We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
[https://www.uniprot.org/uniprot/RBS_SYNE7 RBS_SYNE7] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_00859]<ref>PMID:24585024</ref> <ref>PMID:30675061</ref> Beta-carboxysome assembly initiates when soluble RuBisCO aggregates is condensed into a liquid matrix in a pre-carboxysome by the RbcS-like domains of probably both CcmM58 and CcmM35. CcmN interacts with the N-terminus of CcmM58, and then recruits the CcmK2 major shell protein via CcmN's encapsulation peptide. Shell formation requires CcmK proteins and CcmO. CcmL caps the otherwise elongated carboxysome. Once fully encapsulated carboxysomes are formed, they migrate within the cell probably via interactions with the cytoskeleton.<ref>PMID:24267892</ref> <ref>PMID:30675061</ref>
+
[https://www.uniprot.org/uniprot/RBL_SYNE7 RBL_SYNE7] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
-
== References ==
+
-
<references/>
+
==See Also==
+
*[[RuBisCO 3D structures|RuBisCO 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
Current revision
Structure of Synechococcus elongatus PCC 7942 Rubisco recombinantly expressed from E.coli
RBL_SYNE7 RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
