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Team:Missouri Miners/Parts
From 2014.igem.org
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<h1>Parts</h1> | <h1>Parts</h1> | ||
| - | <p><a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K1370000">Part BBa_K1370000</a> is the isolated <i>hmp</i> gene from <i>Escherichia Coli</i>, and produces a protein, dihydropteridine reductase, which catalyzes the reduction of nitric oxide to nitrate. Synthesis of its product is elevated in response to nitrite or nitric oxide through transcriptional regulation.</p> | + | <p><a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K1370000" style="color:blue">Part BBa_K1370000</a> is the isolated <i>hmp</i> gene from <i>Escherichia Coli</i>, and produces a protein, dihydropteridine reductase, which catalyzes the reduction of nitric oxide to nitrate. Synthesis of its product is elevated in response to nitrite or nitric oxide through transcriptional regulation.</p> |
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<div id="references"> | <div id="references"> | ||
Latest revision as of 04:35, 17 October 2014
Parts
Part BBa_K1370000 is the isolated hmp gene from Escherichia Coli, and produces a protein, dihydropteridine reductase, which catalyzes the reduction of nitric oxide to nitrate. Synthesis of its product is elevated in response to nitrite or nitric oxide through transcriptional regulation.
Cruz-Ramos, H., Crack, J., Wu, G., Hughes, M. N., Scott, C., Thomson, A. J., ... & Poole, R. K. (2002). NO sensing by FNR: regulation of the Escherichia coli NO-detoxifying flavohaemoglobin, Hmp. The EMBO journal, 21(13), 3235-3244.
Gardner, P. R., Gardner, A. M., Martin, L. A., & Salzman, A. L. (1998). Nitric oxide dioxygenase: an enzymic function for flavohemoglobin. Proceedings of the National Academy of Sciences, 95(18), 10378-10383.
Hausladen, A., Gow, A. J., & Stamler, J. S. (1998). Nitrosative stress: metabolic pathway involving the flavohemoglobin. Proceedings of the National Academy of Sciences, 95(24), 14100-14105.
Hmp fused nitric oxide dioxygenase/dihydropteridine reductase 2. (n.d.). Retrieved from http://www.ncbi.nlm.nih.gov/gene/947018
