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A superfamily of metalloenzymes unifies phosphopentomutase and cofactor‐independent phosphoglycerate mutase with alkaline phosphatases and sulfatases
Author(s) -
Galperin Michael Y.,
Koonin Eugene V.,
Bairoch Amos
Publication year - 1998
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560070819
Subject(s) - phosphoglycerate mutase , mutase , biochemistry , chemistry , enzyme , phosphatase , histidine , biology , glycolysis
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.