Abell L M, Schloss J V
E. I. du Pont de Nemours and Company, Stine-Haskell Research Center, Newark, Delaware 19714.
Biochemistry. 1991 Aug 13;30(32):7883-7. doi: 10.1021/bi00246a002.
Enzymes that mediate carbanion chemistry must protect their reactants from solvent and undesirable electrophiles, such as molecular oxygen. A number of enzymes that utilize carbanionic intermediates were surveyed for O2-consuming side reactions. Several of these enzymes, acetolactate synthase, pyruvate decarboxylase, class II aldolase, and glutamate decarboxylase, catalyze previously undetected oxygen-consuming reactions, while others such as class I aldolase, [(phosphoribosyl)amino]imidazole carboxylase, 6-phosphogluconate dehydrogenase, isocitrate dehydrogenase, and triosephosphate isomerase do not. Prior to this work, only ribulosebisphosphate carboxylase was known to catalyze an oxygenase side reaction. These new example indicate that while O2-consuming side reactions are a more general feature of enzyme-mediated carbanion chemistry than has been previously appreciated, they are not necessarily an inevitable consequence of this chemistry. Expression of an oxygenase activity not only depends on the accessibility of the carbanionic intermediate to molecular oxygen but also may depend on the ability of the enzyme to stabilize the initially formed peroxide anion either through protonation with an appropriate enzymic group or through metal coordination.
