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Literature summary for 4.1.1.1 extracted from

  • Kellett, W.F.; Brunk, E.; Desai, B.J.; Fedorov, A.A.; Almo, S.C.; Gerlt, J.A.; Rothlisberger, U.; Richards, N.G.
    Computational, structural, and kinetic evidence that Vibrio vulnificus FrsA is not a cofactor-independent pyruvate decarboxylase (2013), Biochemistry, 52, 1842-1844.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
no activity in Vibrio vulnificus
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enzyme FrsAis not a cofactor-independent pyruvate decarboxylase. No pyruvate decarboxylase activity is detected for recombinant crystallized FrsA protein. The barrier to C-C bond cleavage in the bound substrate is 28 kcal/mol, which is similar to that estimated for the uncatalyzed decarboxylation of pyruvate in water at 25°C
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