Microbial ribulose 1,5-bisphosphate carboxylase/oxygenase: a molecule for phylogenetic and enzymological investigation

• Published in: FEMS microbiology letters Vol. 146; no. 1; pp. 13 - 22
• Main Authors: Watson, Gregory M.F, Tabita, F.Robert
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.01.1997; Oxford University Press
• Subjects: Cyanobacteria - enzymology; Cyanobacteria - genetics; Enzymes; Gene Transfer Techniques; Genes, Bacterial; Kinetics; Macromolecules; Microbiology; Microorganisms; Models, Molecular; Molecular phylogeny; Molecular Structure; Multigene Family; Mutagenesis; Oxygenase; Pentose; Pentose phosphate pathway; Phylogeny; Protein Conformation; Ribulose 1,5‐bisphosphate carboxylase/oxygenase; Ribulose-bisphosphate carboxylase; Ribulose-Bisphosphate Carboxylase - chemistry; Ribulose-Bisphosphate Carboxylase - genetics; Ribulose-Bisphosphate Carboxylase - metabolism; RubisCO; Structure; RubisCO; Molecular phylogeny; Kinetics; Mutagenesis; Structure; Ribulose 1,5-bisphosphate carboxylase/oxygenase
• ISSN: 0378-1097; 1574-6968
• DOI: 10.1111/j.1574-6968.1997.tb10165.x

Abstract Ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO) catalyzes the key reaction of the Calvin reductive pentose phosphate cycle and as such is responsible for life as we know it. This enzyme has been intensively studied for decades. Evidence that RubisCO phylogenies are incongruent with those derived from other macromolecules has been accumulating and recent discoveries have driven home this point. Here we review findings regarding RubisCO phylogeny and discuss these in the context of the important biochemical and structural features of the enzyme. The implications for the engineering of improved RubisCO enzymes are considered.