NADPH activates a decarboxylation reaction catalysed by lamb liver 6-phosphogluconate dehydrogenase.
NADP-dependent lamb liver 6-phosphogluconate dehydrogenase catalyses the oxidative decarboxylation of 2-deoxy-6-phosphogluconate, an analogue of the natural substrate. The first products of the reaction are NADPH and 3-keto-2-deoxy-6-phosphogluconate. The NADPH, released from the enzyme, binds to the coenzyme site of the same or the other subunit, activating the decarboxylation reaction in which has not a redox role, since it can be substituted by an analogue devoid of enzymatic redox power. These findings are compared to those obtained with other NADP-dependent decarboxylating dehydrogenases.
Hanau
S
S
Istituto di Chimica Biologica, Università, Ferrara, Italy.
Dallocchio
F
F
Rippa
M
M
D000818:Animals; D003653:Decarboxylation / Q000187:drug effects; D004789:Enzyme Activation / Q000187:drug effects; D005942:Gluconates / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000187:drug effects* / Q000201:enzymology; D009249:NADP / Q000494:pharmacology*; D010084:Oxidation-Reduction; D010734:Phosphogluconate Dehydrogenase / Q000378:metabolism*; D012756:Sheep; D013379:Substrate Specificity
D005942:Gluconates; C005067:2-deoxy-6-phosphogluconate; D009249:NADP; D010734:Phosphogluconate Dehydrogenase