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Literature summary for 5.4.99.4 extracted from

  • Buckel, W.; Pierik, A.J.; Plett, S.; Alhapel, A.; Suarez, D.; Tu, S.; Golding, B.T.
    Mechanism-based inactivation of coenzyme B12-dependent 2-methyleneglutarate mutase by (Z)-glutaconate and buta-1,3-diene-2,3-dicarboxylate (2006), Eur. J. Inorg. Chem., 2006, 3622-3626.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
(Z)-glutaconate mechanism-based inactivation. Inhibitor induces homolysis of the Co-C bond of coenzyme B12 to afford cob(II)alamin and the 5'-deoxyadenosyl radical. The 5'-deoxyadenosyl radical adds to the double bond of (Z)-glutaconate to afford a radical adduct and subsequent formation of aquocobalamin Eubacterium barkeri
buta-1,3-diene-2,3-dicarboxylate mechanism-based inactivation. Inhibitor induces homolysis of the Co-C bond of coenzyme B12 to afford cob(II)alamin and the 5'-deoxyadenosyl radical. The 5'-deoxyadenosyl radical adds to a double bond of buta-1,3-diene-2,3-dicarboxylate to afford a relatively stable radical adduct in the active site of the enzyme Eubacterium barkeri

Organism

Organism UniProt Comment Textmining
Eubacterium barkeri
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