Oligomeric Structures Determine the Biochemical Characteristics of Human Nucleoside Diphosphate Kinases

Sun Young Kim, Eun Joo Song, Keun Hye Chang, Eunhee Kim, Suhn Kee Chae, Hansoo Lee, Kong Joo Lee

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


Major human Nucleoside diphosphate kinases (NDPKs) exist as hetero-oligomers, consisting of NDPK-A and NDPK-B, rather than homo-oligomer. To investigate their biological function depending on the oligomeric structure in vivo, we characterized the biochemical properties of cellular NDPK. Cellular NDPKs, which are made up of a unique combination of isoforms, were purified from human erythrocyte and placenta. We found that cellular NDPK and recombinant isoforms NDPKs have their own distinct biochemical properties in autophosphorylation, stability toward heat or urea, and DNA binding. Cellular NDPK was found to have unique characteristics rather than the expected additive properties of recombinant isoforms. The mutations in the dimeric interface of NDPK-B (R34G, N69H or K135L) caused defective DNA binding and simultaneously reduced the enzymatic stability. These results suggest that the oligomeric interaction could play a major role in the stability of catalytic domain and might be related to the regulation of various cellular functions of NDPK.

Original languageEnglish
Pages (from-to)355-364
Number of pages10
JournalJournal of Biochemistry and Molecular Biology
Issue number4
StatePublished - 31 Jul 2001


  • DNA binding property
  • Enzymatic activity
  • Heteromeric NDPK
  • Nucleoside diphosphate kinase
  • Quaternary structure


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