A new D-stereospecific amino acid amidase from Ochrobactrum anthropi.
A new D-stereospecific amino acid amidase has been partially purified from Ochrobactrum anthropi SCRC SV3, which had been isolated and selected from soil. The Mr of the enzyme was estimated to be about 38,000, and its isoelectric point was 5.3. The enzyme catalyzes the stereospecific hydrolysis of D-amino acid amide to yield D-amino acid and ammonia. The major substrates included D-phenylalanine amide, D-tyrosine amide, D-tryptophan amide, D-leucine amide, and D-alanine amide.
Asano
Y
Y
Sagami Chemical Research Center, Kanagawa, Japan.
Mori
T
T
Hanamoto
S
S
Kato
Y
Y
Nakazawa
A
A
D000421:Alcaligenes / Q000201:enzymology*; D000581:Amidohydrolases / Q000302:isolation & purification* / Q000378:metabolism; D001426:Bacterial Proteins / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D013237:Stereoisomerism; D013379:Substrate Specificity; D013696:Temperature
D001426:Bacterial Proteins; D000581:Amidohydrolases