Difference between revisions of "Team:Aix-Marseille/Basic Part"
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| − | + | ==Basic parts we have designed== | |
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| − | + | ===<b> <li> des A, lysine decarboxylase coding sequence (BbaK1951000)</b></li>=== | |
This DNA sequence codes Lysine descarboxylase (Streptomyces) is an enzyme from the lyase family that converts lysine to cadaverin. The enzyme realizes the carbonyl group of the lysin amino acid. There is cadeverin producing (1,5-diaminopentane), a primary diamine which alkaline environment. The lysine decarboxylase is an enzyme induced the synthesis of which is promoted by anaerobiosis and an acidic pH. | This DNA sequence codes Lysine descarboxylase (Streptomyces) is an enzyme from the lyase family that converts lysine to cadaverin. The enzyme realizes the carbonyl group of the lysin amino acid. There is cadeverin producing (1,5-diaminopentane), a primary diamine which alkaline environment. The lysine decarboxylase is an enzyme induced the synthesis of which is promoted by anaerobiosis and an acidic pH. | ||
In bacteriology, this enzyme is sought through the middle of Moeller lysine or medium lysine Taylor. This enzyme is also the first step in the production of desferrioxame B which is a siderophore. | In bacteriology, this enzyme is sought through the middle of Moeller lysine or medium lysine Taylor. This enzyme is also the first step in the production of desferrioxame B which is a siderophore. | ||
| − | + | ===des B, monooxygenase coding sequence (BbaK1951001)=== | |
This sequence codes 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. | This sequence codes 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. | ||
| − | + | === des C, acyl transferase coding sequence (BbaK1951002)=== | |
desC is the coding sequence of DesC which is an acyl transferase of the Desferrioxamine production pathway. It is the enzyme of the third step that transform N-hydroxycadaverin into N-acetyl N-hydroxucadaverine by an Acetyl-CoA dependent manner. | desC is the coding sequence of DesC which is an acyl transferase of the Desferrioxamine production pathway. It is the enzyme of the third step that transform N-hydroxycadaverin into N-acetyl N-hydroxucadaverine by an Acetyl-CoA dependent manner. | ||
| − | + | ===des D, desferrioxamine biosynthesis coding sequence (BbaK1951003)=== | |
This coding sequence codes 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 to transform N-acetyl N-hydroxycadaverine into Desferrioxamine B (by the transformation of 3a nucleoside triphosphate into 3a nucleoside 5'monophosphate-3-diphosphate). | This coding sequence codes 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 to transform N-acetyl N-hydroxycadaverine into Desferrioxamine B (by the transformation of 3a nucleoside triphosphate into 3a nucleoside 5'monophosphate-3-diphosphate). | ||
| − | + | === fliC E. coli, flagellin C coding sequence (BbaK1951005)=== | |
This coding sequence codes the Flagellin C (FliC) protein from Escherichia coli strain. FliC is the main protein constitutive of the flagelar filament and is involved to promote bacterial swimming. This sequence is conserved in many bacterial strains. It has been demonstrated that Flagellin C has the ability to adsorb precious metal such as Platinum, gold.. | This coding sequence codes the Flagellin C (FliC) protein from Escherichia coli strain. FliC is the main protein constitutive of the flagelar filament and is involved to promote bacterial swimming. This sequence is conserved in many bacterial strains. It has been demonstrated that Flagellin C has the ability to adsorb precious metal such as Platinum, gold.. | ||
| − | + | ===fliC Desulfovibrio, flagellin C coding sequence (BbaK1951006)=== | |
This coding sequence codes flagellin C which is a main protein involved for the extracellular flagellar establishment. Flagellar enables bacterial swimming. It has been shown that the flagellin structure from Desulfovibrio vulgaris strain Hildenborough can adsorb metallic nanoparticules as gold, Platinum.. | This coding sequence codes flagellin C which is a main protein involved for the extracellular flagellar establishment. Flagellar enables bacterial swimming. It has been shown that the flagellin structure from Desulfovibrio vulgaris strain Hildenborough can adsorb metallic nanoparticules as gold, Platinum.. | ||
| − | + | === CsgA, curlin coding sequence (BbaK1951007)=== | |
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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. Curli 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. Curli also mediate host cell adhesion and invasion, and they are potent inducers of the host inflammatory response. </ul> | 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. Curli 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. Curli also mediate host cell adhesion and invasion, and they are potent inducers of the host inflammatory response. </ul> | ||
