Conformation and kinetic properties of photosynthetic glyceraldehyde-3-phosphate dehydrogenase "in vivo".
Photosynthetic GAPDH has been studied in chloroplast extracts, obtained in presence of physiological concentrations of NADP and NAD. The enzyme is shown to have a molecular weight of 600,000, on the basis of zymograms obtained after electrophoresis on polyacrylamide gradient gels. Km values of 0.08 and 0.16 mM, respectively, were found for NADP and NAD. The same V is reached with both NADP and NAD. The two coenzymes bind to the enzyme at the same catalytic site.
D002736:Chloroplasts / Q000201:enzymology; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D010788:Photosynthesis; D010944:Plants / Q000201:enzymology*; D011487:Protein Conformation
D009243:NAD; D009249:NADP; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases