Aminopeptidase which hydrolyzes substrates with free N-terminal amino acid residues but not N-terminal blocked ones. May be important in the nutrition and pathogenesis of the organism in the human oral cavity.
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RNPEP: Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(- 1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4). Belongs to the peptidase M1 family.
Protein type: EC 188.8.131.52; Protease
Chromosomal Location of Human Ortholog: 1q32
Cellular Component: extracellular region; plasma membrane; secretory granule
Molecular Function: aminopeptidase activity; peptide binding; zinc ion binding
Biological Process: negative regulation of blood pressure; peptide catabolic process; proteolysis
encodes an aminopeptidase, a ortholog of mouse microsomal AP (EC 184.108.40.206).
Aminopeptidases catalyze the hydrolysis of amino acid residues from the N-terminus of peptide or protein substrates. Able to cleave angiotensin III to generate angiotensin IV, a bioactive peptide of the renin-angiotensin pathway. Not able to cleave angiotensin I and angiotensin II. May play a role in the proteolytic processing of bioactive peptides in tissues such as testis and heart ().
LVRN: Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo- maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met- MCA, Arg-LCA and Lys-LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C. Belongs to the peptidase M1 family. 4 isoforms of the human protein are produced by alternative splicing.
Protein type: EC 3.4.-.-; EC 3.4.11.-; Membrane protein, integral; Protease
Chromosomal Location of Human Ortholog: 5q23.1
Cellular Component: cytoplasm; plasma membrane
Molecular Function: peptide binding; zinc ion binding
Biological Process: cell-cell signaling; peptide catabolic process; proteolysis; regulation of blood pressure; signal transduction
An exopeptidase specific for larger hydrophobic amino acids (especially leucine), no cleavage occurs if the next residue is proline (PubMed:8444149).
Catalyzes the hydrolysis of a range of N-terminal amino acids.