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Scientific article
Open access
English

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

Published inProtein science, vol. 7, no. 8, p. 1829-1835
Publication date1998
Abstract

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 monoesterase, streptomycin-6-phosphate phosphatase, alkaline phosphodiesterase/nucleotide pyrophosphatase PC-1, and several closely related sulfatases. In addition to the metal-binding motifs, all these enzymes contain a set of conserved amino acid residues that are likely to be required for the enzymatic activity. Mutational changes in the vicinity of these residues in several sulfatases cause mucopolysaccharidosis (Hunter, Maroteaux-Lamy, Morquio, and Sanfilippo syndromes) and metachromatic leucodystrophy.

Keywords
  • Alkaline Phosphatase/classification
  • Amino Acid Sequence
  • Computer Simulation
  • Databases, Factual
  • Humans
  • Hydrogen-Ion Concentration
  • Metalloendopeptidases/classification
  • Models, Molecular
  • Molecular Sequence Data
  • Phosphoglycerate Mutase/classification
  • Phosphotransferases/classification
  • Phylogeny
  • Sequence Homology, Amino Acid
  • Sulfatases/classification
Research group
Citation (ISO format)
GALPERIN, Michael Y, BAIROCH, Amos Marc, KOONIN, Eugene V. A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases. In: Protein science, 1998, vol. 7, n° 8, p. 1829–1835. doi: 10.1002/pro.5560070819
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Article (Published version)
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Identifiers
ISSN of the journal0961-8368
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258downloads

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