The induction of 2-amino-Δ
2-thiazoline-4-carboxylic acid hydrolase (ATCase) and N-carbamoylcysteine amidohydrolase (NCCase), both of which are involved in the conversion step of 2-amino-Δ
2-thiazoline carboxylic acid (ATC) to cysteine, was studied with
Pseudomonas putida AJ3865. We found that
L-ATC induced
L-ATCase and
L-NCCase, but that
D-ATC induced only
L-NCCase, whereas
L- or
D-NCC and thiazoline derivatives did not induce both enzymes. The bacterium showed neither
D-ATCase nor
D-NCCase activities, indicating that the role of
L-ATC and
D-ATC was different in the enzyme induction. We also found new inducers,
D- and
L-methionine, S-methyl-
L-cysteine, cysteic acid, and 2-aminoethane sulfonic acid. However, the induction level of both enzymes by new inducers was much lower than those by
L-ATC and
D-ATC. Furthermore, the induction rate of both enzymes was synergistically increased only under a combination of
D,
L-ATC and new inducers. S-Compounds, however, such as new inducers except S-methyl-
L-cysteine, inhibited both enzyme activities. This is the first report on the new inducers, synergistic induction, and the new inhibitors of
L-ATCase and
L-NCCase.
View full abstract