Kinetic studies and site-directed mutagenesis of Escherichia coli agmatinase. A role for Glu274 in binding and correct positioning of the substrate guanidinium group.

@article{Carvajal2004KineticSA,
  title={Kinetic studies and site-directed mutagenesis of Escherichia coli agmatinase. A role for Glu274 in binding and correct positioning of the substrate guanidinium group.},
  author={Nelson Carvajal and Mar{\'i}a Soledad Orellana and M{\'o}nica Salas and Paula Enr{\'i}quez and Ricardo Alarc{\'o}n and Elena A. Uribe and Vasthi L{\'o}pez},
  journal={Archives of biochemistry and biophysics},
  year={2004},
  volume={430 2},
  pages={185-90}
}
The interaction of Escherichia coli agmatinase (EC 3.5.3.11) with the substrate guanidinium group was investigated by kinetic and site-directed mutagenesis studies. Putrescine and guanidinium ions (Gdn+) were slope-linear, competitive inhibitors with respect to agmatine and their bindings to the enzyme were not mutually exclusive. By site-directed mutagenesis, the E274A variant exhibiting about 1-2% of wild-type activity was obtained. Mutation produced a moderate, but significant, increase in… CONTINUE READING

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