Difference between revisions of "Part:BBa K5108004"
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<p><a href="https://www.uniprot.org/uniprotkb/P83772/entry" target="blank">CrnA</a> is an enzyme that catalyzes the degradation of creatinine into creatine in <i>Pseudomonas putida</i>. | <p><a href="https://www.uniprot.org/uniprotkb/P83772/entry" target="blank">CrnA</a> is an enzyme that catalyzes the degradation of creatinine into creatine in <i>Pseudomonas putida</i>. | ||
− | In the context of our project, the gene encoding this enzyme (<i>crnA</i>) was synthesized in an operon together with the gene for creatine degradation. You can find more information about construct and our results in <a href="https://parts.igem.org/Part:BBa_K5108009" target="blank">BBa_K5108009</a> | + | In the context of our project, the gene encoding this enzyme (<i>crnA</i>) was synthesized in an operon together with the gene for creatine degradation. You can find more information about construct and our results in <a href="https://parts.igem.org/Part:BBa_K5108009" target="blank">BBa_K5108009.</a> |
</p> | </p> | ||
Revision as of 13:47, 29 September 2024
Creatinine amidohydrolase form Pseudomonas putida
- Contents
- Usage and Biology
- References
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 61
Illegal NgoMIV site found at 663 - 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI site found at 199
Illegal BsaI.rc site found at 547
Usage and Biology
CrnA is an enzyme that catalyzes the degradation of creatinine into creatine in Pseudomonas putida. In the context of our project, the gene encoding this enzyme (crnA) was synthesized in an operon together with the gene for creatine degradation. You can find more information about construct and our results in BBa_K5108009.
References
- UniProt. (s. d.). https://www.uniprot.org/uniprotkb/P83772/entry
- Tsuru, D., Oka, I., & Yoshimoto, T. (1976c). Creatinine Decomposing Enzymes inPseudomonas putida. Agricultural And Biological Chemistry, 40(5), 1011‑1018. https://doi.org/10.1080/00021369.1976.10862151