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 be break down the ester bond between p nitrophenol and octanoic acid using a p nitrophenol octanoate assay and because of this its main role appears to be as a lipase (an enzyme that breaks down triglycerols).  
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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)
  
 
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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:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]