Yeast glyceraldehyde-3-phosphate dehydrogenase : Evidence that subunit cooperativity in catalysis can be controlled by the formation of a complex with phosphoglycerate kinase

Functional studies of chloroplast glycer

Functional studies of chloroplast glyceraldehyde-3-phosphate dehydrogenase subunits A and B expressed inEscherichia coli: formation of highly active A4and B4homotetramers and evidence that aggregation of the B4complex is mediated by the B subunit carboxy terminus

✍ Elisabeth Baalmann; Renate Scheibe; Rüdiger Cerff; William Martin 📂 Article 📅 1996 🏛 Springer 🌐 English ⚖ 791 KB

Chloroplast glyceraldehyde-3-phosphate dehydrogenase (phosphorylating, E.C. 1.2.1.13) (GAPDH) of higher plants exists as an A2B2 heterotetramer that catalyses the reductive step of the Calvin cycle. In dark chloroplasts the enzyme exhibits a molecular mass of 600 kDa, whereas in illuminated chloropl