Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD+/Mn2+ -dependent phospho-alpha-glucosidase from Bacillus subtilis.

@article{Rajan2004NovelCM,
  title={Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD+/Mn2+ -dependent phospho-alpha-glucosidase from Bacillus subtilis.},
  author={Shyamala S. Rajan and Xiaojing Yang and Frank L Collart and Vivian L Y Yip and Stephen G Withers and Annabelle Varrot and John Thompson and Gideon J Davies and Wayne F Anderson},
  journal={Structure},
  year={2004},
  volume={12 9},
  pages={1619-29}
}
GlvA, a 6-phospho-alpha-glucosidase from Bacillus subtilis, catalyzes the hydrolysis of maltose-6'-phosphate and belongs to glycoside hydrolase family GH4. GH4 enzymes are unique in their requirement for NAD(H) and a divalent metal for activity. We have determined the crystal structure of GlvA in complex with its ligands to 2.05 A resolution. Analyses of the active site architecture, in conjunction with mechanistic studies and precedent from the nucleotide diphosphate hexose dehydratases and… CONTINUE READING

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