The anomeric form of D-fructose 1,6-bisphosphate used as substrate in the muscle and yeast aldolase reactions.

Liver aldolase anomeric specificity

“…The curve in Figure 2a is clearly biphasic with the rapid initial phase (k = 4.7 s-1) accounting for the utilization of ~74% of the initial substrate concentration and a slow phase (k = 0.69 s_l) completing the reaction. These data are identical with those previously described (Schray et al, 1975;Wurster & Hess, 1974). The trace from a similar experiment employing liver Unlike the muscle aldolase experiment, this replot is linear with k = 1.7 s'1 which is in reasonable agreement with the turnover number under dilute enzyme conditions (1.8 s'1 at 25 °C) (Rutter, 1964).…”

“…Muscle aldolase has been shown by Wurster & Hess (1973) as well as by Schray et al (1975) to be specific for the /? anomer of fructose 1,6-bisphosphate (FBP)1 and to bind the 0006-2960/80/0419-2593S01.00/0 © 1980 American Chemical Society a-FBP so tightly as to slow anomerization and inhibit its use as a substrate, In rapid kinetic experiments which employed mixtures of muscle aldolase and yeast apoaldolase, the latter authors have demonstrated the presence of an anomerase activity in the yeast enzyme which allows utilization of all substrate forms.…”

Anomeric specificity of yeast pyruvate kinase toward activation by D-fructose 1,6-bisphosphate

“…2 Estimations of the rate constants of the mutarotation processes used in eq 2 and 3 were obtained from several sources (Fishbein et al, 1974;Wurster and Hess, 1974a,b;and Schray et al, 1975). It should be noted that there is some variation in these numbers.…”

“…Since D-fructose-T6-P2 exists in solution in three rapidly equilibrating configurations, it became of interest to investigate whether pyruvate kinase from yeast is subject to stereospecific activation by only one of the three possible forms. Several other glycolytic and gluconeogenic enzymes have been observed to show a dependence on the anomeric nature of their substrates; these include phosphoglucose isomerase (Schray et al, 1973), Dfructose-6-P kinase (Fishbein et al, 1974;Wurster and Hess, 1974a; Bar-Tana and Cleland, 1974;Koerner et al, 1974), fructose bisphosphatase (Benkovic et al, 1974), and aldolase (Schray et al, 1975;Wurster and Hess, 1974b).…”

From Bioorganic Models to Cells

“…In the case of fructose 1,6-bisphosphatase, both matched our quench studies on this sugar implicating the α-anomers as the enzyme's substrate. We then went on to elucidate the anomeric specificity of all of the enzymes in the glycolytic pathway (16)(17)(18)(19)(20).…”