LOC56985 intro

At least one third of enzymes requires metal ions to function, the majority of these enzymes require two metal ions for functionality however the are examples of multinuclear metal clusters (Schenk, Elliott, Leung, Carrington, Mitić, & Guddat, 2008). One such process that metalloenzymes catalyse is the hydrolysis of phosphodiester bonds, a crucial biochemical reaction in a number of different metabolic and regulatory pathways (Boyer, 1971). The substrates for this reaction are usually mono- and dinucleotides, polynucleotides and phosphorylated proteins (Koonin, 1994). Here we have characterised the hypothetical protein LOC56985, which contains the conserved motif GN/GNH[ED] common in phosphoresterases. Secondary structure analysis has indicated that structural homologues of this protein include purple acid phosphatases and glycerophosphodiesterases that are all defined as Calcineurin-like phosphoesterases (Pfam domain PF00149). This domain classification is large and diverse group of proteins that contain 47 structures and 113 protein architectures (Finn, et al., 2006; Bateman, et al., 2004).

Purple acid phosphatases (PAPs) (EC 3.1.3.2) are metalloenzymes that hydrolyse phosphate esters and anhydrides. Usually these proteins are referred to as PAPs when in plants, and titrate-resistant acid phosphatases (TRAPs) when in animals. In biology, most of the high-energy phosphate compounds are formed from the condensation of the phosphate ion with a phosphorylated sugar (like ribose on a nucleotide like ADP/ CDP), the resulting pyrophosphate bond is a classic anhydride bond. (which is exactly what our protein hydrolyses according to that article on the rat ortholog). Mammalian and plant PAPs only show <20% sequence similarity but all the critical residues are always conserved (Schenk, Korsinczky, Hume, Hamilton, & Jersey, 2000).

Abstract | Introduction | Results | Discussion | Conclusion | Method | References

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