Difference between revisions of "Part:BBa K3771041"
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<br>L-cysteine dioxygenase (CDO1) is an enzyme that weighs 23 kDa. CDO1 functions in the L-cysteine sulfinic acid taurine biosynthesis pathway, converting L-cysteine to L-cysteine sulfinic acid. [1]<br> | <br>L-cysteine dioxygenase (CDO1) is an enzyme that weighs 23 kDa. CDO1 functions in the L-cysteine sulfinic acid taurine biosynthesis pathway, converting L-cysteine to L-cysteine sulfinic acid. [1]<br> | ||
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| − | <img src="https://2021.igem.org/wiki/images/c/c9/T--NCKU_Tainan--taurine_pathway_1.png" style="width: | + | <img src="https://2021.igem.org/wiki/images/c/c9/T--NCKU_Tainan--taurine_pathway_1.png" style="width:50%;"></html> |
<br>CDO1 is part of the L-cysteine sulfinic acid pathway, one of three possible taurine synthesis pathways. CDO1 oxidizes L-cysteine naturally found in the intestine into L-cysteine sulfinic acid, which is later converted to taurine by CSAD [1].<br> | <br>CDO1 is part of the L-cysteine sulfinic acid pathway, one of three possible taurine synthesis pathways. CDO1 oxidizes L-cysteine naturally found in the intestine into L-cysteine sulfinic acid, which is later converted to taurine by CSAD [1].<br> | ||
Revision as of 19:20, 18 October 2021
CDO1-6xHis
Description
L-cysteine dioxygenase (CDO1) is an enzyme that weighs 23 kDa. CDO1 functions in the L-cysteine sulfinic acid taurine biosynthesis pathway, converting L-cysteine to L-cysteine sulfinic acid. [1]
CDO1 is part of the L-cysteine sulfinic acid pathway, one of three possible taurine synthesis pathways. CDO1 oxidizes L-cysteine naturally found in the intestine into L-cysteine sulfinic acid, which is later converted to taurine by CSAD [1].
Usage
CDO1 was used in in vivo testing of taurine production. The sequence for CDO1 enzyme and trc promoter were ligated and transformed into E. coli to calculate taurine production using high-performance liquid chromatography (HPLC). A 6xHis-tag is added to the C-terminal of the CoaBC protein, allowing for confirmation of JJU10 expression by western blot using the anti-6xHis antibody.
Characterization
The CDO1 fragment was synthesized by IDT and amplified by PCR. Agarose gel electrophoresis result is shown in Fig. 2.
The CDO1 fragment was synthesized by IDT and amplified by PCR. Agarose gel electrophoresis result is shown in Fig. 2.
References
Joo Y-C, Ko YJ, You SK, et al. Creating a New Pathway in Corynebacterium glutamicum for the Production of Taurine as a Food Additive. Journal of Agricultural and Food Chemistry. 2018;66(51):13454-13463. doi:10.1021/acs.jafc.8b05093
Sequence and Features
Assembly Compatibility:
- 10
COMPATIBLE WITH RFC[10]- 12
COMPATIBLE WITH RFC[12]- 21
COMPATIBLE WITH RFC[21]- 23
COMPATIBLE WITH RFC[23]- 25
INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 447- 1000
COMPATIBLE WITH RFC[1000]