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Gene Review

ECs0077  -  3-isopropylmalate dehydrogenase

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs0077

  • A DNA fragment carrying the LEU2 gene of methylotrophic yeast Hansenula polymorpha was isolated by complementation of the leuB mutation of Escherichia coli [1].
  • We have investigated factors affecting stability at the subunit-subunit interface of the dimeric enzyme 3-isopropylmalate dehydrogenase (IPMDH) from Bacillus subtilis [2].
  • RESULTS: We have co-crystallized Thermus thermophilus IMDH with NAD+ and have determined the structure at 2.5 A resolution [3].

High impact information on ECs0077

  • Beta-decarboxylating dehydrogenases comprise 3-isopropylmalate dehydrogenase, isocitrate dehydrogenase, and homoisocitrate dehydrogenase [4].
  • The activity of 3-isopropylmalate dehydrogenase (EC, encoded by the leuB gene, was significantly increased in C. glutamicum cells harbouring a plasmid containing the 2.2-kb fragment [5].
  • BACKGROUND: The leucine biosynthetic enzyme 3-isopropylmalate dehydrogenase (IMDH) belongs to a unique class of bifunctional decarboxylating dehydrogenases [3].
  • Physiological specificity of IMDH for NAD+ versus NADP+ can be explained by the unique interaction between Asp278 and the free 2'-hydroxyl of the NAD+ adenosine, discrimination against the presence of the 2'-phosphate by the negative charge on Asp278, and the absence of potential favorable interactions with the 2'-phosphate of NADP+ [3].
  • The cloned 7.2 kb DNA consisting of HindIII fragments of 4.0 kb and 3.2 kb could substitute for leucine genes (alpha-isopropylmalate (alpha-IPM) synthetase gene, beta-IPM dehydrogenase gene, and alpha-IPM isomerase gene) of E. coli and B. subtilis, but not ilvB gene of B. subtilis [6].

Chemical compound and disease context of ECs0077


Biological context of ECs0077


Analytical, diagnostic and therapeutic context of ECs0077


  1. Isolation and characterization of the LEU2 gene of Hansenula polymorpha. Agaphonov, M.O., Poznyakovski, A.I., Bogdanova, A.I., Ter-Avanesyan, M.D. Yeast (1994) [Pubmed]
  2. Increased thermal stability against irreversible inactivation of 3-isopropylmalate dehydrogenase induced by decreased van der Waals volume at the subunit interface. Ohkuri, T., Yamagishi, A. Protein Eng. (2003) [Pubmed]
  3. Structure of 3-isopropylmalate dehydrogenase in complex with NAD+: ligand-induced loop closing and mechanism for cofactor specificity. Hurley, J.H., Dean, A.M. Structure (1994) [Pubmed]
  4. Bifunctional isocitrate-homoisocitrate dehydrogenase: a missing link in the evolution of beta-decarboxylating dehydrogenase. Miyazaki, K. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  5. Analysis of the leuB gene from Corynebacterium glutamicum. Pátek, M., Hochmannová, J., Jelínková, M., Nesvera, J., Eggeling, L. Appl. Microbiol. Biotechnol. (1998) [Pubmed]
  6. Cloning of leucine genes of alkalophilic Bacillus No. 221 in E. coli and B. subtilis. Honda, H., Kato, C., Kudo, T., Horikoshi, K. J. Biochem. (1984) [Pubmed]
  7. Statistical criteria for the identification of protein active sites using Theoretical Microscopic Titration Curves. Ko, J., Murga, L.F., André, P., Yang, H., Ondrechen, M.J., Williams, R.J., Agunwamba, A., Budil, D.E. Proteins (2005) [Pubmed]
  8. Crystallization and preliminary X-ray studies of a Bacillus subtilis and Thermus thermophilus HB8 chimeric 3-isopropylmalate dehydrogenase. Onodera, K., Moriyama, H., Takenaka, A., Tanaka, N., Akutsu, N., Muro, M., Oshima, T., Imada, K., Sato, M., Katsube, Y. J. Biochem. (1991) [Pubmed]
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