Phylogenetic engineering at an interface between large and small subunits imparts land-plant kinetic properties to algal Rubisco.

ABSTRACT: Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the rate-limiting step of photosynthetic CO(2) fixation and, thus, limits agricultural productivity. However, Rubisco enzymes from different species have different catalytic constants. If the structural basis for such differences were known, a rationale could be developed for genetically engineering an improved enzyme. Residues at the bottom of the large-subunit alpha/beta-barrel active site of Rubisco from the green alga Chlamydomonas reinhardtii (methyl-Cys-256, Lys-258, and Ile-265) were previously changed through directed mutagenesis and chloroplast transformation to residues characteristic of land-plant Rubisco (Phe-256, Arg-258, and Val-265). The resultant enzyme has decreases in carboxylation efficiency and CO(2)/O(

SUBMITTER: Spreitzer RJ 

PROVIDER: S-EPMC1287997 | biostudies-literature | 2005 Nov

REPOSITORIES: biostudies-literature