Difference between revisions of "Part:BBa K4893001:Design"
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===Design Notes=== | ===Design Notes=== | ||
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+ | The replacement of Ser231 to Lys resulted in an increase in thermal stability.[1] | ||
===Source=== | ===Source=== | ||
− | + | Acinetobacter calcoaceticus | |
===References=== | ===References=== | ||
+ | |||
+ | [1] Sode K, Ootera T, Shirahane M, Witarto AB, Igarashi S, Yoshida H. Increasing the thermal stability of the water-soluble pyrroloquinoline quinone glucose dehydrogenase by single amino acid replacement. Enzyme Microb Technol. 2000 Apr 1;26(7):491-496. doi: 10.1016/s0141-0229(99)00196-9. PMID: 10771051. | ||
+ | |||
+ | [2] Igarashi S, Sode K. Stabilization of quaternary structure of water-soluble quinoprotein glucose dehydrogenase. Mol Biotechnol. 2003 Jun;24(2):97-104. doi: 10.1385/MB:24:2:97. PMID: 12746550. |
Latest revision as of 05:36, 12 October 2023
Pyrroloquinoline Quinone Glucose Dehydrogenase
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal XhoI site found at 450
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Design Notes
The replacement of Ser231 to Lys resulted in an increase in thermal stability.[1]
Source
Acinetobacter calcoaceticus
References
[1] Sode K, Ootera T, Shirahane M, Witarto AB, Igarashi S, Yoshida H. Increasing the thermal stability of the water-soluble pyrroloquinoline quinone glucose dehydrogenase by single amino acid replacement. Enzyme Microb Technol. 2000 Apr 1;26(7):491-496. doi: 10.1016/s0141-0229(99)00196-9. PMID: 10771051.
[2] Igarashi S, Sode K. Stabilization of quaternary structure of water-soluble quinoprotein glucose dehydrogenase. Mol Biotechnol. 2003 Jun;24(2):97-104. doi: 10.1385/MB:24:2:97. PMID: 12746550.