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]

Chemical Compound Review:

AC1MIVDU (Z)-but-2-ene-1,2,3- tricarboxylic acid

Synonyms: CHEBI:16717, HMDB06357, AKOS006309225, C04225, 6061-93-4, ...

Beach, R.L. et al., Lauble, H. et al., Brock, M. 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 alpha-Methyl-cis-aconitate

The product of the dehydration of enzymatically synthesized (2S,3S)-methylcitrate was designated cis-2-methylaconitate because of its ability to form a cyclic anhydride at low pH [1].

High impact information on alpha-Methyl-cis-aconitate

Formation of alpha-methyl-cis-aconitate from synthetic methylcitrate could not be detected spectrophotometrically with the liver aconitase; if it occurs with either the liver or the heart enzyme, the rate would be less than 0.1% that obtained with DL-threo-alpha-methylisocitrate [2].
The alternate substrate alpha-methylisocitrate is derived from alpha-methyl-cis-aconitate during crystallization and is observed to bind in the active site in a manner very similar to that observed for isocitrate [3].

Gene context of alpha-Methyl-cis-aconitate

Mitochondrial bovine heart aconitase catalyzes a reversible reaction between D-threo-alpha-methylisocitrate (Km, 0.2 mM) and alpha-methyl-cis-aconitate (Km, 0.05 mM) at pH 7 [2].

References

Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase. Brock, M., Maerker, C., Schütz, A., Völker, U., Buckel, W. Eur. J. Biochem. (2002) [Pubmed]
Identification of D-threo-alpha-methylisocitrate as stereochemically specific substrate for bovine heart aconitase and inhibitor of TPN-linked isocitrate dehydrogenase. Beach, R.L., Aogaichi, T., Plaut, G.W. J. Biol. Chem. (1977) [Pubmed]
Steric and conformational features of the aconitase mechanism. Lauble, H., Stout, C.D. Proteins (1995) [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.