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J Bacteriol. 1962 November; 84(5): 877-881
Copyright © 1962, The Williams & Wilkins Company. All Rights Reserved.

SUBSTRATE SPECIFICITY OF A GLUCOSE PERMEASE OF ESCHERICHIA COLI¹

^a Department of Food and Nutrition, Utah State University, Logan, Utah

ABSTRACT

ROGERS, DEXTER (Utah State University, Logan) AND SHON-HUA YU. Substrate specificity of a glucose permease of Escherichia coli. J. Bacteriol. 84:877–881. 1962.—A study was made of D-galactose uptake by galactose-negative Escherichia coli strain A (Weigle). Uptake probably occurred through a glucose-permease system, because D-glucose and a variety of nonmetabolizable glucose derivatives inhibited the accumulation of galactose and were themselves accumulated. D-Fructose did not inhibit galactose uptake. 6-Deoxy-D-galactose (D-fucose) was taken up by a different permease system. The glucose permease apparently favored pyranoses, and it required the 6-hydroxyl group of the substrate to a greater extent than any of the other hydroxyl groups. Although much of the absorbed glucose-permease substrate was recovered in the free form, a significant amount was recovered as the 6-phosphate ester. Depending on the conditions employed to study uptake, the 6-phosphate ester could amount to as much as 60% of the absorbed galactose.

² Present address: Department of Chemistry, Utah State University, Logan.

¹ Approved as Journal paper no. 273 by the Utah Agricultural Experiment Station, 1962. A preliminary report was given at the Pacific Slope Biochemical Conference, Davis, Calif., 1960.

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