reviewAnnual Review of Plant BiologyJun 1, 2002Closed access

R UBISCO : Structure, Regulatory Interactions, and Possibilities for a Better Enzyme

University of Nebraska–Lincoln · Institute of Agriculture and Natural Resources · +2 more institutions

PubMed
Indexed incrossrefpubmed

Abstract

Ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) catalyzes the first step in net photosynthetic CO2 assimilation and photorespiratory carbon oxidation. The enzyme is notoriously inefficient as a catalyst for the carboxylation of RuBP and is subject to competitive inhibition by O2, inactivation by loss of carbamylation, and dead-end inhibition by RuBP. These inadequacies make Rubisco rate limiting for photosynthesis and an obvious target for increasing agricultural productivity. Resolution of X-ray crystal structures and detailed analysis of divergent, mutant, and hybrid enzymes have increased our insight into the structure/function relationships of Rubisco. The interactions and associations…

Citation impact

874
total citations
FWCI
8.97
Percentile
100%
References
165
Citations per year

Authors

2

Topics & keywords

Keywords
  • RuBisCO
  • Photosynthesis
  • Ribulose
  • Photorespiration
  • Biochemistry
  • Pyruvate carboxylase
  • Oxygenase
  • Enzyme
UN Sustainable Development Goals
  • Zero hunger
No related works found for this paper.