From phosphatases to vanadium peroxidases: a similar architecture of the active site.
We show here that the amino acid residues contributing to the active sites of the vanadate containing haloperoxidases are conserved within three families of acid phosphatases; this suggests that the active sites of these enzymes are very similar. This is confirmed by activity measurements showing that apochloroperoxidase exhibits phosphatase activity. These observations not only reveal interesting evolutionary relationships between these groups of enzymes but may also have important implications for the research on acid phosphatases, especially glucose-6-phosphatase-the enzyme affected in von Gierke disease-of which the predicted membrane topology may have to be reconsidered.
Hemrika
W
W
E. C. Slater Institute, Plantage Muidergracht, Amsterdam, The Netherlands.
Renirie
R
R
Dekker
H L
HL
Barnett
P
P
Wever
R
R
D000135:Acid Phosphatase / Q000737:chemistry; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D005952:Glucose-6-Phosphatase / Q000737:chemistry; D005953:Glycogen Storage Disease Type I / Q000201:enzymology; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000737:chemistry* / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry* / Q000378:metabolism*
D010544:Peroxidases; C026195:bromide peroxidase; D000135:Acid Phosphatase; D010744:Phosphoric Monoester Hydrolases; D005952:Glucose-6-Phosphatase