Difference between revisions of "Part:BBa K5291034:Design"
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===Source=== | ===Source=== | ||
| − | + | CYPY96F: <i>Pseudomonas putida</i><br> | |
| − | + | <i>vgb</i>: <i>Vitreoscilla</i> sp.<br> | |
| + | pS, BiTerm: <i>Escherichia coli</i> | ||
===References=== | ===References=== | ||
| + | [1]Ramandeep, et al. (2001). "Vitreoscilla Hemoglobin: INTRACELLULAR LOCALIZATION AND BINDING TO MEMBRANES*." Journal of Biological Chemistry 276(27): 24781-24789.<br> | ||
| + | [2]Stevenson, J.-A., et al. (1996). "The Catalytic Oxidation of Linear and Branched Alkanes by Cytochrome P450cam." Journal of the American Chemical Society 118(50): 12846-12847.<br> | ||
| + | [3]Stevenson, J.-A., et al. (1996). "The Catalytic Oxidation of Linear and Branched Alkanes by Cytochrome P450cam." Journal of the American Chemical Society 118(50): 12846-12847. | ||
Latest revision as of 10:59, 2 October 2024
pAB1-cypY96F-vgb
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 604
Illegal BamHI site found at 684
Illegal BamHI site found at 1513 - 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 401
Illegal NgoMIV site found at 569 - 1000COMPATIBLE WITH RFC[1000]
Design Notes
The obligate aerobic bacterium, Vitreoscilla, synthesizes elevated quantities of a homodimeric hemoglobin (VHb) under hypoxic growth conditions. Expression of VHb in heterologous hosts often enhances growth and product formation. A role in facilitating oxygen transfer to the respiratory membranes is one explanation of its cellular function. Immunogold labeling of VHb in both Vitreoscilla and recombinant Escherichia coli bearing the VHb gene clearly indicated that VHb has a cytoplasmic (not periplasmic) localization and is concentrated near the periphery of the cytosolic face of the cell membrane. OmpA signal-peptide VHb fusions were transported into the periplasm in E. coli, but this did not confer any additional growth advantage. The interaction of VHb with respiratory membranes was also studied. The K d values for the binding of VHb to Vitreoscilla and E. coli cell membranes were ∼5–6 μm, a 4–8-fold higher affinity than those of horse myoglobin and hemoglobin for these same membranes. VHb stimulated the ubiquinol-1 oxidase activity of inverted Vitreoscilla membranes by 68%. The inclusion of Vitreoscilla cytochrome bo in proteoliposomes led to 2.4- and 6-fold increases in VHb binding affinity and binding site number, respectively, relative to control liposomes, suggesting a direct interaction between VHb and cytochrome bo.
Source
CYPY96F: Pseudomonas putida
vgb: Vitreoscilla sp.
pS, BiTerm: Escherichia coli
References
[1]Ramandeep, et al. (2001). "Vitreoscilla Hemoglobin: INTRACELLULAR LOCALIZATION AND BINDING TO MEMBRANES*." Journal of Biological Chemistry 276(27): 24781-24789.
[2]Stevenson, J.-A., et al. (1996). "The Catalytic Oxidation of Linear and Branched Alkanes by Cytochrome P450cam." Journal of the American Chemical Society 118(50): 12846-12847.
[3]Stevenson, J.-A., et al. (1996). "The Catalytic Oxidation of Linear and Branched Alkanes by Cytochrome P450cam." Journal of the American Chemical Society 118(50): 12846-12847.