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DC Field | Value | Language |
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dc.citation.endPage | 9259 | - |
dc.citation.number | 14 | - |
dc.citation.startPage | 9252 | - |
dc.citation.title | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.citation.volume | 272 | - |
dc.contributor.author | Lee, SH | - |
dc.contributor.author | Seo, HY | - |
dc.contributor.author | Kim, JC | - |
dc.contributor.author | Heo, WD | - |
dc.contributor.author | Chung, WS | - |
dc.contributor.author | Lee, KJ | - |
dc.contributor.author | Kim, MC | - |
dc.contributor.author | Cheong, YH | - |
dc.contributor.author | Choi, JY | - |
dc.contributor.author | Lim, CO | - |
dc.contributor.author | Cho, Moo Je | - |
dc.date.accessioned | 2023-12-22T12:37:37Z | - |
dc.date.available | 2023-12-22T12:37:37Z | - |
dc.date.created | 2014-09-19 | - |
dc.date.issued | 1997-04 | - |
dc.description.abstract | NAD kinase is a Ca2+/calmodulin (CaM)-dependent enzyme capable of converting cellular NAD to NADP. The enzyme purified from pea seedlings can be activated by highly conserved soybean CaM, SCaM-1, but not by the divergent soybean CaM isoform, SCaM-4 (Lee, S. H., Kim, J. C., Lee, M. S., Heo, W. D., Seo, H. Y., Yoon, H. W., Hong, J. C., Lee, S. Y., Bahk, J. D., Hwang, I., and Cho, M. J. (1995) J. Biol. Chem. 270, 21806-21812). To determine which domains were responsible for this differential activation of NAD kinase, a series of chimeric SCaMs were generated by exchanging functional domains between SCaM-4 and SCaM-1. SCaM-4111, a chimeric SCaM-1 that contains the first domain of SCaM-4, was severely impaired (only 40% of maximal) in its ability to activate NAD kinase. SCaM-1444, a chimeric SCaM-4 that contains the first domain of SCaM-1 exhibited nearly full (~70%) activation of NAD kinase. Only chimeras containing domain I of SCaM-1 produced greater than half-maximal activation of NAD kinase. To define the amino acid residue(s) in domain I that were responsible for this differential activation, seven single residue substitution mutants of SCaM-1 were generated and tested for NAD kinase activation. Among these mutants, only K30E and G40D showed greatly reduced NAD kinase activation. Also a double residue substitution mutant, K30E/G40D, containing these two mutations in combination was severely impaired in its NAD kinase-activating potential, reaching only 20% of maximal activation. Furthermore, a triple mutation, K30E/M36I/G40D, completely abolished NAD kinase activation. Thus, our data suggest that domain I of CaM plays a key role in the differential activation of NAD kinase exhibited by SCaM-1 and SCaM-4. Further, the residues Lys30 and Glu40 of SCaM-1 are critical for this function. | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.272, no.14, pp.9252 - 9259 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.scopusid | 2-s2.0-0001281471 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/6321 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0001281471 | - |
dc.identifier.wosid | A1997WU03700064 | - |
dc.language | 영어 | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.title | Differential activation of NAD kinase by plant calmodulin isoforms - The critical role of domain I | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
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