Scientific article
OA Policy
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 groups
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
Main files (1)
Article (Published version)
accessLevelPublic
Identifiers
Journal ISSN0961-8368
522views
302downloads

Technical informations

Creation12/08/2015 13:12:00
First validation12/08/2015 13:12:00
Update time14/03/2023 23:33:54
Status update14/03/2023 23:33:54
Last indexation31/10/2024 01:05:16
All rights reserved by Archive ouverte UNIGE and the University of GenevaunigeBlack