Reaction mechanism for the conversion of 5-monosubstituted hydantoins to enantiomerically pure L-amino acids.
The specific conversion of D,L-5-monosubstituted hydantoins to optically pure L-amino acids by resting cells of Arthrobacter sp. DSM 7330 has been evaluated. A new nonstereoselective hydantoinase from Arthrobacter sp. DSM 7330 was isolated and characterized. When whole cells were tested, the conversion of D,L-5-methylthioethylhydantoin (D,L-5-MTEH) led to the optically pure intermediate D-carbamoylmethionine (D-CM) and to the optically pure amino acid L-methionine. After purification of the hydantoin hydrolyzing enzyme, the probable reaction mechanism of the conversion of 5-monosubstituted hydantoins to enantiomerically pure L-amino acids could be enlightened.
Völkel
D
D
Institute of Biochemistry and Biotechnology Technical University of Braunschweig, Germany.
Wagner
F
F
D000581:Amidohydrolases / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000138:chemical synthesis*; D001173:Arthrobacter / Q000378:metabolism; D001711:Biotransformation; D006827:Hydantoins / Q000737:chemistry*; D008969:Molecular Sequence Data; D013237:Stereoisomerism
D000596:Amino Acids; D006827:Hydantoins; D000581:Amidohydrolases; C020047:dihydropyrimidinase