1.1.1.363	additional information	-	the enzyme is rapidly inactivated by micromolar concentrations of Fe2+ and H2O2. Fe2+ binds to the glucose 6-phosphate binding site and interaction of the enzyme-bound Fe2+ with H2O2 leads to the oxidative modification of amino acids essential for enzyme activity. Partially inactivated enzyme remains predominantly in the dimeric form, and no change in the apparent affinity of the remaining active subunits for substrate is observed. Partial inactivation leads to a decrease in the thermal stability of the remaining activity. This decrease in thermal stability could be largely overcome by the addition of glucose 6-phosphate. Thus, although exposure to H2O2 and Fe2+ results in the irreversible inactivation of the enzyme, the resulting modification is selective, leads to the formation of heterodimers of both active and inactive subunits, and does not appear to cause large scale structural changes	722593	
1.1.1.363	4	20	the secondary structure of the enzyme is maintained between 4-40°C, its activity and tertiary structure are better preserved between 4-20°C	761295	
1.1.1.363	49	-	first order rate constant for inactivation is 0.05/min. Protection by 72 mM NAD+ or by 6.3 mM glucose 6-phosphate or 72 mM NADP+	721406	
1.1.1.363	60	-	20 min, complete loss of activity	761295