L-Leucine-7-amido-4-methylcoumarin hydrochloride (Leu-AMC) is a fluorogenic peptidyl substrate for leucine aminopeptidase, an extracellular enzyme found abundantly in natural aquatic systems. This enzyme is one of the various enzymes used by bacteria for protein hydrolysis.
Application
L-Leucine-7-amido-4-methylcoumarin hydrochloride (Leu-AMC) as a substrate analog to determine leucine aminopeptidase activity
L-Leucine-7-amido-4-methylcoumarin hydrochloride has been used:
as a substrate in fluorescence-based soil assays[1]
to determine leucine aminopeptidase activity of both Plasmodium falciparum M1 (PfA-M1) and PfA-M17 enzymes[2]
Aminopeptidase N (APN/CD13) is a zinc-dependent ubiquitous transmembrane ectoenzyme that is widely present in different types of cells. APN is one of the most extensively studied metalloaminopeptidases as an anti-cancer target due to its significant role in the regulation of
Acanthamoeba are a free-living protozoan whose pathogenic strain can cause severe human diseases, such as granulomatous encephalitis and keratitis. As such, the pathogenic mechanism between humans and Acanthamoeba is still unknown. In our previous study, we identified the secreted Acanthamoeba
M17 leucine aminopeptidase of the human malaria parasite Plasmodium vivax
Lee JY, et al.
Molecular and Biochemical Parasitology, 170, 45-48 (2010)
Activity profiling of ectomycorrhiza communities in two forest soils using multiple enzymatic tests
Journal of environmental quality, 37(3), 972-976 (2008-05-06)
Enzyme catalyzed reactions are generally considered the rate-limiting step in organic matter degradation and may be significantly influenced by the structure and composition of plant communities. Changes in these rates have the potential to effect long-term peat accumulation and influence
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