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.
Aplicación
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]
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
Journal of hazardous materials, 411, 125121-125121 (2021-04-17)
Pharmaceutical industry effluents are complex and highly variable in time. Assessing the efficiency of a pharmaceutical industry wastewater treatment plant (WWTP) and the resulting decrease in effluent toxicity and ecological risk is thus not straightforward. We set up an original
Activity profiling of ectomycorrhiza communities in two forest soils using multiple enzymatic tests
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
Enzyme activity responses to nutrient loading in subtropical wetlands
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