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Literature summary extracted from

  • Weeks, A.M.; Chang, M.C.
    Catalytic control of enzymatic fluorine specificity (2012), Proc. Natl. Acad. Sci. USA, 109, 19667-19672.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.1.2.29 H76A the kinetic isotope effec observed with [2H2]fluoroacetyl-CoA is abolished in the H76A mutant, showing that H76 is directly involved in Calpha deprotonation Streptomyces cattleya

Organism

EC Number Organism UniProt Comment Textmining
3.1.2.29 Streptomyces cattleya Q1EMV2
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.2.29 additional information the high selectivity of fluoroacetyl-CoA thioesterase is achieved through catalysis rather than molecular recognition. Deprotonation at the Calpha position to form a putative ketene intermediate only occurs on the fluorinated substrate, thereby accelerating the rate of hydrolysis 10000fold compared with the nonfluorinated congene. An enzyme-anhydride intermediate is formed for the nonfluorinated substrate Streptomyces cattleya ?
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