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Reaction Mechanism for the Conversion of 5‐Monosubstituted Hydantoins to Enantiomerically Pure l ‐Amino Acids a
Author(s) -
VÖLKEL DIRK,
WAGNER FRITZ
Publication year - 1995
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1995.tb19916.x
Subject(s) - hydantoin , arthrobacter , amino acid , chemistry , optically active , methionine , stereochemistry , enzyme , organic chemistry , biochemistry
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.