Back روبيسكو Arabic Rubisco BS RuBisCO Catalan Rubisco Czech RuBisCO Danish RuBisCO German Ριβουλόζη-1,5-διφωσφορική καρβοξυλάση/οξυγενάση Greek Rubisko Esperanto RuBisCO Spanish RuBisCO Basque
| Ribulose-1,5-bisphosphate carboxylase oxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 A 3d depiction of the activated RuBisCO from spinach in open form with active site accessible. The active site Lys175 residues are marked in pink, and a close-up of the residue is provided to the right for one of the monomers composing the enzyme. | |||||||||
| Identifiers | |||||||||
| EC no. | 4.1.1.39 | ||||||||
| CAS no. | 9027-23-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Ribulose-1,5-bisphosphate carboxylase/oxygenase, commonly known by the abbreviations RuBisCo, rubisco,[1] RuBPCase,[2] or RuBPco,[3] is an enzyme (EC 4.1.1.39) involved in the light-independent (or "dark") part of photosynthesis, including the carbon fixation by which atmospheric carbon dioxide is converted by plants and other photosynthetic organisms to energy-rich molecules such as glucose. It emerged approximately four billion years ago in primordial metabolism prior to the presence of oxygen on Earth.[4] It is probably the most abundant enzyme on Earth. In chemical terms, it catalyzes the carboxylation of ribulose-1,5-bisphosphate (also known as RuBP).[5][6][7]
- ^ Sharkey TD (May 2019). "Discovery of the canonical Calvin-Benson cycle". Photosynthesis Research. 140 (2): 235–252. Bibcode:2019PhoRe.140..235S. doi:10.1007/s11120-018-0600-2. OSTI 1607740. PMID 30374727. S2CID 53092349.
- ^ Nivison, Helen; Stocking, C. (1983). "Ribulose Bisphosphate Carboxylase Synthesis in Barley Leaves". Plant Physiology. 73 (4): 906–911. doi:10.1104/pp.73.4.906. PMC 1066578. PMID 16663341.
- ^ Mächler, Felix; Nösberger, Josef (1988). "Bicarbonate Inhibits Ribulose-1,5-Bisphosphate Carboxylase". Plant Physiology. 88 (2): 462–465. doi:10.1104/pp.88.2.462. PMC 1055600. PMID 16666327.
- ^ Back to the future of photosynthesis: Resurrecting billon-year-old enzymes reveals how photosynthesis adapted to the rise of oxygen., News from the Max Planck Society, October 13, 2022
- ^ Cooper GM (2000). "10.The Chloroplast Genome". The Cell: A Molecular Approach (2nd ed.). Washington, D.C.: ASM Press. ISBN 978-0-87893-106-4.
, one of the subunits of ribulose bisphosphate carboxylase (rubisco) is encoded by chloroplast DNA. Rubisco is the critical enzyme that catalyzes the addition of CO2 to ribulose-1,5-bisphosphate during the Calvin cycle. It is also thought to be the single most abundant protein on Earth, so it is noteworthy that one of its subunits is encoded by the chloroplast genome.
- ^ Dhingra A, Portis AR, Daniell H (April 2004). "Enhanced translation of a chloroplast-expressed RbcS gene restores small subunit levels and photosynthesis in nuclear RbcS antisense plants". Proceedings of the National Academy of Sciences of the United States of America. 101 (16): 6315–6320. Bibcode:2004PNAS..101.6315D. doi:10.1073/pnas.0400981101. PMC 395966. PMID 15067115.
(Rubisco) is the most prevalent enzyme on this planet, accounting for 30–50% of total soluble protein in the chloroplast;
- ^ Feller U, Anders I, Mae T (2008). "Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated". Journal of Experimental Botany. 59 (7): 1615–1624. doi:10.1093/jxb/erm242. PMID 17975207.