Racemic 3,3,3-trifluoro-2-aminoisobutyrate (F3AIB) causes complete, irreversible inactivation of Pseudomonas cepaciaα-dialkylamino acid transaminase. The inactivation reaction is first order in enzyme and is saturable with respect to F3AIB, with an apparent Michaelis constant of 0.15 mM. Competitive inhibition of the inactivation reaction by substrate, 2-aminoisobutyrate, and product, L-alanine, implicates complex formation between F3AIB and the enzyme active site. Tracer studies using [1-14C]F3AIB reveal that decarboxylation of F3AIB precedes inactivation. © 1979.