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The mechanism of stereospecific conversion of DL-5-substituted hydantoins to the corresponding L-amino acids by Pseudomonas sp. strain NS671 was studied. The results indicated that the hydantoinase catalyzed the hydrolysis reaction of both D- and L-5-(2-methylthioethyl)hydantoin, and that the hydrolysis of the L-enantiomer proceeded preferentially compared with that of the D-enantiomer. On the basis of these findings, the mechanism was speculated to be as follows: DL-5-substituted hydantoins are converted exclusively to the L-forms of the corresponding N-carbamyl-amino acids by the hydantoinase in combination with hydantoin racemase. The N-carbamyl-L-amino acids are then converted to L-amino acids by N-carbamyl-L-amino acid amidohydrolase.

bioscience, biotechnology, and biochemistry

Mechanism of Stereospecific Conversion of<scp>dl</scp>-5-Substituted Hydantoins to the Corresponding<scp>l</scp>-Amino Acids by<i>Pseudomonas</i>sp. Strain NS671

Mechanism of Stereospecific Conversion ofdl-5-Substituted Hydantoins to the Correspondingl-Amino Acids byPseudomonassp. Strain NS671