View source for Part:BBa C0160

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<partinfo>BBa_C0160 short</partinfo>

same as [[Part:BBa_C0060]] except no [[Help:Tag|LVA tag]] 

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===Usage and Biology===

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<span class='h3bb'>Sequence and Features</span>
<partinfo>BBa_C0160 SequenceAndFeatures</partinfo>
===Characterization done by ETH Zurich 2015===
Check the characterization done by ETH Zurich 2015 iGEM team in the experience page. 



==Functional Parameters: Austin_UTexas==
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<partinfo>BBa_C0160 parameters</partinfo>
<h3><center>Burden Imposed by this Part:</center></h3>
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<center><img src = "https://static.igem.org/mediawiki/parts/f/fa/T--Austin_Utexas--no_burden_icon.png" style = "width:160px;height:120px"></center>
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<figcaption><center><b>Burden Value: 0.8 ± 5.7% </b></center></figcaption>
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<p> Burden is the percent reduction in the growth rate of <i>E. coli</i> cells transformed with a plasmid containing this BioBrick (± values are 95% confidence limits). This BioBrick did not exhibit a burden that was significantly greater than zero (i.e., it appears to have little to no impact on growth). Therefore, users can depend on this part to remain stable for many bacterial cell divisions and in large culture volumes. Refer to any one of the 
<a href="https://parts.igem.org/Part:BBa_K3174002">BBa_K3174002</a> - <a href="https://parts.igem.org/Part:BBa_K3174007">BBa_K3174007</a> pages for more information on the methods, an explanation of the sources of burden,  and other conclusions from a large-scale measurement project conducted by the <a href="http://2019.igem.org/Team:Austin_UTexas">2019 Austin_UTexas team</a>.</p> 
<p>This functional parameter was added by the <a href="https://2020.igem.org/Team:Austin_UTexas/Contribution">2020 Austin_UTexas team.</a></p>
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==Kinetic Parameters and Enzyme Activity in different conditions: WHU-China 2020==
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<partinfo>BBa_C0160 parameters</partinfo>
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<figcaption><center><b>Fig1: Kinetic parameters of AHL-lactonase against different kinds of AHLs. a: The data are means from triplicate experiments. b: ND indicates not determined due to poor solubility of the substrate in phosphate buffer. c: 3-Hydroxylbutanoyl L-homoserine lactone. </b></center></figcaption>
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<center><img src = "https://2020.igem.org/wiki/images/8/87/T--WHU-China--parts2-2.png" style = "width:320px;height:240px"></center>
<center><img src = "https://2020.igem.org/wiki/images/7/7c/T--WHU-China--parts3-3.png" style = "width:320px;height:240px"></center>
<center><img src = "https://2020.igem.org/wiki/images/a/ab/T--WHU-China--parts4-4.png" style = "width:320px;height:240px"></center>
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<figcaption><center><b>Fig2: Effect of pH (A), temperature (B), and metal ions (C) on aiiA activity. </b></center></figcaption>
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<p> The Michaelis constant (Km) and kcat value of an enzyme have always been important as they show the efficiency of the enzyme towards its substrate. So they are frequently used to decide whether the enzyme is “good” or not according to specific situation. And what is also important is the conditions influencing the enzyme activity, such as temperature, PH, metal ions and so on. Here we add the data we obtain from literature[1] about aiiA gene, including kinetic parameters towards different substrates and its activity changes versus different conditions. Further users can conduct their experiments or models based on these data then.</p> 
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<p>Reference: </p>
<p>1.Wang L H, Weng L X, et al., Specificity and Enzyme Kinetics of the Quorum-quenching N-Acyl Homoserine Lactone Lactonase (AHL-lactonase) [J]. Journal of Biological Chemistry, 2004, 279(14):13645-51. </P>