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Title

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

Authors
Galperin, Michael Y
Koonin, Eugene V
Published in Protein Science. 1998, vol. 7, no. 8, p. 1829-35
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/classificationAmino Acid SequenceComputer SimulationDatabases, FactualHumansHydrogen-Ion ConcentrationMetalloendopeptidases/classificationModels, MolecularMolecular Sequence DataPhosphoglycerate Mutase/classificationPhosphotransferases/classificationPhylogenySequence Homology, Amino AcidSulfatases/classification
Identifiers
PMID: 10082381
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Research group Calipho (80)
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. 1829-35. https://archive-ouverte.unige.ch/unige:74726

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Deposited on : 2015-08-17

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