Glyoxalase II from A. thaliana requires Zn(II) for catalytic activity.

@article{Crowder1997GlyoxalaseIF,
  title={Glyoxalase II from A. thaliana requires Zn(II) for catalytic activity.},
  author={Michael W Crowder and Motilal Maiti and L Banovic and Christopher A Makaroff},
  journal={FEBS letters},
  year={1997},
  volume={418 3},
  pages={351-4}
}
Cytosolic glyoxalase II from Arabidopsis thaliana, GLX2-2, was overexpressed and purified to homogeneity using Q-sepharose chromatography. MALDI-TOF mass spectrometry studies indicated a molecular weight of 28 767 Da. Using steady-state kinetics studies, the purified enzyme exhibited a Km of 660 +/- 100 microM and a kcat of 484 +/- 92 s(-1) at 37 degrees C. Metal analyses demonstrated that the enzyme binds 2.1 +/- 0.5 moles of Zn(II) per monomer; the binding of Zn(II) is essential for enzyme… CONTINUE READING
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