Difference between revisions of "Part:BBa K3051421"
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<partinfo>BBa_K3051421 short</partinfo> | <partinfo>BBa_K3051421 short</partinfo> | ||
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+ | <div align="center"><img height="85%" width="85%" src="https://2019.igem.org/wiki/images/b/b8/T--Warwick--2019-CLMP-DATA.png"></img></div> | ||
+ | <p><b>Figure 1. CLMP Lipase Activity Assay.</b> The protein expressed Lipase enzyme activity which was examined using a p-Nitrophenol octanoate assay.</p> | ||
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+ | 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 [https://2019.igem.org/Team:Warwick/Results 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. | ||
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+ | The enzyme showed 77% identity to Thermostable Lipase A <bbpart>BBa_K258006</bbpart>, 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. | ||
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+ | <div align="center"><img height="85%" width="85%" src="https://2019.igem.org/wiki/images/a/a1/T--Warwick--CMLP_3D_structure.png"></img></div> | ||
+ | <p><b>Figure 1. CLMP 3D Structure.</b> 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).</p> | ||
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<!-- Add more about the biology of this part here | <!-- Add more about the biology of this part here | ||
===Usage and Biology=== | ===Usage and Biology=== |
Revision as of 00:42, 22 October 2019
Compost Lipase
![](https://2019.igem.org/wiki/images/b/b8/T--Warwick--2019-CLMP-DATA.png)
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.
</div>
![](https://2019.igem.org/wiki/images/a/a1/T--Warwick--CMLP_3D_structure.png)
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]