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An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases
1National Center for Biotechnology Information, National Institutes of Health, Bethesda, Maryland 20894, USA. neuwald@ncbi.nlm.nih.gov
Protein Science : a Publication of the Protein Society
|August 1, 1997
Summary
Sequence motifs suggest type 2 phosphatidic acid phosphatase (PAP2) shares a catalytic mechanism with vanadium-dependent chloroperoxidase. This implies conserved active site structures across diverse soluble and membrane-bound phosphatases.
Area of Science:
- Biochemistry
- Enzymology
- Molecular Biology
Background:
- Type 2 phosphatidic acid phosphatase (PAP2) is a key enzyme in phospholipid signaling pathways.
- Understanding the catalytic mechanism of membrane-bound enzymes like PAP2 is crucial for cellular regulation.
Purpose of the Study:
- To elucidate the catalytic mechanism of the membrane-bound enzyme PAP2.
- To identify conserved structural and functional elements across different phosphatases.
Main Methods:
- Comparative sequence analysis of PAP2 with proteins of known structure.
- Identification of conserved sequence motifs and potential catalytic residues.
Main Results:
- Sequence motifs in PAP2 are shared with soluble vanadium-dependent chloroperoxidase.
- These conserved regions are also found in bacterial acid phosphatases, mammalian glucose-6-phosphatases, and Drosophila Wunen protein.
- This suggests a conserved catalytic residue arrangement in active sites.
Conclusions:
- The catalytic mechanism of PAP2 is likely similar to that of vanadium-dependent chloroperoxidase.
- A conserved active site structure is implied for both soluble and membrane-spanning domains of phosphatases.
- This finding provides insights into the evolution and function of phosphatases.