rbcL (Large subunit of the ribulose-bisphosphate carboxylase/oxygenase)
Ribulose-1,5-biphosphate carboxylase/oxygenase catalyzes the first reaction of the Calvin cycle, converting the combination of Ribulose-1,5-biphosphate(RuBP) and carbon dioxide to two 3-phosphoglycerate molecular. The rbcL part encodes the large subunit of the RubisCo enzyme, which also contain the active site of the enzyme. In our carbon fixing pathway, the RubisCO enzyme is the most important enzyme catalyzing the reaction of RuBP and CO2.
The rbcL gene is from cynobacteria Synechococcus elongatus PCC7002.The activation of RubisCO will be maximize with the binding of the RbcS subunit. To get more information, see our composite part: RubisCO
Expression in E. coli
We inserted the part on pSB1C3 and transformed the plasmid into DH5 alpha. After the the formation of the colony, we extracted the plasmid and screened the construction by enzyme digestion.
Sequence and Features
- 10COMPATIBLE WITH RFC
- 12COMPATIBLE WITH RFC
- 21COMPATIBLE WITH RFC
- 23COMPATIBLE WITH RFC
- 25Illegal NgoMIV site found at 1149
Illegal AgeI site found at 252
- 1000COMPATIBLE WITH RFC
Codon oprimized Synechococcus elongatus PCC7002.
 Janet Newman 1t and Steven Gutteridge2*. (1994,JUN.15). Structure of an effector-induced inactivated state of ribulose 1,5-bisphosphate carboxylase/oxygenase: the binary complex between enzyme and xylulose 1,5-bisphosphate. Cell
 Inger Andersson a,*, Anders Backlund b. (2007, DEC.20). Structure and function of Rubisco. Plant Physiology and Biochemistry.
 Fuyu Gong, Guoxia Liu, Xiaoyun Zhai,Jie Zhou, Zhen Cai and Yin Li1 .(2015,Jun 18). Quantitative analysis of an engineered CO2-fixing Escherichia coli reveals great potential of heterotrophic CO2 fixation. Biotechnology for Biofuels.