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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Mutations within the Putative Active Site of Heterodimeric Deoxyguanosine Kinase Block the Allosteric Activation of the Deoxyadenosine Kinase Subunit

  • Park, In-Shik (Faculty of Food Science, Dong-A University) ;
  • Ives, David H. (Department of Biochemistry, The Ohio State University)
  • Published : 2002.03.31
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Abstract

Replacement of the Asp-84 residue of the deoxyguanosine kinase subunit of the tandem deoxyadenosine kinase/deoxyguanosine kinase (dAK/dGK) from Lactobacillus acidophilus R-26 by Ala, Asn, or Glu produced increased $K_m$ values for deoxyguanosine on dGK. However, it did not seem to affect the binding of Mg-ATP. The Asp-84 dGK replacements bad no apparent effect on the binding of deoxyadenosine by dAK. However, the mutant dGKs were no longer inhibited by dGTP, normally a potent distal end-product inhibitor of dGK. Moreover, the allosteric activation of dAK activity by dGTP or dGuo was lost in the modified heterodimeric dAK/dGK enzyme. Therefore, it seems very likely that Asp-84 participates in dGuo binding at the active site of the dGK subunit of dAK/dGK from Lactobacillus acidophilus R-26.

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References

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