Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/38172
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dc.contributor.authorLiu, Y.C.en_US
dc.contributor.author洪慧芝zh_TW
dc.contributor.authorLiu, Y.L.en_US
dc.contributor.authorSu, J.Y.en_US
dc.contributor.authorLiu, G.Y.en_US
dc.contributor.authorHung, H.C.en_US
dc.date2011zh_TW
dc.date.accessioned2014-06-06T08:00:35Z-
dc.date.available2014-06-06T08:00:35Z-
dc.identifier.issn1932-6203zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/38172-
dc.description.abstractBoth ornithine decarboxylase (ODC) and its regulatory protein, antizyme inhibitor (AZI), can bind with antizyme (AZ), but the latter has a higher AZ-binding affinity. The results of this study clearly identify the critical amino acid residues governing the difference in AZ-binding affinities between human ODC and AZI. Inhibition experiments using a series of ODC mutants suggested that residues 125 and 140 may be the key residues responsible for the differential AZ-binding affinities. The ODC_N125K/M140K double mutant demonstrated a significant inhibition by AZ, and the IC(50) value of this mutant was 0.08 mu M, three-fold smaller than that of ODC_WT. Furthermore, the activity of the AZ-inhibited ODC_N125K/M140K enzyme was hardly rescued by AZI. The dissociation constant (K(d)) of the [ODC_N125K/M140K]-AZ heterodimer was approximately 0.02 mu M, which is smaller than that of WT_ODC by approximately 10-fold and is very close to the K(d) value of AZI_WT, suggesting that ODC_N125K/M140K has an AZ-binding affinity higher than that of ODC_WT and similar to that of AZI. The efficiency of the AZI_K125N/K140M double mutant in the rescue of AZ-inhibited ODC enzyme activity was less than that of AZI_WT. The K(d) value of [AZI_K125N/K140M]-AZ was 0.18 mu M, nine-fold larger than that of AZI_WT and close to the K(d) value of ODC_WT, suggesting that AZI_K125N/K140M has an AZ-binding affinity lower than that of AZI_WT and similar to that of ODC. These data support the hypothesis that the differences in residues 125 and 140 in ODC and AZI are responsible for the differential AZ-binding affinities.en_US
dc.language.isoen_USzh_TW
dc.relationPlos Oneen_US
dc.relation.ispartofseriesPlos One, Volume 6, Issue 4.en_US
dc.relation.urihttp://dx.doi.org/10.1371/journal.pone.0019253en_US
dc.titleCritical Factors Governing the Difference in Antizyme-Binding Affinities between Human Ornithine Decarboxylase and Antizyme Inhibitoren_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1371/journal.pone.0019253zh_TW
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeJournal Article-
item.cerifentitytypePublications-
item.fulltextno fulltext-
item.languageiso639-1en_US-
item.grantfulltextnone-
Appears in Collections:生命科學系所
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