Mutagenesis of Ala290, which modulates substrate subsite affinity at the catalytic interface of dimeric ThMA.

@article{Park2005MutagenesisOA,
  title={Mutagenesis of Ala290, which modulates substrate subsite affinity at the catalytic interface of dimeric ThMA.},
  author={S. Park and H. Cha and Hee-Kwon Kang and Jae-Hoon Shim and Eui-Jeon Woo and J. Kim and K. Park},
  journal={Biochimica et biophysica acta},
  year={2005},
  volume={1751 2},
  pages={
          170-7
        }
}
  • S. Park, H. Cha, +4 authors K. Park
  • Published 2005
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • The goal of this study was to develop a maltose-producing enzyme using protein engineering and to clarify the relation between the substrate specificity and the structure of the substrate-binding site of dimeric maltogenic amylase isolated from Thermus (ThMA). Ala290 at the interface of ThMA dimer in the vicinity of the substrate-binding site was substituted with isoleucine, which may cause a structural change due to its bulky side chain. TLC analysis of the action pattern of the mutant ThMA… CONTINUE READING
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