Part:BBa_K3051421
Compost Lipase
Figure 1. CLMP Lipase Activity Assay. The protein expressed Lipase enzyme activity which was examined using a p-Nitrophenol octanoate assay.
The lipase was found in a metagenomics search of a compost performed by the University of Gottingen. The lipase enzyme was tested and characterized using a p nitrophenol octanoate assay. The enzyme activity was determined by measuring change in light absorbance at a wavelength of 400nm, which directly correlated to the concentration of p-Nitrophenol (pNP), caused by lipolysis of p-Nitrophenol octanoate (pNPO) substrate. The data from the pNPO lipolysis assay defined the enzyme activity.
The enzyme showed 77% identity to Thermostable Lipase A BBa_K258006, and likely conserves a similar function. The conserved domains include a hydrolase site and an RTX toxin related Ca2+ binding site - which could either cause sensitivity to Calcium ions or Calcium ions could act as a cofactor.
Figure 1. CLMP 3D Structure. The protein has a kDa of 64.6 and an estimated molar extinction coefficient of 75290 M-1cm-1 (calculated using ProtoPram ExPaSy tool); the following 3D structure (calculated using Phyre 2).
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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