Part:BBa_K325219

Input: L-Arabinose Output: Light

pBad/araC I0500 Luciferase/LRE K325210

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Description
This part generates a red-mutant of the luciferase from the Japanese firefly (L.cruciata) as well as the luciferin regenerating enzyme (LRE). It is under the control of an Arabinose induced promoter. D-Luciferin has to be added to obtain light output.

Performance

Experiment1	Characteristic1	Value1
Transfer Function	Maximum Output	6.6 PoPS cell-1
	Hill coefficient	1.6
	Switch Point	1.5E-9 M 3OC6HSL, exogenous
Response time:	<1 min
Input compatibility	Strong response to	3OC6HSL, C6HSL , C7HSL, 3OC8HSL, C8HSL
	Weak response to	C4HSL, C10HSL, C12HSL
Stability	Genetic Stability (Low/High Input)	>92/>56 generations
	Performance Stability (Low/High Input)	>92/>56 generations
Demand	Internal Demand (Low/High Input)	Not measured
	Transcriptional output demand: (Low/High Input) Nt = length of downstream transcript in nucleotides	(0/6xNt) nucleotides cell-1 s-1
		(0/1.5E-1xNt) RNAP cell-1
	Growth Rate (Low/High Input)	54/59 min Doubling time

¹Measured by the [http://2010.igem.org/Team:Cambridge Cambridge iGEM team 2010]

Compatibility
Chassis: Device has been shown to work in Top 10 (Invitrogen)
Plasmids: Device has been shown to work on pSB1C3

References
[http://www.ncbi.nlm.nih.gov/pubmed/18949818 [1]:] S.M. Marques and J.C.G. Esteves da Silva, (2009) Firefly Bioluminescence: A Mechanistic Approach of Luciferase Catalyzed Reactions,Life 61, 6-17.

[http://www.nature.com/nature/journal/v440/n7082/abs/nature04542.html [2]:] T. Nakatsu et al. (2006) Structural Basis for the spectral difference in luciferase bioluminescence, Nature 440(16), 372-376.

[http://www.ncbi.nlm.nih.gov/pubmed/11457857 [3]:] K. Gomi and N. Kajiyama, (2001) Oxyluciferin, a Luminescence Product of Firefly Luciferase, Is Enzymatically Regenerated into Luciferin, The Journal of Biological Chemistry, 276(39), 36508-36513.