Evolution and origins of rubisco.
Curr Biol
; 34(16): R764-R767, 2024 Aug 19.
Article
in En
| MEDLINE
| ID: mdl-39163833
ABSTRACT
Rubisco (D-ribulose 1,5-bisphosphate carboxylase/oxygenase) is the most abundant enzyme in the world, constituting up to half of the soluble protein content in plant leaves. Such is its ubiquity that its chemical fingerprint can be detected in the geological record spanning billions of years. Rubisco catalyses the conversion of inorganic CO2 into organic sugars, which underpin almost all of the biosphere, including our entire food chain. Due to its central role in the global carbon cycle, rubisco has been the subject of intense research for over 50 years. Rubisco is often considered inefficient due to its slow rate of carboxylation compared with other central metabolism enzymes, and its promiscuous oxygenase activity, which competes with the productive carboxylation reaction. It is hoped that engineering improved CO2 fixation will have significant advantages in agriculture and climate change mitigation. However, rubisco has proven difficult to engineer, with decades of efforts yielding limited results. Recent research has focused on reconstructing the evolutionary trajectory of rubisco to help elucidate its cryptic origins. Such evolutionary studies have led to a better understanding of both the origins of more complex rubisco forms and the broader relationship between rubisco's structure and function.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Ribulose-Bisphosphate Carboxylase
/
Evolution, Molecular
Language:
En
Journal:
Curr Biol
Journal subject:
BIOLOGIA
Year:
2024
Document type:
Article
Affiliation country: