Difference between revisions of "Team:Aix-Marseille/Basic Part"

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{{:Team:Aix-Marseille/Template-Top|Basic Part}}
 
{{:Team:Aix-Marseille/Template-Top|Basic Part}}
  
You will find on this page the basic parts which have been designed by our team. For further details, you can also go on [http://www.parts.igem.org parts page] and have a look to the corresponding BioBrick's page.
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You will find on this page the basic parts which have been designed by our team. For further details, you can also go on [http://parts.igem.org/Main_Page parts page] and have a look to the corresponding BioBrick's page.
  
 
==Mobilisation by a siderophore==  
 
==Mobilisation by a siderophore==  
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===desA, lysine decarboxylase coding sequence [http://parts.igem.org/Part:BBa_K1951000 BBa_K1951000]===
 
===desA, lysine decarboxylase coding sequence [http://parts.igem.org/Part:BBa_K1951000 BBa_K1951000]===
  
This DNA sequence codes a [http://metacyc.org/gene?orgid=META&id=SCO2782 Lysine decarboxylase] (''Streptomyces'') which is an enzyme from the lyase family that converts lysine into cadaverine. The enzyme releases the carbonyl group of the lysin amino acid. Cadaverine (or 1,5-diaminopentane) is a primary diamine which renders the medium alkaline. The lysine decarboxylase is an enzyme whose synthesis is promoted by anaerobiosis and an acidic pH.  
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This DNA sequence codes a [http://metacyc.org/gene?orgid=META&id=SCO2782 Lysine decarboxylase] (''Streptomyces coelicolor'') which is an enzyme from the lyase family that converts lysine into cadaverine. The enzyme releases the carbonyl group of the lysin amino acid. Cadaverine (or 1,5-diaminopentane) is a primary diamine which renders the medium alkaline. The lysine decarboxylase is an enzyme whose synthesis is promoted by anaerobiosis and an acidic pH.  
 
This enzyme is also the first step in the production of desferrioxame B which is a siderophore.
 
This enzyme is also the first step in the production of desferrioxame B which is a siderophore.
  
 
===desB, monooxygenase coding sequence [http://parts.igem.org/Part:BBa_K1951001 BBa_K1951001]===
 
===desB, monooxygenase coding sequence [http://parts.igem.org/Part:BBa_K1951001 BBa_K1951001]===
  
This sequence codes a [http://metacyc.org/gene?orgid=META&id=SCO2783-MONOMER monooxygenase] which is an enzyme that incorporate one hydroxyl group into substrates in many metabolic pathways. In this reaction, the two atoms of dioxygen are reduced to one hydroxyl and one H2O molecule by the concomitant oxidation of NAD(P)H. It is also the second step in the production of Desferrioxamine B in ''Streptomyces'', allowing the transformation of cadeverine into N-hydroxycadaverine.
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This sequence codes a [http://metacyc.org/gene?orgid=META&id=SCO2783-MONOMER monooxygenase] which is an enzyme that incorporates one hydroxyl group into substrates in many metabolic pathways. In this reaction, the two atoms of dioxygen are reduced to one hydroxyl and one H2O molecule by the concomitant oxidation of NAD(P)H. It is also the second step in the production of Desferrioxamine B in ''Streptomyces'', allowing the transformation of cadeverine into N-hydroxycadaverine.
  
 
===desC, acyl transferase coding sequence [http://parts.igem.org/Part:BBa_K1951002 BBa_K1951002]===
 
===desC, acyl transferase coding sequence [http://parts.igem.org/Part:BBa_K1951002 BBa_K1951002]===
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===desD, Desferrioxamine biosynthesis coding sequence [http://parts.igem.org/Part:BBa_K1951003 BBa_K1951003]===
 
===desD, Desferrioxamine biosynthesis coding sequence [http://parts.igem.org/Part:BBa_K1951003 BBa_K1951003]===
  
This coding sequence codes [http://metacyc.org/gene?orgid=META&id=SCO2785-MONOMER DesD] of ''Streptomyces coelicolor'', which is the last protein involved in the metabolic pathway of Desferrioxamine B. This enzyme is called Desferrioxamine biosynthesis protein or DesD and allows the transformation of N-acetyl N-hydroxycadaverine into Desferrioxamine B (by the transformation of 3 nucleoside triphosphate into 3 nucleoside 5'monophosphate-3-diphosphate).
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This coding sequence codes [http://metacyc.org/gene?orgid=META&id=SCO2785-MONOMER DesD] of ''Streptomyces coelicolor'', which is the last protein involved in the metabolic pathway of Desferrioxamine B. This enzyme is called Desferrioxamine biosynthesis protein or DesD and allows the conversion of N-acetyl N-hydroxycadaverine into Desferrioxamine B (by the transformation of 3 nucleoside triphosphate into 3 nucleoside 5'monophosphate-3-diphosphate).
  
 
==Biosorption==
 
==Biosorption==
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===CsgA, curlin coding sequence  [http://parts.igem.org/Part:BBa_K1951007 BBa_K1951007]===
 
===CsgA, curlin coding sequence  [http://parts.igem.org/Part:BBa_K1951007 BBa_K1951007]===
  
[http://ecocyc.org/gene?orgid=ECOLI&id=EG11489-MONOMER CsgA] is the major and structural subunit of the curli fimbriae. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli are the major proteinaceous component of a complex extracellular matrix produced by many ''Enterobacteriaceae''. They were first discovered in the late 1980s on ''Escherichia coli'' strains that caused bovine mastitis, and have since been implicated in many physiological and pathogenic processes of ''E. coli'' and ''Salmonella'' spp. Curli fibers are involved in adhesion to surfaces, cell aggregation, and biofilm formation. They also mediate host cell adhesion and invasion, and they are potent inducers of the host inflammatory response. It has been shown that amyloid proteins, like curli, can bind some metals <ref name="metal_adhesion">[http://www.nature.com/nnano/journal/v11/n4/full/nnano.2015.310.html Sreenath Bolisetty and Raffaele Mezzenga 2016, Nature Nanotechnology]</ref> and thats why we wanted to use it in our project.
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[http://ecocyc.org/gene?orgid=ECOLI&id=EG11489-MONOMER CsgA] is the major and structural subunit of the curli fimbriae. Curli fibers are involved in adhesion to surfaces, cell aggregation, and biofilm formation <ref name="Curli">[https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2838481/ Michelle M. Barnhart and Matthew R. Chapman 2010, Annual Review of Microbiology]</ref>. It has been shown that amyloid proteins, like curli, can bind some metals <ref name="metal_adhesion">[http://www.nature.com/nnano/journal/v11/n4/full/nnano.2015.310.html Sreenath Bolisetty and Raffaele Mezzenga 2016, Nature Nanotechnology]</ref> and thats why we wanted to use it in our project.
  
 
<references/>
 
<references/>
  
 
{{:Team:Aix-Marseille/Template-Footer}}
 
{{:Team:Aix-Marseille/Template-Footer}}

Latest revision as of 23:29, 19 October 2016