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J Biol Chem, Vol. 273, Issue 5, 3076-3081, January 30, 1998

Human Small Intestinal Maltase-glucoamylase cDNA Cloning
HOMOLOGY TO SUCRASE-ISOMALTASE

Buford L. Nichols, Joyce Eldering^¶, Stephen Avery, Dagmar Hahn^¶, Andrea Quaroni, and Erwin Sterchi^¶

From the  United States Department of Agriculture Children's Nutrition Research Center, Baylor College of Medicine, Houston, Texas 77030-2600,  Department of Physiology, School of Veterinary Medicine, Cornell University, Ithaca, New York 14853-6401, and ^¶ Institute of Biochemistry and Molecular Biology, University of Berne, Büehlstrasse 28, CH-3012 Berne, Switzerland

It has been hypothesized that human mucosal glucoamylase (EC 3.2.1.20 and 3.2.1.3) activity serves as an alternate pathway for starch digestion when luminal -amylase activity is reduced because of immaturity or malnutrition and that maltase-glucoamylase plays a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing. As a first step toward the testing of this hypothesis, we have cloned human small intestinal maltase-glucoamylase cDNA to permit study of the individual catalytic and binding sites for maltose and starch enzyme hydrolase activities in subsequent expression experiments. Human maltase-glucoamylase was purified by immunoisolation and partially sequenced. Maltase-glucoamylase cDNA was amplified from human intestinal RNA using degenerate and gene-specific primers with the reverse transcription-polymerase chain reaction. The 6,513-base pair cDNA contains an open reading frame that encodes a 1,857-amino acid protein (molecular mass 209,702 Da). Maltase-glucoamylase has two catalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous. Both are members of glycosyl hydrolase family 31, which has a variety of substrate specificities. Our findings suggest that divergences in the carbohydrate binding sequences must determine the substrate specificities for the four different enzyme activities that share a conserved catalytic site.

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