Abstract
The three forms of glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor muscle, namely apo native enzyme, apo calboxymethylated enzyme and the enzyme carrying two fluorescent NAD deriva- tives per tetramer have been crystallized. The space groups and unit cell dimensions of these crystals are isomorphous to each other and to those of three corresponding holo-enzymes saturated with NAD~+ reported in a previous paper suggesting that binding of coenzyme to the apo enzymes does not lead to significant conformational changes involving domain movement as demonstrated in the case of glyceraldehyde-3-phos- phate dehydrogenase from Bacillus stearothermophilus.
Published Version
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