Aminopeptidases catalyze the cleavage of amino acids from the amino terminus of protein or peptide substrates.The majority of aminopeptidases have metallo-enzymes as their catalytic mechanism, but cysteine and serine peptidases are also a part of this class. Aminopeptidases are present in a variety of subcellular organelles, the cytoplasm, and membrane components throughout the animal and plant kingdoms. Numerous aminopeptidases carry out vital cellular tasks. These peptidases include many zinc metalloenzymes, but not all of them, and the transition-state analog bestatin inhibits them all. Some are monomeric, while others are collections of subunits with a relatively high mass (50 kDa).
The corresponding proteolytic regulatory enzymes aspartyl aminopeptidase (ASAP), aminopeptidase A (APA), aminopeptidase B (APB), aminopeptidase N (APN), and insulin-regulated aminopeptidase (IRAP) can be used to analyze the functional roles of the angiotensin peptides of the renin-angiotensin system (RAS) cascade. These enzyme processes result in active or inactive angiotensin peptides, which change the ratios between their bioactive forms and control a number of critical processes, including the regulation of cardiovascular functions, the regulation of body water, normal memory consolidation and retrieval, but also cell growth, differentiation, and apoptosis or the inflammatory response.
| Structure | Cat No. | Product Name | CAS No. | Product Description |
|---|---|---|---|---|
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V106533 | 2-(2′-Pyridyl)benzimidazole | 1137-68-4 | 2-(2'-Pyridyl)benzimidazole is a potential tridentate ligand that can form stable complexes with a variety of transition metal ions. |
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V106845 | 4-MDM | 834-14-0 | 4-MDM (4-methoxydiphenylmethane) is an orally available anti-inflammatory compound that selectively enhances the aminopeptidase activity of leukotriene A4 hydrolase (LTA4H). |
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V110235 | Aminopeptidase I, Streptomyces griseus | Streptomyces aminopeptidase I (EC 3.4.11.22) has broad substrate specificity and can remove N-terminal residues from most proteins, except when the penultimate residue is an imino acid. | |
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V110157 | Aminopeptidase M, Porcine | Porcine aminopeptidase M (EC 3.4.11.2) is a metalloproteinase that hydrolyzes almost all N-terminal amino acids of unsubstituted oligopeptides. | |
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V72984 | Aminopeptidase N Ligand (CD13) NGR peptide | 760947-20-4 | Aminopeptidase N Ligand (CD13) NGR peptide is a CD13-targeting peptide that serves as a carrier to mediate intracellular delivery. |
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V72986 | Aminopeptidase-IN-1 | 374102-08-6 | Aminopeptidase-IN-1 (compound 16o) is a potent insulin-regulated aminopeptidase (IRAP) inhibitor (antagonist) with Ki of 7.7 μM. |
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V87297 | Apstatin | 160470-73-5 | Apstatin is a potent aminopeptidase P (APP) inhibitor with Ki values of 2.6 and 0.64 µM for rat and human APP respectively. |
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V87296 | Bestatin methyl ester | 65322-89-6 | Bestatin methyl ester is a cell-permeable inhibitor of Zn2+-binding aminopeptidases. |
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V118429 | Cyanostatin B | 850131-23-6 | Cyanostatin B is a leucine aminopeptidase (LAP) inhibitor (IC50 = 12 ng/mL). |
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V72983 | EC33 | 232261-88-0 | EC33 is a selective aminopeptidase A (APA) inhibitor. |
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V104878 | ERAP1-IN-3 | ERAP1-IN-3 (Compound 13) is a potent endoplasmic reticulum aminopeptidase 1 (ERAP1) inhibitor with a pIC50 value of 8.6. | |
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V111220 | GSK235 | GSK235 is an orally administered, highly potent, selective allosteric endoplasmic reticulum aminopeptidase 1 (ERAP1) inhibitor with a pIC50 value of 8.45 for human ERAP1 and 7.59 for mouse ERAP1. | |
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V72988 | H-Leu-Trp-Met-Arg-OH | 67368-23-4 | H-Leu-Trp-Met-Arg-OH is a tetrapeptide. |
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V72985 | HD-Ala-D-Ala-D-Ala-D-Ala-OH | 926-78-3 | H-Ala-D-Ala-D-Ala-D-Ala-OH is a substrate of D-aminopeptidase. |
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V85031 | HFI-437 | 1110650-74-2 | |
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V87295 | IRAP-IN-1 | IRAP-IN-1 (compound 3) is a potent and selective insulin regulated aminopeptidase (IRAP) inhibitor with IC50 of 157 nM. | |
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V86059 | JNJ-40929837 | 1191044-42-4 | |
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V109877 | Leucine Aminopeptidase (microsomal), Porcine | Leucine aminopeptidase (microsomal) and porcine (EC 3.4.11.2) are enzymes that preferentially catalyze the hydrolysis of N-terminal leucine residues in peptides and proteins. | |
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V110229 | Leucine Aminopeptidase, Porcine | Porcine leucine aminopeptidase (EC 3.4.11.1) is a proteolytic enzyme that hydrolyzes peptide bonds adjacent to free amino groups. | |
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V85897 | LTA4H-IN-2 | 2851480-52-7 |