Molecular symmetry of human glyceraldehyde 3-phosphate dehydrogenase and its transformation during coenzyme binding

Preparation and active-site specific properties of sturgeon muscle glyceraldehyde-3-phosphate dehydrogenase

“…Near pH 9, where the catalytic oxidative phosphorylation rate is nearly optimal for both the sturgeon muscle and the yeast enzyme, the two highly purified enzymes have virtually the same specific activity. The highly purified enzyme tetramer T A he chemical (Velick and Furfine, 1963; Furfine and Velick, 1965;Harris, 1970), physical (Jaenicke, 1969;Watson et al 1972; Gorjunov et al, 1972), and allosteric (Conway and Koshland, 1968;Malhotra and Bernhard, 1968; Kirschner et al, 1971;Trentham, 1971b;Boers et al, 1971) properties of a variety of glyceraldehyde-3-phosphate dehydrogenases have been discussed in considerable detail. Enzymes obtained from a wide range of species have very similar structural properties.…”

D-Glyceraldehyde-3-Phosphate Dehydrogenase: Three-Dimensional Structure and Evolutionary Significance

“…Preliminary crystallographic studies have been reported on glyceraldehyde-3-phosphate dehydrogenase from lobster (6), crayfish (7), Bacillus stearothermophilus (8), and humans (9 (16). The assumption that the subunits are identical at 3-A resolution is justified by the heavyatom sites obeying the molecular 222 symmetry to better than 0.5 A.…”

The investigation of regulatory transition in D‐glyceraldehyde‐3‐phosphate dehydrogenase quaternary structure

“…We suppose that regulatory mechanisms involve mainly nondissociative transitions in the quaternary structure such as oligomer symmetry changes. These rearrangements have been observed by X-ray analysis of hemoglobin [l] and some dehydrogenases [2,3], as a result of their interactions with coenzyme and substrate. There might be a change in the interactions between monomers in the course of an enzymatic reaction to provide the co-ordinate of the functions of several active sites.…”