title: Purification and characterization of L-aminoacylase from Alcaligenes denitrificans DA181.
abstract: The L-aminoacylase produced intracellularly by Alcaligenes denitrificans DA181 was purified to homogeneity. This enzyme had an apparent molecular weight of 80,000, and was composed of two subunits of identical molecular weight. Its isoelectric point was pH 5.1. The optimal reaction temperature and pH were 65 degrees C and 8.0, respectively. This enzyme showed specificity toward N-acetyl-derivative of hydrophobic L-amino acids with N-acetyl-L-valine as the favored substrate, followed by N-acetyl-L-alanine.
authors.affiliation: Institute of Biochemistry, National Yang-Ming Medical College, Taipei, Taiwan, R.O.C.
authors.forename: Y B
authors.initials: YB
authors.lastname: Yang
authors.forename: H L
authors.initials: HL
authors.lastname: Hu
authors.forename: M C
authors.initials: MC
authors.lastname: Chang
authors.forename: H
authors.initials: H
authors.lastname: Li
authors.forename: Y C
authors.initials: YC
authors.lastname: Tsai
mesh_terms: D000421:Alcaligenes / Q000201:enzymology*; D000581:Amidohydrolases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D007526:Isoelectric Point; D008969:Molecular Sequence Data; D013379:Substrate Specificity
chemical_list: D000581:Amidohydrolases; C019672:aminoacylase I