Production of optically active amino acids and their derivatives by microbial hydantoinase

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(1)A novel ATP-dependent amidohydrolase(AIP-hydantoinase), which catalyzes hydrolysis of various 5-substituted hydantoins and ATP to the corresponding N-carbamoyl-L-amino acids, ammonia and carbon dioxide, and ADP and inorganic phosphate, respectively, was purified and crystallized from cells of a soil isolated bacterium PseudoMonas putida 77. the enzyme was found to catalyze the hydrolysis of several nucleoside triphosphates not only in the presence but also in the absence of amide substrate. The kinetic data suggested the conformational change of the enzyme after the binding of amide substrate. Such binding seemed to be absolutely necessary for the hydrolysis of nucleoside triphosphate. The enzyme was shown to be useful for the synthesis of various optically active N-carbamoyl-L-amino acids and for the determination of serum or urine creatine.(2)A new N-carbamoyl-D-amino acid amidohydrolase, which shows high specificity toward N-carbamoyl-D-p-hydroxyphenylglycine, was isolated from a Gram negative soil isolated bacterium and characterized in some details. The enzyme was shown to be highly thermostable and useful catalyst for the practical production of D-p-hydroxyphenylglycine.(3)A novel aromatic-aryl amidase which hydrolyzes various aromatic aryl-acyl amities, was found in a soil isolated Pseudomonase putida Sc-2. The enzyme was shown to be useful for optical resolution of various arcxuatic amines.(4)A new enzyme, nucleoside odidase which catalyzes oxidation of various nucleosides to the corresponding nucleoside 5'-carboxylic acids with concomitant production of hydrogenperoxide, was found in a soil isolated bacterium. The enzyme was seemed to have very close relation to the metabolism of hydantoin-pyrimidine metabolism.