- Cat. No.
- A22059
H-β-Ala-AMC TFA
H-β-Ala-AMC TFA is a substrate for aminopeptidase.
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Aminopeptidase inhibitors block enzymes that remove amino acids from the N-terminus of proteins and peptides. Methionine aminopeptidase 2 (MetAP2) cleaves the initiator methionine from many newly made proteins. In 1997 two groups showed that fumagillin and its analog TNP-470 bind MetAP2 covalently, which linked the enzyme to angiogenesis. Beloranib is a further fumagillin-derived MetAP2 inhibitor studied in models of obesity and metabolism. Ubenimex, also called bestatin, inhibits aminopeptidase N and leukotriene A4 hydrolase, and bestatin hydrochloride and bestatin methyl ester are related forms. Tosedostat is a cell-permeable prodrug that inhibits M1 family aminopeptidases. HFI-142 targets insulin-regulated aminopeptidase (IRAP), an enzyme studied in memory research.
H-β-Ala-AMC TFA is a substrate for aminopeptidase.
H-D-Ala-D-Ala-D-Ala-D-Ala-OH is a substrate for D-aminopeptidase, an enzyme that catalyzes the cleavage of D-amino acids from peptide chains. This compound is primarily utilized in biochemical studies to investigate D-aminopeptidase activity and its role in various physiological processes. It serves as a valuable tool for researchers studying peptide metabolism and the implications of D-amino acids in biological systems.
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Aeromonas proteolytica aminopeptidase is an enzyme that acts as an aminopeptidase, catalyzing the hydrolysis of peptide bonds at the N-terminal of substrates. Additionally, this enzyme exhibits esterase activity, demonstrating the ability to hydrolyze L-leucine ethyl ester (L-Leu-OEt) with a Km value of 700 µM. Its role in protein processing and peptide metabolism makes it a valuable tool for biochemical research and enzymatic studies.
Synonyms: L-Valine β-naphthylamide
H-Val-βNA (L-Valine β-naphthylamide) is a substrate for aminopeptidases and valine arylamidases. It is utilized in biochemical assays to study enzyme activity and substrate specificity. The reaction of H-Val-βNA with these enzymes generates a measurable product, facilitating the investigation of enzymatic processes related to amino acid metabolism and protein turnover.
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Lysine-2-naphthylamide is a substrate for dipeptidylaminopeptidase (DAP) enzymes. Its primary mechanism involves the cleavage of peptide bonds, facilitating the release of naphthylamide. This compound is useful in biochemical assays for studying DAP activity and can be employed in various research applications, including peptide hydrolysis and enzyme kinetics studies.
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