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Aminopeptidase

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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Aminopeptidase B

Also known as Aminopeptidase B (AP-B) (Arginine aminopeptidase) (Arginyl aminopeptidase).
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 3.4.11.6; 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

Aminopeptidase E

Can hydrolyze internal peptide bonds in Met-enkephalin and bradykinin; however, hydrolysis of alpha-, beta-, and kappa-caseins is not detected.

Aminopeptidase Ey

Broad specificity aminopeptidase. Degrades a variety of peptides possessing various N-terminal amino acids including hydrophobic, basic and acidic amino acids. Preferentially hydrolyzes small peptides consisting of 4 or 5 amino acids. Hydrolyzes the N-terminal Xaa-Pro bonds in the chicken brain peptide Leu-Pro-Leu-Arg-PheNH2, the substance P fragment Arg-Pro-Lys-Pro and the bradykinin fragment Arg-Pro-Pro-Gly-Phe. Hydrolyzes the N-formylated peptides fMet-Leu-Phe, fMet-Ala-Gly-Ser-Glu and fMet-Nle-Leu-Phe-Nle-Tyr-Lys, but does not hydrolyze peptides with acetylation or pyroglutamic acid at N-terminus. Does not hydrolyze large peptides such as complete substance P, bradykinin or schistoFLRFamide.

Aminopeptidase G

Hydrolyzes preferentially the N-terminal glycine and can also hydrolyze other amino acids which are used by PepN but is unable to hydrolyze basic amino acids.

Aminopeptidase N

Also known as Aminopeptidase N (Alanine aminopeptidase) (Lysyl aminopeptidase) (Lys-AP).
Aminopeptidase with broad substrate specificity to several peptides.

Aminopeptidase O

Also known as Aminopeptidase O (AP-O).
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 ().

Aminopeptidase PepS

Exhibits a high specificity towards peptides possessing arginine or aromatic amino acids at the N-terminus. Could be involved both in bacterial growth by supplying amino acids.

Aminopeptidase Q

Also known as Aminopeptidase Q (AP-Q) (APQ) (CHL2 antigen) (Laeverin).
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

Aminopeptidase S

Also known as Aminopeptidase S (API) (SGAP).
An exopeptidase specific for larger hydrophobic amino acids (especially leucine), no cleavage occurs if the next residue is proline (PubMed:8444149).

Aminopeptidase YpdE

Has a broad aminopeptidase activity on non-blocked peptides by progressively cleaving amino acids off the peptide substrate. Aminopeptidase activity stops at the residue before the first proline in the peptide. Cannot cleave when proline is the first N-terminal residue.

Aminopeptidase YpdF

Hydrolyzes the N-terminal methionine when the next amino acid is alanine, proline or serine. The substrate preference for methionyl aminopeptidase activity is Pro > Ala > Ser. Also able to hydrolyze the Xaa-Pro peptide bond when the first amino acid is alanine, asparagine or methionine.

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