Purple acid phosphatase: a journey into the function and mechanism of a colorful enzyme
Purple acid phosphatases (PAPs) catalyze the hydrolysis of a wide range of phosphomonoester and amide substrates. These enzymes have been identified and characterized from numerous plant and animal sources, and it is likely that a limited number of bacterial organisms also utilize this catalyst. The...
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| Main Authors: | , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
2013
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| In: |
Coordination chemistry reviews
Year: 2013, Volume: 257, Issue: 2, Pages: 473-482 |
| ISSN: | 0010-8545 |
| DOI: | 10.1016/j.ccr.2012.03.020 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.ccr.2012.03.020 Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0010854512000604 
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| Author Notes: | Gerhard Schenk, Nataša Mitić, Graeme R. Hanson, Peter Comba |
| Summary: | Purple acid phosphatases (PAPs) catalyze the hydrolysis of a wide range of phosphomonoester and amide substrates. These enzymes have been identified and characterized from numerous plant and animal sources, and it is likely that a limited number of bacterial organisms also utilize this catalyst. The biological roles of this enzyme are diverse, including bone resorption, microbial killing and possibly iron transport in animals, and phosphate acquisition in plants. While animal and plant PAPs share less than 20% amino acid sequence identity and differ (with a couple of exceptions) greatly in size (35kDa vs. 55kDa per monomer) and oligomeric structure (monomer vs. homodimer), their catalytically relevant active sites are highly conserved, with seven invariant amino acid side chains coordinating an Fe3+ and an M2+ (M=Fe or Zn, Mn in animal or plant PAPs, respectively). Recent functional studies have indicated that PAPs are rather flexible in terms of the precise mechanistic strategy they may employ. Here, we review advances that have facilitated detailed insight into how these enzymes operate. The knowledge gained is not only of interest for coordination chemists and biochemists who focus on the physicochemical and mechanistic properties of the active site metal ion center in a metalloenzyme, but also for medicinal chemists who aim to exploit PAP as a target for the development of novel chemotherapeutics to treat osteoporosis. |
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| Item Description: | Available online 24 March 2012 Gesehen am 07.02.2022 |
| Physical Description: | Online Resource |
| ISSN: | 0010-8545 |
| DOI: | 10.1016/j.ccr.2012.03.020 |