26081-02-7Relevant articles and documents
Mechanism of Stereospecific Production of L-Amino Acids from the Corresponding 5-Substituted Hydantoins by Bacillus brevis
Yamashiro, Akihiro,Kubota, Koji,Yokozeki, Kenzo
, p. 2857 - 2864 (2007/10/02)
The mechanism of stereospecific production of L-amino acids from the corresponding 5-substituted hydantoins by Bacillus brevis AJ-12299 was studied.The enzymes involved in the reaction were partially purified by DEAE-Toyopearl 650M column chromatography and their properties were investigated.The conversion of DL-5-substituted hydantoins to the corresponding L-amino acids consisted of the following two successive reactions.The first step was the ring-opening hydrolysis to N-carbamoyl amino acids catalyzed by an ATP dependent L-5-substituted hydantoin hydrolase.This reaction was stereospecific and the N-carbamoyl amino acid produced was exclusively the L-form.N-Carbamoyl-L-amino acid was also produced from the D-form of 5-substituted hydantoin, which suggests that spontaneous racemization occurred in the reaction mixture.In the second step, N-carbamoyl-L-amino acid was hydrolyzed to L-amino acid by an N-carbamoyl-L-amino acid hydrolase, which was also an L-specific enzyme.The ATP dependency of the L-5-substituted hydantoin hydrolase was supposed to be the limiting factor in the production of L-amino acids from the corresponding 5-substituted hydantoins by this bacterium.