| Range |
~1-5 cycles/sec
|
| Organism |
Various |
| Reference |
Wilson, R.H. & Whitney S.M. Improving CO2 fixation by enhancing Rubisco performance. In: Directed Enzyme Evolution: advances and applications. Alcalde, M. (ed.). Springer, Switzerland. Pp: 101-126 (2017) p.102 top paragraph |
| Primary Source |
[9] Carmo-Silva E, Scales JC, Madgwick PJ, Parry MAJ (2015) Optimizing Rubisco and its regulation for greater resource use efficiency. Plant Cell Environ 38(9):1817–1832 doi: 10.1111/pce.12425 [45] Long Stephen P, Marshall-Colon A, Zhu X-G (2015) Meeting the global food demand of the future by engineering crop photosynthesis and yield potential. Cell 161(1):56–66 doi: 10.1016/j.cell.2015.03.019PubMed ID25123951, 25815985
|
| Comments |
P.102 top paragraph: "The CO2-fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the catalytic gatekeeper linking the inorganic and organic phases of the
biosphere’s carbon cycle. Rubisco initiates carbon assimilation in the Calvin cycle by fixing CO2 to the pentose sugar substrate ribulose-1,5-bisphosphate (RuBP) and cleaving it into two molecules of 3-phosphoglycerate (3-PGA, Fig. 4.1a). The 3-PGA is the precursor to carbohydrate synthesis that is required for energy and growth. In plants and algae the carboxylation reaction of Rubisco occurs at a slow
pace (~1–5 cycles per second) resulting in its catalytic properties often limiting the rate of photosynthesis and growth in these organisms [primary sources]. To compensate for this shortcoming, many photosynthetic organisms require high amounts of Rubisco to meet their metabolic needs." Please note-turnover rate wasn't located in primary sources |
| Entered by |
Uri M |
| ID |
114623 |