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dc.contributor.authorHuang, CYen_US
dc.contributor.authorYang, YSen_US
dc.date.accessioned2014-12-08T15:19:35Z-
dc.date.available2014-12-08T15:19:35Z-
dc.date.issued2005-03-01en_US
dc.identifier.issn1046-5928en_US
dc.identifier.urihttp://dx.doi.org/10.1016/j.pep.2004.12.008en_US
dc.identifier.urihttp://hdl.handle.net/11536/13943-
dc.description.abstractEnzymatic hydrolysis of the N-iminylamide was investigated in this study. An enzyme possessing N-iminylamidase activity from pig liver was purified to electrophoretic homogeneity. This enzyme was also active, however, with imides and appears to be identical to pig liver imidase. The identification was confirmed by copurification of enzyme activities and by specificities of typical substrates of mammalian imidase, such as phthalimide, dihydrouracil, and maleimide. The hydrolysis of 3-iminoisoindolinone was further analyzed by HPLC, C-13 NMR spectrometry, and LC-MS measurements to determine its chemicoselectivity. All data indicated that this enzyme chemicoselectively catalyzed the hydrolysis of the N-iminylamide to produce the compound bearing the diamine and carboxylate group. The pH profiles of this enzyme suggest that one of the protons of 3-iminoisoindolinone was important to promote the ring-opening process of this substrate. These results constituted a first study on the enzymatic hydrolysis of compounds bearing the N-iminylamide functional group. (c) 2004 Elsevier Inc. All rights reserved.en_US
dc.language.isoen_USen_US
dc.subjectN-iminylamidaseen_US
dc.subjectimidaseen_US
dc.subjecthydantoinaseen_US
dc.subjectdihydropyrimidinaseen_US
dc.titleDiscovery of a novel N-iminylamidase activity: substrate specificity, chemico selectivity and catalytic mechanismen_US
dc.typeArticleen_US
dc.identifier.doi10.1016/j.pep.2004.12.008en_US
dc.identifier.journalPROTEIN EXPRESSION AND PURIFICATIONen_US
dc.citation.volume40en_US
dc.citation.issue1en_US
dc.citation.spage203en_US
dc.citation.epage211en_US
dc.contributor.department生醫工程研究所zh_TW
dc.contributor.departmentInstitute of Biomedical Engineeringen_US
dc.identifier.wosnumberWOS:000227516900024-
dc.citation.woscount5-
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