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- W2170996876 abstract "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 (35 kDa vs. 55 kDa 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." @default.
- W2170996876 created "2016-06-24" @default.
- W2170996876 creator A5007489810 @default.
- W2170996876 creator A5018905339 @default.
- W2170996876 creator A5026257435 @default.
- W2170996876 creator A5081056588 @default.
- W2170996876 date "2013-01-01" @default.
- W2170996876 modified "2023-10-17" @default.
- W2170996876 title "Purple acid phosphatase: A journey into the function and mechanism of a colorful enzyme" @default.
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