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Chemical Compound Review:

AG-F-26115 2-methylidenepentanedioic acid

Synonyms: CHEBI:17207, NSC-21369, AC1L3TOU, NSC21369, KB-25112, ...

Beatrix, B. et al., Pierik, A.J. et al., Michel, C. et al., Hartrampf, G. et al., Chen, H. et al., et al.

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Disease relevance of NSC21369

2-Methyleneglutarate mutase from the anaerobe Eubacterium (Clostridium) barkeri is an adenosylcobalamin (coenzyme B(12))-dependent enzyme that catalyzes the equilibration of 2-methyleneglutarate with (R)-3-methylitaconate [1].
Rotation of the exo-methylene group of (R)-3-methylitaconate catalyzed by coenzyme B(12)-dependent 2-methyleneglutarate mutase from Eubacterium barkeri [1].
Only 2-methylenepentanedioic acid (2-MPA), which resembles closely the ketone form of 2-OG, is able to elicit cell responses in the cyanobacterium Anabaena by inducing nitrogen-fixing cells called heterocysts [2].
(c) Cell-free extracts from E. coli carrying the mgm gene showed 2-methyleneglutarate mutase activity that was strictly dependent on the addition of coenzyme B12 [3].

High impact information on NSC21369

Searching for intermediates in the carbon skeleton rearrangement of 2-methyleneglutarate to (R)-3-methylitaconate catalyzed by coenzyme B12-dependent 2-methyleneglutarate mutase from Eubacterium barkeri [4].
The kinetics of this process suggest that cob(II)alamin may reduce the enzyme-bound organic radical so that stable adducts between the adenosyl moiety of the coenzyme and 2-methyleneglutarate are formed [5].
Partially purified 2-methyleneglutarate mutase from Clostridium barkeri was separated from 3-methylitaconate delta-isomerase by treatment with 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS) followed by FPLC on the anion exchange column Mono Q in the presence of the detergent [6].
(a) The mgm gene encoding 2-methyleneglutarate mutase was cloned and its nucleotide sequence was determined [3].
The coenzyme B12 (adenosylcobalamin)-dependent 2-methyleneglutarate mutase catalyses the carbon skeleton rearrangement of 2-methyleneglutarate to (R)-3-methylitaconate in the fermentation of nicotinic acid by the strict anaerobic bacterium Clostridium barkeri [3].

Chemical compound and disease context of NSC21369

On the role of two different cobalt(II) species in coenzyme B12-dependent 2-methyleneglutarate mutase from Clostridium barkeri [7].

Associations of NSC21369 with other chemical compounds

The results demonstrate that 2-methyleneglutarate mutase catalyses the reversible migration of an acryloyl residue from the alpha-carbon to the beta-carbon of propionate with inversion of configuration at the alpha-carbon [8].

Analytical, diagnostic and therapeutic context of NSC21369

Purification of the coenzyme B12-containing 2-methyleneglutarate mutase from Clostridium barkeri by high-performance liquid chromatography [9].

References

Rotation of the exo-methylene group of (R)-3-methylitaconate catalyzed by coenzyme B(12)-dependent 2-methyleneglutarate mutase from Eubacterium barkeri. Pierik, A.J., Ciceri, D., Bröker, G., Edwards, C.H., McFarlane, W., Winter, J., Buckel, W., Golding, B.T. J. Am. Chem. Soc. (2002) [Pubmed]
Studying the signaling role of 2-oxoglutaric acid using analogs that mimic the ketone and ketal forms of 2-oxoglutaric acid. Chen, H., Laurent, S., Bédu, S., Ziarelli, F., Chen, H.L., Cheng, Y., Zhang, C.C., Peng, L. Chem. Biol. (2006) [Pubmed]
Cloning, sequencing and expression of the gene encoding the coenzyme B12-dependent 2-methyleneglutarate mutase from Clostridium barkeri in Escherichia coli. Beatrix, B., Zelder, O., Linder, D., Buckel, W. Eur. J. Biochem. (1994) [Pubmed]
Searching for intermediates in the carbon skeleton rearrangement of 2-methyleneglutarate to (R)-3-methylitaconate catalyzed by coenzyme B12-dependent 2-methyleneglutarate mutase from Eubacterium barkeri. Pierik, A.J., Ciceri, D., Lopez, R.F., Kroll, F., Bröker, G., Beatrix, B., Buckel, W., Golding, B.T. Biochemistry (2005) [Pubmed]
A novel reaction between adenosylcobalamin and 2-methyleneglutarate catalyzed by glutamate mutase. Huhta, M.S., Ciceri, D., Golding, B.T., Marsh, E.N. Biochemistry (2002) [Pubmed]
Coenzyme B12-dependent 2-methyleneglutarate mutase from Clostridium barkeri. Protection by the substrate from inactivation by light. Michel, C., Buckel, W. FEBS Lett. (1991) [Pubmed]
On the role of two different cobalt(II) species in coenzyme B12-dependent 2-methyleneglutarate mutase from Clostridium barkeri. Zelder, O., Buckel, W. Biol. Chem. Hoppe-Seyler (1993) [Pubmed]
On the steric course of the adenosylcobalamin-dependent 2-methyleneglutarate mutase reaction in Clostridium barkeri. Hartrampf, G., Buckel, W. Eur. J. Biochem. (1986) [Pubmed]
Purification of the coenzyme B12-containing 2-methyleneglutarate mutase from Clostridium barkeri by high-performance liquid chromatography. Michel, C., Buckel, W., Linder, D. J. Chromatogr. (1991) [Pubmed]

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