Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.

@article{Sim2010StructuralBF,
  title={Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.},
  author={Lyann Sim and Carly Willemsma and Sankar Mohan and Hassan Y Naim and Brian Mario Pinto and David R. Rose},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 23},
  pages={17763-70}
}
Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products. MGAM and SI are each composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities. The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1… CONTINUE READING

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