X-Prolyl Aminopeptidase (Aminopeptidase P) 1, Soluble, XPNPEPL, SAMP, X-Prolyl Aminopeptidase 1, Soluble, Aminoacylproline Aminopeptidase, Cytosolic Aminopeptidase P, Soluble Aminopeptidase P, X-Pro Aminopeptidase 1, EC 3.4.11.9, XPNPEPL1, X-Prolyl Aminopeptidase (Aminopeptidase P)-Like, Aminopeptidase P, Cytosolic, Xaa-Pro Aminopeptidase 1, XPNPEP, APP1, Xaa-Pro aminopeptidase 1.
X-Prolyl Aminopeptidase (Aminopeptidase P) 1, Soluble, XPNPEPL, SAMP, X-Prolyl Aminopeptidase 1, Soluble, Aminoacylproline Aminopeptidase, Cytosolic Aminopeptidase P, Soluble Aminopeptidase P, X-Pro Aminopeptidase 1, EC 3.4.11.9, XPNPEPL1, X-Prolyl Aminopeptidase (Aminopeptidase P)-Like, Aminopeptidase P, Cytosolic, Xaa-Pro Aminopeptidase 1, XPNPEP, APP1, Xaa-Pro aminopeptidase 1.
XPNPEP1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
PAT9C7AT.
Anti-human XPNPEP1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human XPNPEP1 amino acids 1-623 purified from E. coli.
Mouse IgG2b heavy chain and κ light chain.
X-Prolyl Aminopeptidase-1 (XPNPEP1) is a proline-specific metalloaminopeptidase that plays a crucial role in the degradation and maturation of various peptides, including peptide hormones, neuropeptides, and tachykinins. This enzyme is encoded by the XPNPEP1 gene in humans and has significant implications in biological processes and potential therapeutic applications.
The XPNPEP1 gene is located on chromosome 10 in humans and chromosome 19 in mice . The gene encodes a cytosolic form of the enzyme that specifically catalyzes the removal of any unsubstituted N-terminal amino acid adjacent to a penultimate proline residue . This specificity towards proline residues is essential for its function in peptide metabolism.
X-Prolyl Aminopeptidase-1 is involved in the catabolic process of bradykinin, a peptide that plays a role in inflammation and blood pressure regulation . The enzyme’s activity is crucial for the degradation of bradykinin and other peptides, ensuring proper physiological function. The enzyme’s mechanism involves the binding of manganese ions, which are essential for its catalytic activity .
The enzyme’s ability to degrade proline-containing peptides makes it vital for various biological processes. It complements pancreatic peptidases in the digestion of dietary proteins and is involved in the maturation and degradation of peptide hormones and neuropeptides . Deficiency in X-Prolyl Aminopeptidase-1 can lead to the excretion of large amounts of imino-oligopeptides in urine, indicating its importance in peptide metabolism .
Research on X-Prolyl Aminopeptidase-1 has highlighted its potential therapeutic applications. The enzyme’s role in degrading bradykinin suggests it could be targeted for conditions related to inflammation and blood pressure regulation . Additionally, understanding its function and mechanism can provide insights into developing treatments for related metabolic disorders.