PMID:18234116
| Citation |
Schenk, G, Elliott, TW, Leung, E, Carrington, LE, Mitić, N, Gahan, LR and Guddat, LW (2008) Crystal structures of a purple acid phosphatase, representing different steps of this enzyme's catalytic cycle. BMC Struct. Biol. 8:6 |
|---|---|
| Abstract |
Purple acid phosphatases belong to the family of binuclear metallohydrolases and are involved in a multitude of biological functions, ranging from bacterial killing and bone metabolism in animals to phosphate uptake in plants. Due to its role in bone resorption purple acid phosphatase has evolved into a promising target for the development of anti-osteoporotic chemotherapeutics. The design of specific and potent inhibitors for this enzyme is aided by detailed knowledge of its reaction mechanism. However, despite considerable effort in the last 10 years various aspects of the basic molecular mechanism of action are still not fully understood. |
| Links |
PubMed PMC2267794 Online version:10.1186/1472-6807-8-6 |
| Keywords |
Acid Phosphatase/chemistry; Binding Sites; Catalysis; Crystallography, X-Ray; Fluorides/chemistry; Fluorides/metabolism; Glycoproteins/chemistry; Kinetics; Ligands; Models, Molecular; Phaseolus/enzymology; Plant Proteins/chemistry; Protein Conformation; Sulfates/chemistry; Sulfates/metabolism |
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