A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases.

@article{Galperin1998ASO,
  title={A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases.},
  author={Michael Y. Galperin and Amos Bairoch and Eugene V. Koonin},
  journal={Protein science : a publication of the Protein Society},
  year={1998},
  volume={7 8},
  pages={1829-35}
}
Sequence analysis of the probable archaeal phosphoglycerate mutase resulted in the identification of a superfamily of metalloenzymes with similar metal-binding sites and predicted conserved structural fold. This superfamily unites alkaline phosphatase, N-acetylgalactosamine-4-sulfatase, and cerebroside sulfatase, enzymes with known three-dimensional structures, with phosphopentomutase, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, phosphoglycerol transferase, phosphonate… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 50 extracted citations

Enzymatic Platform for Nucleoside Analogues Production

Sergi Pérez Ozcáriz
2017
View 1 Excerpt

Similar Papers

Loading similar papers…