title: A new D-stereospecific amino acid amidase from Ochrobactrum anthropi.
abstract: 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.
authors.affiliation: Sagami Chemical Research Center, Kanagawa, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Asano
authors.forename: T
authors.initials: T
authors.lastname: Mori
authors.forename: S
authors.initials: S
authors.lastname: Hanamoto
authors.forename: Y
authors.initials: Y
authors.lastname: Kato
authors.forename: A
authors.initials: A
authors.lastname: Nakazawa
mesh_terms: 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
chemical_list: D001426:Bacterial Proteins; D000581:Amidohydrolases