A lysosomal arylamidase is a member of a larger family of peptidases in lysosomes.
One form (form VI) of lysosomal arylamidase, having a molecular weight of 135,000 and an isoelectric point of 7.8, was purified from rat liver to apparent electrophoretic homogeneity. The enzyme consisted of three identical polypeptides with a molecular weight of 45,000, as judged by disk electrophoresis in the presence of sodium dodecyl sulfate (SDS). The enzyme hydrolyzed di- and tripeptides. The enzyme released a N-terminal amino acid from Leu5-enkephalin and Met-Lys-bradykinin; these have a tyrosine and a methionine at the N-terminus, respectively. The enzyme did not hydrolyze bradykinin, angiotensin and melanocyte-stimulating hormone release-inhibitory factor (MIF); these have a basic amino acid, an acidic amino acid, and a proline at the N-terminus, respectively.
Hiroi
Y
Y
Department of Nutritional Chemistry, Nakamura Gakuen University, Fukuoka, Japan.
Yamamoto
S
S
Oka
T
T
D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D001920:Bradykinin / Q000031:analogs & derivatives / Q000378:metabolism; D002458:Cell Fractionation; D002851:Chromatography, High Pressure Liquid; D004743:Enkephalin, Leucine / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007526:Isoelectric Point; D008099:Liver / Q000201:enzymology / Q000648:ultrastructure*; D008247:Lysosomes / Q000201:enzymology*; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D013379:Substrate Specificity
D010446:Peptide Fragments; C018103:bradykinin, Met-Lys-; D004743:Enkephalin, Leucine; D000626:Aminopeptidases; D001920:Bradykinin