References
- Dhuna, V., Bains, J. S., Kamboj, S. S., Sinngh, J., Shanmugavel and Saxena, A. K. (2005) Purification and characterization of a lectin from Arisaema tortuosum Schott having in-vitro anticancer activity against human cancer cell lines. J. Biochem. Mol. Biol. 38, 526-532. https://doi.org/10.5483/BMBRep.2005.38.5.526
- Jentoft, J. E., Shoham, M., Hurst, D. and Patel, M. S. (1992) A structural model for human dihydrolipoamide dehydrogenase. Proteins: Struct. Funct. Genet. 14, 88-101 https://doi.org/10.1002/prot.340140110
- Kim, H. (1999a) Protein engineering of an artificial intersubunit disulfide bond linkage in human dihydrolipoamide dehydrogenase. J. Biochem. Mol. Biol. 32, 76-81
- Kim, H. (1999b) Deletion of the last five amino acid residues in human dihydrolipoamide dehydrogenase. Bull. Korean Chem. Soc. 20, 1221-1224
- Kim, H. (2001) Consensus sequence for the active site disulfide bond region of dihydrolipoamide dehydrogenase with known primary structure. J. Natl. Sci. 18, 23-29
- Kim, H. (2002) Activity of human dihydrolipoamide dehydrogenase is reduced by mutation at threonine-44 of FAD-binding region to valine. J. Biochem. Mol. Biol. 35, 437-441 https://doi.org/10.5483/BMBRep.2002.35.4.437
- Kim, H. (2005) Asparagine-473 residue is important to the efficient function of human dihydrolipoamide dehydrogenase. J. Biochem. Mol. Biol. 38, 248-252 https://doi.org/10.5483/BMBRep.2005.38.2.248
- Kim, H., Liu, T.-C. and Patel, M. S. (1991) Expression of cDNA sequences encoding mature and precursor forms of human dihydrolipoamide dehydrogenase in Escherichia coli. J. Biol. Chem. 266, 9367-9373
-
Kim, H. and Patel, M. S. (1992) Characterization of two sitespecifically mutated human dihydrolipoamide dehydrogenases (His-452
${\rightarrow}$ Gln and Glu-457${\rightarrow}$ Gln). J. Biol. Chem. 267, 5128-5132 - Liu, T., Korotchkina, L. G., Hyatt, S. L., Vettakkorumakankav, N. N. and Patel, M. S. (1995) Spectroscopic studies of the characterization of recombinant human dihydrolipoamide dehydrogenase and its site-directed mutants. J. Biol. Chem. 270, 15545-15550 https://doi.org/10.1074/jbc.270.26.15545
-
Mattevi, A., Obmolova, G., Sokatch, J.R., Betzel, C., Hol, W. G. J. (1992) The refined crystal structure of Pseudomonas putide lipoamide dehydrogenase complexed with
$NAD^+$ at 2.45${\AA}$ resolution. Proteins Struct. Funct. Genet. 13, 336-351 https://doi.org/10.1002/prot.340130406 -
Pons, G., Raefsky-Estrin, C., Catothers, D. J., Pepin, R. A., Javed, A. A., Jesse, B. W., Ganapathi, M. K., Samols, D. and Patel, M. S. (1988) Cloning and cDNA sequence of the dihydrolipoamide dehydrogenase component of human
${\alpha}$ - ketoacid dehydrogenase complexes. Proc. Natl. Acad. Sci. USA 85, 1422-1426 https://doi.org/10.1073/pnas.85.5.1422 - Reed, L. J. (1974) Multienzyme complexes. Acc. Chem. Res. 7, 40-46 https://doi.org/10.1021/ar50074a002
- Schierbeek, A. J., Swarte, M. B. A., Dijkstra, B. W., Vriend, G., Reed, R. J., Hol, W. G. J. and Drenth, J. (1989) X-ray structure of lipoamide dehydrogenase from Azotobacter vinelandii determined by a combination of molecular and isomorphous replacement techniques. J. Mol. Biol. 206, 365-379 https://doi.org/10.1016/0022-2836(89)90486-5
- Srisuparbh, D., Klinbunga S., Wongsiri, A. and Sittipraneed, S. (2003) Isolation and characterization of major royal jelly cDNAs and proteins of the honey bee (Apis cerana). J. Biochem. Mol. Biol. 36, 572-579 https://doi.org/10.5483/BMBRep.2003.36.6.572
-
Thieme, R., Pai, E. F., Schirmer, R. H. and Schulz, G. E. (1981) Three-dimensional structure of glutathione reductase at 2
${\AA}$ resolution. J. Mol. Biol. 152, 763-782 https://doi.org/10.1016/0022-2836(81)90126-1 - Walker, J. L. and Oliver, D. J. (1986) Glycine decarboxylase multienzyme complex. Purification and partial characterization from leaf mitochondria. J. Biol. Chem. 261, 2214-2221
- Williams, C. H. Jr. (1976) Flavin containing dehydrogenases; in Enzymes, Boyer, P. (ed.), pp. 89-173, Academic Press, New York, USA
Cited by
- Radish phospholipid hydroperoxide glutathione peroxidase provides protection against hydroperoxide-mediated injury in mouse 3T3 fibroblasts vol.42, pp.10, 2009, https://doi.org/10.5483/BMBRep.2009.42.10.648
- The role of amino acids T148 and R281 in human dihydrolipoamide dehydrogenase vol.15, pp.1, 2007, https://doi.org/10.1007/s11373-007-9208-9
- Refolding of the human dihydrolipoamide dehydrogenase vol.45, pp.2, 2009, https://doi.org/10.1016/j.bej.2009.03.004
- Periplasmic cold expression and one-step purification of human dihydrolipoamide dehydrogenase vol.63, pp.1, 2009, https://doi.org/10.1016/j.pep.2008.09.009