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Team:Cambridge/References/ProjectBioluminescence/Recovery
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| - | {{:Team:Cambridge/Templates/ | + | {{:Team:Cambridge/Templates/headerMinimalprototype}} |
| - | {{:Team:Cambridge/ | + | {{:Team:Cambridge/Templates/RefBar}} |
| + | {{:Team:Cambridge/Templates/headerbar|colour=#96d446|title=Bioluminescence: Luciferin Recovery}} | ||
==LRE== | ==LRE== | ||
*[http://www.ncbi.nlm.nih.gov/pubmed/11457857 Paper on isolation of A-LRE] | *[http://www.ncbi.nlm.nih.gov/pubmed/11457857 Paper on isolation of A-LRE] | ||
*[http://www.ncbi.nlm.nih.gov/nucleotide/14331151?report=genbank&log$=nucltop&blast_rank=1&RID=4EUAXMJW01R A-LRE (P.pyralis) Sequence] | *[http://www.ncbi.nlm.nih.gov/nucleotide/14331151?report=genbank&log$=nucltop&blast_rank=1&RID=4EUAXMJW01R A-LRE (P.pyralis) Sequence] | ||
| + | * [http://www.ncbi.nlm.nih.gov/nuccore/AB072448.1 G-LRE (L. cruciata) Sequence] | ||
*[http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TG1-506W6R3-1&_user=1495569&_coverDate=06%2F01%2F2010&_rdoc=1&_fmt=high&_orig=search&_sort=d&_docanchor=&view=c&_searchStrId=1409765644&_rerunOrigin=google&_acct=C000053194&_version=1&_urlVersion=0&_userid=1495569&md5=eec2ba99cb96a1e286d7ce14e8449b2a RACE-based amplification of cDNA and expression of a luciferin-regenerating enzyme (LRE): An attempt towards persistent bioluminescent signal] | *[http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TG1-506W6R3-1&_user=1495569&_coverDate=06%2F01%2F2010&_rdoc=1&_fmt=high&_orig=search&_sort=d&_docanchor=&view=c&_searchStrId=1409765644&_rerunOrigin=google&_acct=C000053194&_version=1&_urlVersion=0&_userid=1495569&md5=eec2ba99cb96a1e286d7ce14e8449b2a RACE-based amplification of cDNA and expression of a luciferin-regenerating enzyme (LRE): An attempt towards persistent bioluminescent signal] | ||
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*[http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B73G9-47G3TGV-1S9-1&_cdi=11521&_user=1495569&_pii=0006300258903810&_orig=search&_coverDate=12%2F31%2F1958&_sk=999729999&view=c&wchp=dGLbVzz-zSkWA&md5=4420b38ef24aba8ca23e0b8ce2b3a953&ie=/sdarticle.pdf CoA is required to remove oxyluciferin from luciferase] | *[http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B73G9-47G3TGV-1S9-1&_cdi=11521&_user=1495569&_pii=0006300258903810&_orig=search&_coverDate=12%2F31%2F1958&_sk=999729999&view=c&wchp=dGLbVzz-zSkWA&md5=4420b38ef24aba8ca23e0b8ce2b3a953&ie=/sdarticle.pdf CoA is required to remove oxyluciferin from luciferase] | ||
| - | {{:Team:Cambridge/Templates/ | + | ==D-Cysteine== |
| + | E. coli growth is impaired in the presence of micromolar amounts of D-cysteine. [http://www.ncbi.nlm.nih.gov/pubmed/11527960 Soutourina et al.] found that E. coli contain a D-cysteine desulfhydrase which can convert D-cysteine into pyruvate, H2S, and NH3. Overexpression of yedO (the E. coli gene encoding D-cysteine desulfydrase activity) protected E. coli against D-cysteine, whereas its inactivation rendered E. coli hypersensitive. With yedO intact, E. coli growth was improved by addition of D-cysteine as the sole sulfur source. | ||
| + | Similar to L-cysteine, D-cysteine exerts toxicity through inhibition of threonine deaminase, a key enzyme of the isoleucine, leucine, and valine biosynthesis pathway. Growth protection against D-cysteine in minimal medium was conferred by simultaneous addition of isoleucine, leucine and valine. L-aspartate was also observed to exert a protective effect against D-cysteine toxicity. | ||
| + | <html> | ||
| + | </div> | ||
| + | </html> | ||
| + | {{:Team:Cambridge/Templates/footerMinimal}} | ||
Latest revision as of 12:18, 7 October 2010
Link dumps: Bioluminescence |
Firefly luciferases|
Lucferin recovery|
Light output|
Experiments|
Modelling
Bioluminescence: Luciferin Recovery
LRE
- [http://www.ncbi.nlm.nih.gov/pubmed/11457857 Paper on isolation of A-LRE]
- [http://www.ncbi.nlm.nih.gov/nucleotide/14331151?report=genbank&log$=nucltop&blast_rank=1&RID=4EUAXMJW01R A-LRE (P.pyralis) Sequence]
- [http://www.ncbi.nlm.nih.gov/nuccore/AB072448.1 G-LRE (L. cruciata) Sequence]
- [http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TG1-506W6R3-1&_user=1495569&_coverDate=06%2F01%2F2010&_rdoc=1&_fmt=high&_orig=search&_sort=d&_docanchor=&view=c&_searchStrId=1409765644&_rerunOrigin=google&_acct=C000053194&_version=1&_urlVersion=0&_userid=1495569&md5=eec2ba99cb96a1e286d7ce14e8449b2a RACE-based amplification of cDNA and expression of a luciferin-regenerating enzyme (LRE): An attempt towards persistent bioluminescent signal]
CoA
- [http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B73G9-47G3TGV-1S9-1&_cdi=11521&_user=1495569&_pii=0006300258903810&_orig=search&_coverDate=12%2F31%2F1958&_sk=999729999&view=c&wchp=dGLbVzz-zSkWA&md5=4420b38ef24aba8ca23e0b8ce2b3a953&ie=/sdarticle.pdf CoA is required to remove oxyluciferin from luciferase]
D-Cysteine
E. coli growth is impaired in the presence of micromolar amounts of D-cysteine. [http://www.ncbi.nlm.nih.gov/pubmed/11527960 Soutourina et al.] found that E. coli contain a D-cysteine desulfhydrase which can convert D-cysteine into pyruvate, H2S, and NH3. Overexpression of yedO (the E. coli gene encoding D-cysteine desulfydrase activity) protected E. coli against D-cysteine, whereas its inactivation rendered E. coli hypersensitive. With yedO intact, E. coli growth was improved by addition of D-cysteine as the sole sulfur source. Similar to L-cysteine, D-cysteine exerts toxicity through inhibition of threonine deaminase, a key enzyme of the isoleucine, leucine, and valine biosynthesis pathway. Growth protection against D-cysteine in minimal medium was conferred by simultaneous addition of isoleucine, leucine and valine. L-aspartate was also observed to exert a protective effect against D-cysteine toxicity.
