The N-acylpeptide hydrolase from porcine intestine: isolation, subcellular localization and comparative hydrolysis of peptide and isopeptide bonds.
The N-acylpeptide hydrolase from porcine intestinal mucosa was 2000-fold purified by a five-step procedure. The resulting protein (about 300 kDa) is composed of four apparently identical N-acylated polypeptide chains. The enzyme activity was found to be equally distributed along the crypt-villus axis in the intestine and was characterized as a cytosolic protein. Besides the ability of porcine intestinal APH to cleave the first peptide bond in N-protected peptides (Km: 0.8 mM), it is worth stressing that the enzyme was also found to efficiently catalyze the hydrolysis of the isopeptide bond in N-epsilon-Ac-L-Met-L-Lys (Km: 0.7-1.1 mM). It is suggested that N-acylpeptide hydrolase might not only be involved in the catabolism of intracellular N-acylated protein catabolism but also be responsible for the biological utilization of N-acylated food proteins.
Raphel
V
V
Laboratoire de Biochimie et Biologie de la Nutrition, CNRS-ERS 25, Faculté des Sciences et Techniques St-Jérôme, Marseille, France.
Lupi
N
N
Dupuis
L
L
Puigserver
A
A
D000469:Alkaline Phosphatase / Q000378:metabolism; D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D018826:CD13 Antigens; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D007413:Intestinal Mucosa / Q000166:cytology / Q000201:enzymology*; D007700:Kinetics; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009842:Oligopeptides / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar; D013552:Swine; D014018:Tissue Distribution
D009842:Oligopeptides; D000469:Alkaline Phosphatase; D010447:Peptide Hydrolases; D000626:Aminopeptidases; D018826:CD13 Antigens; C038220:acylaminoacyl-peptidase