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From the
1 From the Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139
The pathway of myo-inositol catabolism in Aerobacter aerogenes has been studied, beginning with the first noncyclic intermediate, 2-deoxy-5-keto-d-gluconic acid. A kinase acts on 2-deoxy-5-keto-d-gluconic acid to yield a monophosphorylated product. The isolation of the kinase product was rendered difficult by the presence, in both crude and 20-fold purified extracts, of the next enzyme in the pathway, an aldolase which catalyzes the cleavage of the kinase product to yield dihydroxyacetone phosphate and malonic semialdehyde. However, accumulation of the kinase product was accomplished by specific inactivation of the aldolase by reduction with sodium borohydride in the presence of dihydroxyacetone phosphate. The kinase product was identified as 2-deoxy-5-keto-d-gluconic acid 6-phosphate. Malonic semialdehyde is further metabolized by the last enzyme in the pathway, malonic semialdehyde oxidative decarboxylase. This enzyme was also partially purified. It catalyzes the conversion of malonic semialdehyde, coenzyme A, and NAD+ to acetyl-CoA, CO2, and NADH + H+. All three of the enzymes that have been identified in this study are induced by growth on myo-inositol, and are constitutive in a mutant which is constitutive for the first three enzymes of the inositol pathway. The operation of the pathway thus results in the conversion of myo-inositol to an equimolar mixture of three known metabolites: dihydroxyacetone phosphate, acetyl-CoA, and CO2.
The Pathway of myo-Inositol Degradation in Aerobacter aerogenes
CONVERSION OF 2-DEOXY-5-KETO-d-GLUCONIC ACID TO GLYCOLYTIC INTERMEDIATES
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