TY  - JOUR
  - Curley, P,van der Does, C,Driessen, AJM,Kok, J,van Sinderen, D
  - 2003
  - February
  - Archives of Microbiology
  - Purification and characterisation of a lactococcal aminoacylase
  - Validated
  - ()
  - Lactococcus lactis aminoacylase purification kinetic analysis GENE-EXPRESSION SYSTEMS BACILLUS-STEAROTHERMOPHILUS THERMOSTABLE AMINOACYLASE STREPTOCOCCUS-CREMORIS PYROCOCCUS-HORIKOSHII SEQUENCE-ANALYSIS PORCINE KIDNEY AMINO-ACIDS LACTIS ENZYME
  - 179
  - 402
  - 408
  - The amd1-encoded aminoacylase from Lactococcus lactis MG1363 was cloned and overexpressed in Escherichia coli and purified. The assumed dimeric enzyme has a subunit molecular mass of about 42 kDa and contains 2.0+/-0.1 g-atoms of zinc and cobalt, in equimolar amounts, per subunit of Amd1. The enzyme was characterised with respect to substrate specificity, pH, temperature and metal dependence. Amd1 exhibited a broad activity range towards N-acetylated-L-amino acids with a strong preference towards those containing neutral aliphatic and aromatic side chains. It hydrolysed N-acetyl-L-alanine most efficiently, and exhibited temperature and pH optima of 30 degreesC and 7.0, respectively. The activity of Amd1 towards N-acetyl-L-alanine was enhanced by the divalent cation Co2+, while Cd2+ inhibited activity. Interestingly, Amd1 was shown to catalyse the hydrolysis of several dipeptides at pH 7.0, although with reduced V-max values as compared to hydrolysis of N-acetylated-L-amino acids. This characteristic has also biological significance since Amd1 was able to complement a growth deficiency in a L. lactis triple peptidase mutant.
  - DOI 10.1007/s00203-003-0544-5
DA  - 2003/02
ER  - 

@article{V43338018,
   = {Curley,  P and van der Does,  C and Driessen,  AJM and Kok,  J and van Sinderen,  D },
   = {2003},
   = {February},
   = {Archives of Microbiology},
   = {Purification and characterisation of a lactococcal aminoacylase},
   = {Validated},
   = {()},
   = {Lactococcus lactis aminoacylase purification kinetic analysis GENE-EXPRESSION SYSTEMS BACILLUS-STEAROTHERMOPHILUS THERMOSTABLE AMINOACYLASE STREPTOCOCCUS-CREMORIS PYROCOCCUS-HORIKOSHII SEQUENCE-ANALYSIS PORCINE KIDNEY AMINO-ACIDS LACTIS ENZYME},
   = {179},
  pages = {402--408},
   = {{The amd1-encoded aminoacylase from Lactococcus lactis MG1363 was cloned and overexpressed in Escherichia coli and purified. The assumed dimeric enzyme has a subunit molecular mass of about 42 kDa and contains 2.0+/-0.1 g-atoms of zinc and cobalt, in equimolar amounts, per subunit of Amd1. The enzyme was characterised with respect to substrate specificity, pH, temperature and metal dependence. Amd1 exhibited a broad activity range towards N-acetylated-L-amino acids with a strong preference towards those containing neutral aliphatic and aromatic side chains. It hydrolysed N-acetyl-L-alanine most efficiently, and exhibited temperature and pH optima of 30 degreesC and 7.0, respectively. The activity of Amd1 towards N-acetyl-L-alanine was enhanced by the divalent cation Co2+, while Cd2+ inhibited activity. Interestingly, Amd1 was shown to catalyse the hydrolysis of several dipeptides at pH 7.0, although with reduced V-max values as compared to hydrolysis of N-acetylated-L-amino acids. This characteristic has also biological significance since Amd1 was able to complement a growth deficiency in a L. lactis triple peptidase mutant.}},
   = {DOI 10.1007/s00203-003-0544-5},
  source = {IRIS}
}