","timestamp":1760061467701,"version":"build-2065373602"},"reference-count":31,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2004,2,18]],"date-time":"2004-02-18T00:00:00Z","timestamp":1077062400000},"content-version":"vor","delay-in-days":6928,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biotech &amp; Bioengineering"],"published-print":{"date-parts":[[1985,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Hydrolysis of <jats:sc>L<\/jats:sc>\u2010 and <jats:sc>D<\/jats:sc>\u2010<jats:italic>O<\/jats:italic>\u2010phosphothreonines catalyzed by four different phosphatases, alkaline phosphatases from calf intestine and <jats:italic>E. coli<\/jats:italic> and acid phosphatases from wheat germ and potato, has been kinetically studied. Alkaline phosphatases were found to have comparable reactivities towards the optical isomers. On the other hand, both acid phosphatases displayed a marked stereoselectivity, hydrolyzing the L\u2010ester much faster than its D counterpart. Wheat germ acid phosphatase was the most stereoselective enzyme: <jats:italic>V<\/jats:italic><jats:sub><jats:italic>L<\/jats:italic><\/jats:sub>\/<jats:italic>V<\/jats:italic><jats:sub><jats:italic>D<\/jats:italic><\/jats:sub> = 24 and <jats:italic>K<\/jats:italic><jats:sub><jats:italic>m<\/jats:italic>,<jats:italic>L<\/jats:italic><\/jats:sub>\/<jats:italic>K<\/jats:italic><jats:sub><jats:italic>m<\/jats:italic>,<jats:italic>D<\/jats:italic><\/jats:sub> = 0.17. This enzyme was immobilized (in <jats:italic>k<\/jats:italic>\u2010carrageenan gel, followed by crosslinking with glutaraldehyde) and used for the preparative resolution of <jats:sc>D<\/jats:sc>,<jats:sc>L<\/jats:sc>\u2010threonine: the latter was first chemically <jats:italic>O<\/jats:italic>\u2010phosphorylated and then asymmetrically hydrolyzed by the immobilized phosphatase. As a result, gram quantities of <jats:sc>L<\/jats:sc>\u2010threonine of high optical purity and <jats:italic>O<\/jats:italic>\u2010phospho\u2010<jats:sc>D<\/jats:sc>\u2010threonine were prepared. Immobilized wheat germ phosphatase has been tested for the resolution of other racemic alcohols: serine, 2\u2010amino\u20101\u2010butanol, 1\u2010amino\u20102\u2010propanol, 2\u2010octanol, and menthol. In all those cases, the enzyme was either not sufficiently stereoselective or too slow for preparative resolutions.<\/jats:p>","DOI":"10.1002\/bit.260270306","type":"journal-article","created":{"date-parts":[[2004,12,29]],"date-time":"2004-12-29T11:51:40Z","timestamp":1104321100000},"page":"247-252","source":"Crossref","is-referenced-by-count":21,"title":["Preparative resolution of <scp>D<\/scp>,<scp>L<\/scp>\u2010threonine catalyzed by immobilized phosphatase"],"prefix":"10.1002","volume":"27","author":[{"given":"Mark P.","family":"Scollar","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"George","family":"Sigal","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alexander M.","family":"Klibanov","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2004,2,18]]},"reference":[{"key":"e_1_2_1_2_2","first-page":"107","volume-title":"Applications of Biochemical Systems in Organic Chemistry","author":"Jones J. 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