Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
권호 표지
DOI QR코드

DOI QR Code

Site-Specific Modifications of the Cys-45 Residue in Human Dihydrolipoamide Dehydrogenase to Ser and Tyr

  • Kim, Hak-Jung (Department of Chemistry, College of Natural Science)
  • Published : 2007.06.20
Download PDF
⟨ Previous Next ⟩

Abstract

Keywords

References

  1. Williams, C. H., Jr. Enzymes, 3rd ed; Boyer, P., Ed.; Academic Press: 1976; p 89
  2. Jentoft, J. E.; Shoham, M.; Hurst, D.; Patel, M. S. Proteins: Struct. Funct. Genet. 1992, 14, 88 https://doi.org/10.1002/prot.340140110
  3. Kim, H.; Patel, M. S. J. Biol. Chem. 1992, 267, 5128
  4. Kim, H. Bull. Korean Chem. Soc. 2006, 27, 819 https://doi.org/10.5012/bkcs.2006.27.6.819
  5. Karim, M.; Shim, M.-Y.; Kim, J.; Choi, K.-J.; Kim, J.-R.; Choi, J.-D.; Yoon, M.-Y. Bull. Korean Chem. Soc. 2006, 27, 549 https://doi.org/10.5012/bkcs.2006.27.4.549
  6. Kim, H. J. Biochem. Mol. Biol. 2005, 38, 248 https://doi.org/10.5483/BMBRep.2005.38.2.248
  7. Kim, H. J. Biochem. Mol. Biol. 2006, 39, 223 https://doi.org/10.5483/BMBRep.2006.39.2.223
  8. Thieme, R.; Pai, E. F.; Schirmer, R. H.; Schulz, G. E. J. Mol. Biol., 1981, 152, 763 https://doi.org/10.1016/0022-2836(81)90126-1

Cited by

  1. Characterization of Site-specific Mutations in Human Dihydrolipoamide Dehydrogenase Significantly Destabilizing the Transition State of the Enzyme Catalysis vol.59, pp.4, 2015, https://doi.org/10.5012/jkcs.2015.59.4.344
  2. Characterization of Two Naturally Occurring Mutations Close to Cofactors in Human Dihydrolipoamide Dehydrogenase vol.29, pp.12, 2008, https://doi.org/10.5012/bkcs.2008.29.12.2327
  3. Characterization of Two Site-Specific Human Cytosolic Thioredoxin Mutants (Pro-34 to Ala and Val) vol.30, pp.12, 2007, https://doi.org/10.5012/bkcs.2009.30.12.2869
  4. Characterization of a Naturally Occurring Mutation (Ile-12 to Thr) Close to Prosthetic Group FAD in Human Dihydrolipoamide Dehydrogenase vol.30, pp.4, 2007, https://doi.org/10.5012/bkcs.2009.30.4.777