An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases.
The mechanism of a membrane-bound enzyme important in phospholipid signaling, type 2 phosphatidic acid phosphatase, is suggested by sequence motifs shared with a soluble vanadium-dependent chloroperoxidase of known structure. These regions are also conserved in other soluble globular and membrane-associated proteins, including bacterial acid phosphatases, mammalian glucose-6-phosphatases, and the Drosophila developmental protein Wunen. This implies that a similar arrangement of catalytic residues specifies the active site within both soluble and membrane spanning domains.
Neuwald
A F
AF
National Center for Biotechnology Information, National Institutes of Health, Bethesda, Maryland 20894, USA. neuwald@ncbi.nlm.nih.gov
D000595:Amino Acid Sequence; D002711:Chloride Peroxidase / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000737:chemistry*; D010711:Phosphatidate Phosphatase / Q000737:chemistry*; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D008565:Membrane Proteins; D010544:Peroxidases; C026195:bromide peroxidase; D002711:Chloride Peroxidase; D010711:Phosphatidate Phosphatase