Abstract
1. 1. Crystalline musclel aldolase catalyzes the exchange of deuterium from solvent D 2O with one substituent hydrogen of dihydroxyacetone phosphate. This partial reaction occurs in the absence of added glyceroaldehyde-3-phosphate. 2. 2. Aldolase does not catalyze a deuterium exchange reaction with glyceraldehyde-3-phosphate or 1 (+)-glycerophophate under similar conditions. 3. 3. When dihydroxyacetone phosphate labeled with deuterium by the exchange reaction is allowed to react with glyceraldehyde-3-phosphate in the presence of aldolase, the fructose diphosphate formed contains little if any deuterium. 4. 4. The rate of the aldolase-catalyzed deuterium exchange reaction is of the same order of magnitude as the overall reaction. 5. 5. Possible mechanistic interpretations of aldolase-catalyzed reactions are discussed.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
