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 convers...

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Bibliographic Details
Published in:Annals of the New York Academy of Sciences 1995-03, Vol.750 (1), p.1-9
Main Authors: VÖLKEL, DIRK, WAGNER, FRITZ
Format: Article
Language:English
Subjects:
Amidohydrolases - chemistry
Amidohydrolases - metabolism
Amino Acid Sequence
Amino Acids - chemical synthesis
Arthrobacter - metabolism
Biotransformation
Hydantoins - chemistry
Molecular Sequence Data
Stereoisomerism
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Summary: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.
ISSN:0077-8923
1749-6632
DOI:10.1111/j.1749-6632.1995.tb19916.x