Part:BBa_K2232022
RBS-csoS3-T1
The CsoSCA protein is from H. neapolitanus and its homologues in other α-carboxysome-producing autotrophs represent a novel CA class (ε) based on their unique primary structure. Their secondary and tertiary structures, however, strongly suggest that they constitute a variant of the β-class of these enzymes. The kinetic constants for rCsoSCA were determined with the colorimetric stopped-flow method of Khalifah , which allows one tofollow the progress of the hydration of CO2 and, under some conditions, the dehydration of bicarbonate. At pH 8.0, a kcat of 8.9x 104 s-1 was determined for the hydration of CO2 by rCsoSCA, with an apparent Km for CO2 of 3.2 mM.The kcat for the dehydration of HCO3- was measured to be 4.6x104 s-1 at pH 7.0, with an apparent Km of 9.3 mM for bicarbonate.
Sequence and Features
- 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 74
Illegal NgoMIV site found at 276 - 1000COMPATIBLE WITH RFC[1000]
References
- This part was created and improved by 2017 SZU-iGEM team basing on the original part BBa_K1465205.
- Heinhorst S, Williams E B, Cai F, et al. Characterization of the Carboxysomal Carbonic Anhydrase CsoSCA from Halothiobacillus neapolitanus[J]. Journal of Bacteriology, 2006, 188(23):8087.
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