Functional and structural characterization of four glutaminases from Escherichia coli and Bacillus subtilis.

@article{Brown2008FunctionalAS,
  title={Functional and structural characterization of four glutaminases from Escherichia coli and Bacillus subtilis.},
  author={Greg A. Brown and Alex U Singer and Michael Proudfoot and Tatiana Skarina and Youngchang Kim and Changsoo Chang and Irina N Dementieva and Ekaterina Kuznetsova and Claudio Feij{\'o}o Gonz{\'a}lez and Andrzej Joachimiak and Alexei Savchenko and Alexander F Yakunin},
  journal={Biochemistry},
  year={2008},
  volume={47 21},
  pages={5724-35}
}
Glutaminases belong to the large superfamily of serine-dependent beta-lactamases and penicillin-binding proteins, and they catalyze the hydrolytic deamidation of L-glutamine to L-glutamate. In this work, we purified and biochemically characterized four predicted glutaminases from Escherichia coli (YbaS and YneH) and Bacillus subtilis (YlaM and YbgJ). The proteins demonstrated strict specificity to L-glutamine and did not hydrolyze D-glutamine or L-asparagine. In each organism, one glutaminase… CONTINUE READING