Identification of residues important for NAD+ binding by the Thermotoga maritima alpha-glucosidase AglA, a member of glycoside hydrolase family 4.

@article{Raasch2002IdentificationOR,
  title={Identification of residues important for NAD+ binding by the Thermotoga maritima alpha-glucosidase AglA, a member of glycoside hydrolase family 4.},
  author={Carsten Raasch and Martin Armbrecht and Wolfgang R. Streit and Birte H{\"o}cker and Norbert Str{\"a}ter and Wolfgang Liebl},
  journal={FEBS letters},
  year={2002},
  volume={517 1-3},
  pages={267-71}
}
The NAD+-requiring enzymes of glycoside hydrolase family 4 (GHF4) contain a region with a conserved Gly-XXX-Gly-Ser (GXGS) motif near their N-termini that is reminiscent of the fingerprint region of the Rossmann fold, a conserved structural motif of classical nicotinamide nucleotide-binding proteins. The function of this putative NAD+-binding motif in the alpha-glucosidase AglA of Thermotoga maritima was probed by directed mutagenesis. The K(d) for NAD+ of the AglA mutants G10A, G12A and S13A… CONTINUE READING

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