CC-4829 rbcL-D473E mt+
$30.00
From Robert J. Spreitzer, University of Nebraska, July 2014
Directed mutagenesis and chloroplast transformation of rbcL∆-MX3312 mt+ (CC-4696) were used to create a D473E substitution (GAC-GAA) in the Rubisco large subunit, which causes a decrease in Rubisco CO2/O2 specificity but not holoenzyme stability (Satagopan and Spreitzer 2004). The x-ray crystal structure of the mutant protein has been solved (Karkehabadi et al. 2007). This is the original mutant strain. It was created due to a previous study of the role of Asp-473 in catalysis (Duff et al. 2000). The strain has been maintained with acetate medium in darkness to prevent selection for secondary mutations that may improve Rubisco function.
Duff AP, Andrews TJ, Curmi PM (2000) The transition between the open and closed states of rubisco is triggered by the inter-phosphate distance of the bound bisphosphate. J Mol Biol 298:903-916
Karkehabadi S, Satagopan S, Taylor TC, Spreitzer RJ, Andersson I (2007) Structural analysis of altered large-subunit loop-6/carboxy-terminus interactions that influence catalytic efficiency and CO2/O2 specificity of ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 46:11080-11089
Satagopan S, Spreitzer RJ (2004) Substitutions at the Asp-473 latch residue of Chlamydomonas ribulosebisphosphate carboxylase/oxygenase cause decreases in carboxylation efficiency and CO2/O2 specificity. J Biol Chem 279:14240-14244