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:

MDH1 - malate dehydrogenase 1, NAD (soluble)

Sus scrofa

Shatalin, K. et al., Trejo, F. et al., Cortés, A. et al., Joh, T. et al., Jackson, R.M. 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 MDH1

Surface residues responsible for malate dehydrogenases being dimers were revealed by superimposing the structures of two dimers of pig cytosolic malate dehydrogenase on one homologous tetramer of L-lactate dehydrogenase from Bacillus stearothermophilus [1].

High impact information on MDH1

The interactions between pig heart citrate synthase and mitochondrial malate dehydrogenase or cytosolic malate dehydrogenase were studied using the frontal analysis method of gel filtration and by precipitation in polyethylene glycol [2].
On the other hand, the amino acid sequences of mouse cMDH and mitochondrial MDH (mMDH) showed about 23% overall homology [3].
A cDNA clone, named ppcMDH-1 and covering a part of the coding region for the porcine cytosolic malate dehydrogenase (cMDH) mRNA, was isolated from a porcine liver cDNA library [3].
The interaction of mitochondrial citrate synthase with cytosolic malate dehydrogenase was found to be much weaker, whereas interaction of citrate synthase with another cytosolic enzyme, aldolase, could not be detected [4].
The type of analysis proposed has been tested experimentally by examining inhibition of lactate dehydrogenase by oxalate (an uncompetitive inhibitor with respect to pyruvate) and oxamate (a competitive inhibitor with respect to pyruvate), and of cytosolic malate dehydrogenase by hydroxymalonate (a mixed inhibitor with respect to oxaloacetate) [5].

Biological context of MDH1

As expected based on the observation of extensive linkage conservation and based on the previous assignment of the malate dehydrogenase locus (MDH1) in swine, APOB maps to chromosome 3, specifically to region 3q24-qter [6].
The recombinant cMDH purified was shown to be identical to the native enzyme according to: chromatographic behaviour, isoelectric point, N-terminal amino acid sequence, and physiochemical and catalytic properties [7].
Using the polymerase chain reaction, DNA encoding cytosolic malate dehydrogenase (cMDH) has been cloned from a pig heart cDNA library [7].
A model of the fusion protein with the cytosolic malate dehydrogenase shows no clear positive electrostatic potential surface between the two active sites, thus distinguishing it from the fusion protein with the mitochondrial malate dehydrogenase [8].

Associations of MDH1 with chemical compounds

A fusion protein of porcine citrate synthase and porcine cytosolic malate dehydrogenase does not exhibit any channeling of oxaloacetate [8].

Analytical, diagnostic and therapeutic context of MDH1

Molecular cloning and mapping of a human cDNA for cytosolic malate dehydrogenase (MDH1) [9].

References

Construction of a stable dimer of Bacillus stearothermophilus lactate dehydrogenase. Jackson, R.M., Gelpi, J.L., Cortes, A., Emery, D.C., Wilks, H.M., Moreton, K.M., Halsall, D.J., Sleigh, R.N., Behan-Martin, M., Jones, G.R. Biochemistry (1992) [Pubmed]
Interaction between citrate synthase and malate dehydrogenase. Substrate channeling of oxaloacetate. Morgunov, I., Srere, P.A. J. Biol. Chem. (1998) [Pubmed]
Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase. Joh, T., Takeshima, H., Tsuzuki, T., Setoyama, C., Shimada, K., Tanase, S., Kuramitsu, S., Kagamiyama, H., Morino, Y. J. Biol. Chem. (1987) [Pubmed]
Quantitation of the interaction between citrate synthase and malate dehydrogenase. Tompa, P., Batke, J., Ovadi, J., Welch, G.R., Srere, P.A. J. Biol. Chem. (1987) [Pubmed]
Relationships between inhibition constants, inhibitor concentrations for 50% inhibition and types of inhibition: new ways of analysing data. Cortés, A., Cascante, M., Cárdenas, M.L., Cornish-Bowden, A. Biochem. J. (2001) [Pubmed]
Assignment of the pig apolipoprotein B locus (APOB) to chromosome region 3q24-qter. Solinas, S., Hasler-Rapacz, J., Maeda, N., Rapacz, J., Fries, R. Anim. Genet. (1992) [Pubmed]
Cloning, sequencing and functional expression of a DNA encoding pig cytosolic malate dehydrogenase: purification and characterization of the recombinant enzyme. Trejo, F., Costa, M., Gelpí, J.L., Busquets, M., Clarke, A.R., Holbrook, J.J., Cortés, A. Gene (1996) [Pubmed]
Electrostatic channeling of oxaloacetate in a fusion protein of porcine citrate synthase and porcine mitochondrial malate dehydrogenase. Shatalin, K., Lebreton, S., Rault-Leonardon, M., Vélot, C., Srere, P.A. Biochemistry (1999) [Pubmed]
Molecular cloning and mapping of a human cDNA for cytosolic malate dehydrogenase (MDH1). Tanaka, T., Inazawa, J., Nakamura, Y. Genomics (1996) [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.