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J Bacteriol. 1971 April; 106(1): 90-96
Copyright © 1971 American Society for Microbiology. All Rights Reserved.

Metabolism of D-Arabinose: a New Pathway in Escherichia coli¹

^a Department of Microbiology, University of Massachusetts, Amherst, Massachusetts 01002

ABSTRACT

Several growth characteristics of Escherichia coli K-12 suggest that growth on L-fucose results in the synthesis of all the enzymes necessary for growth on D-arabinose. Conversely, when a mutant of E. coli is grown on D-arabinose, all of the enzymes necessary for immediate growth on L-fucose are present. Three enzymes of the L-fucose pathway in E. coli, L-fucose isomerase, L-fuculokinase, and L-fuculose-l-phospháte aldolase possess activity on D-arabinose, D-ribulose, and D-ribulose-l-phosphate, respectively. The products of the aldolase, with D-ribulose-l-phosphate as substrate, are dihydroxyacetone phosphate and glycolaldehyde. L-Fucose, but not D-arabinose, is capable of inducing these activities in wild-type E. coli. In mutants capable of utilizing D-arabinose as sole source of carbon and energy, these activities are induced in the presence of D-arabinose and in the presence of L-fucose. Mutants unable to utilize L-fucose, selected from strains capable of growth on D-arabinose, are found to have lost the ability to grow on D-arabinose. Enzymatic analysis of cell-free extracts, prepared from cultures of these mutants, reveals that a deficiency in any of the L-fucose pathway enzymes results in the loss of ability to utilize D-arabinose. Thus, the pathway of D-arabinose catabolism in E. coli K-12 is believed to be: D-arabinose D-ribulose D-ribulose-l-phosphate dihydroxyacetone phosphate plus glycolaldehyde. Evidence is presented which suggests that the glycolaldehyde is further oxidized to glycolate.

² Present address: Department of Microbiology, Georgetown University Medical School, Washington, D.C. 20007.

¹ This paper was presented in part at the 70th Annual Meeting of the American Society for Microbiology, Boston, Massachusetts, 26 April-1 May 1970.

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