Table 1 DadY is an imine deaminase in vitro.

^a significant difference in semicarbazone formation (p < 0.05, determined by Tukey’s multiple comparisons test) between indicated reactions and those with no Rid protein. Activity of reactions with DadY was significantly different than LOX alone with all amino acids tested. ^b significant difference in semicarbazone formation between reactions containing DadY and those with either RidA protein.
Reaction mixes (100 μl) contained potassium pyrophosphate pH 8.7 (50 mM), semicarbazide pH 7.0 (10 mM), bovine liver catalase (24 U), L-amino acid oxidase from Crotalus adamanteus (1 μg), and the Rid protein (25 μM, monomeric concentration) indicated. Reactions were initiated by the addition of the indicated substrate (20 mM) and absorbance at 248 nm was monitored over five minutes. The rate of semicarbazone formation was determined using the measured pathlength of each well and the molar extinction coefficient for semicarbazone (ε = 10300 M^-1 cm^-1). Data shown are the mean and standard deviation of three technical replicates. ND, no semicarbazone was de-tected; _SERidA, RidA from S. enterica; _PARidA, RidA from P. aeruginosa