Redox regulation of phosphoglycerate kinase in cyanobacterium Synechocystis sp.PCC 6803

Abstract

Thioredoxin is a small ubiquitous protein, which mediates dithiol-disulfide exchange reaction using reducing equivalents provided by photosynthetic electron transport or NADPH via thioredoxin reductase. For this decade, many target candidate proteins are reported by proteomics analysis using two-dimensional gel electrophoresis and thioredoxin chromatography with immobilized thioredoxin mutant.
Phosphoglycerate kinase (PGK) is an enzyme working at the second step of Calvin-Benson cycle in Synechocystis sp. PCC6803 and recently reported as a target of thioredoxin (Perez-Perez M. E., et al. (2006) Proteomics. Suppl 1:S186-95). In this study, we studied the biochemical properties of this PGK in vitro and in vivo, especially in light of a possible thioredoxin target.