Difference between revisions of "Part:BBa K3051421"
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<partinfo>BBa_K3051421 short</partinfo> | <partinfo>BBa_K3051421 short</partinfo> | ||
− | This is a lipase found in a metagenomics search of a compost done by the University of Gottingen. It was found to | + | This is a lipase found in a metagenomics search of a compost done by the University of Gottingen. It was found to break down the ester bond of p nitrophenol octanoate. It has a similarity (77% identity) to Thermostable Lipase A (BBa_K258006), and we believe it has the same function. Its conserved domains include a hydrolase site and an RTX toxin related Ca2+ binding site, which may make it sensitive to Ca ions or act as a cofactor. |
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+ | It has a kDa of 64.6 and an estimated molar extinction coefficient of 75290 M-1cm-1 (calculated using ProtoPram ExPaSy tool). It has the following 3D structure (calculated using Phyre 2) | ||
<!-- Add more about the biology of this part here | <!-- Add more about the biology of this part here |
Revision as of 20:42, 16 October 2019
Compost Lipase
This is a lipase found in a metagenomics search of a compost done by the University of Gottingen. It was found to break down the ester bond of p nitrophenol octanoate. It has a similarity (77% identity) to Thermostable Lipase A (BBa_K258006), and we believe it has the same function. Its conserved domains include a hydrolase site and an RTX toxin related Ca2+ binding site, which may make it sensitive to Ca ions or act as a cofactor.
It has a kDa of 64.6 and an estimated molar extinction coefficient of 75290 M-1cm-1 (calculated using ProtoPram ExPaSy tool). It has the following 3D structure (calculated using Phyre 2)
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Unknown
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]