Literature summary for 3.1.2.29 extracted from

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

Search for more literature for 3.1.2.29

Protein Variants

Protein Variants	Comment	Organism
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

Organism	UniProt	Comment	Textmining
Streptomyces cattleya	Q1EMV2	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	?	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)