Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Gene Review:

ECs0077 - 3-isopropylmalate dehydrogenase

Escherichia coli O157:H7 str. Sakai

Hurley, J.H. et al., Honda, H. et al., Ko, J. et al., Pátek, M. et al., Ohkuri, T. et al., et al.

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

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 1.1.1.85), 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

Detailed results are given for 4 enzymes with 4 different types of chemistry: arginine kinase from Limulus polyphemus (horseshoe crab); beta-lactamase from Escherichia coli; glutamate racemase from Aquifex pyrophilus; and 3-isopropylmalate dehydrogenase from Thiobacillus ferrooxidans [7].

Biological context of ECs0077

The expression of beta-IPM dehydrogenase gene of alkalophilic Bacillus No. 221 was repressed by the addition of leucine in the culture medium of B. subtilis carrying the plasmid pHK111 [6].

Analytical, diagnostic and therapeutic context of ECs0077

Crystallization and preliminary X-ray studies of a Bacillus subtilis and Thermus thermophilus HB8 chimeric 3-isopropylmalate dehydrogenase [8].

References

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]
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]
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]
Bifunctional isocitrate-homoisocitrate dehydrogenase: a missing link in the evolution of beta-decarboxylating dehydrogenase. Miyazaki, K. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
Analysis of the leuB gene from Corynebacterium glutamicum. Pátek, M., Hochmannová, J., Jelínková, M., Nesvera, J., Eggeling, L. Appl. Microbiol. Biotechnol. (1998) [Pubmed]
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]
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]
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]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.