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Chemical Compound Review:

PubChem10166 2-amino-3-methyl-butanedioic acid

Synonyms: AGN-PC-009I73, AG-L-65456, ACMC-20aegx, M6126_SIGMA, ANW-63274, ...

Botting, N.P. et al., Kato, Y. et al., Boiangiu, C.D. et al., Ogasawara, Y. et al., Plugge, C.M. et al.

Plugge, van Leeuwen, Hummelen, Balk, Stams,

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Disease relevance of beta-methylaspartate

The enzyme 3-methylaspartase (3-methylaspartate ammonia-lyase, EC 4. 3.1.2) was found in the cells of enteric bacteria, especially in the genera Citrobacter and Morganella, that were grown under anoxic and oxygen-limited conditions [1].
The macrolactam antibiotic vicenistatin, produced in Streptomyces halstedii HC34, is biosynthesized by the polyketide pathway, using a unique 3-methylaspartate-derived molecule as starter unit [2].
The coenzyme B(12)-dependent pathway in Clostridium tetanomorphum via 3-methylaspartate involves pyruvate:ferredoxin oxidoreductase and a novel enzyme, a membrane-bound NADH:ferredoxin oxidoreductase [3].

High impact information on beta-methylaspartate

Substrate specificity of the 3-methylaspartate ammonia-lyase reaction: observation of differential relative reaction rates for substrate-product pairs [4].
A range of substituted fumaric and aspartic acid substrates for the enzyme 3-methylaspartate ammonia-lyase (EC 4.3.1.2) have been synthesized and used to study the kinetics of the catalyzed reaction in both the forward (deamination) and reverse (conjugative amination) reaction directions [4].

Analytical, diagnostic and therapeutic context of beta-methylaspartate

Acetate was found to be formed through the beta-methylaspartate pathway in pure culture as well as in coculture [5].

References

3-Methylaspartate ammonia-lyase as a marker enzyme of the mesaconate pathway for (S)-glutamate fermentation in Enterobacteriaceae. Kato, Y., Asano, Y. Arch. Microbiol. (1997) [Pubmed]
Involvement of glutamate mutase in the biosynthesis of the unique starter unit of the macrolactam polyketide antibiotic vicenistatin. Ogasawara, Y., Kakinuma, K., Eguchi, T. J. Antibiot. (2005) [Pubmed]
Sodium ion pumps and hydrogen production in glutamate fermenting anaerobic bacteria. Boiangiu, C.D., Jayamani, E., Brugel, D., Herrmann, G., Kim, J., Forzi, L., Hedderich, R., Vgenopoulou, I., Pierik, A.J., Steuber, J., Buckel, W. J. Mol. Microbiol. Biotechnol. (2005) [Pubmed]
Substrate specificity of the 3-methylaspartate ammonia-lyase reaction: observation of differential relative reaction rates for substrate-product pairs. Botting, N.P., Akhtar, M., Cohen, M.A., Gani, D. Biochemistry (1988) [Pubmed]
Elucidation of the pathways of catabolic glutamate conversion in three thermophilic anaerobic bacteria. Plugge, C.M., van Leeuwen, J.M., Hummelen, T., Balk, M., Stams, A.J. Arch. Microbiol. (2001) [Pubmed]

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