LOC56985 abstract: Difference between revisions
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LOC56985 is a hypothetical protein coded by the gene C17orf48 in humans. We have inferred structural, evolutionary, and functional characteristics of LOC56985 using bioinformatic analysis. Sequence analysis identified LOC56985 as a metallophosphoesterase with high similarity orthologs present in vertebrates and plants. Structural studies, utilising the x-ray structure of | LOC56985 is a hypothetical protein coded by the gene C17orf48 in humans. We have inferred structural, evolutionary, and functional characteristics of LOC56985 using bioinformatic analysis. Sequence analysis identified LOC56985 as a metallophosphoesterase with high similarity orthologs present in vertebrates and plants. Structural studies, utilising the x-ray structure of an ortholog from zebra fish, indicates that LOC56985 is most likely a purple acid phosphatase (PAP). PAPs are binuclear metallohydrolases which catalyse hydrolysis of phosphate esters and other anhydrides under acidic conditions. Genomic analysis indicates the restriction of genes encoding potential PAPs to organisms above and including cyanobacteria and mycobacteria in the tree of life. Distantly related PAPs show poor sequence similarities, but retain the characteristic fold organisation and residues critical for active site structure and function. | ||
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Revision as of 03:42, 30 May 2008
LOC56985 is a hypothetical protein coded by the gene C17orf48 in humans. We have inferred structural, evolutionary, and functional characteristics of LOC56985 using bioinformatic analysis. Sequence analysis identified LOC56985 as a metallophosphoesterase with high similarity orthologs present in vertebrates and plants. Structural studies, utilising the x-ray structure of an ortholog from zebra fish, indicates that LOC56985 is most likely a purple acid phosphatase (PAP). PAPs are binuclear metallohydrolases which catalyse hydrolysis of phosphate esters and other anhydrides under acidic conditions. Genomic analysis indicates the restriction of genes encoding potential PAPs to organisms above and including cyanobacteria and mycobacteria in the tree of life. Distantly related PAPs show poor sequence similarities, but retain the characteristic fold organisation and residues critical for active site structure and function.
Abstract | Introduction | Results | Discussion | Conclusion | Method | References
