Plant purple acid phosphatases - genes, structures and biological function.
نویسندگان
چکیده
منابع مشابه
Plant purple acid phosphatases - genes, structures and biological function.
The properties of plant purple acid phosphatases (PAPs), metallophosphoesterases present in some bacteria, plants and animals are reviewed. All members of this group contain a characteristic set of seven amino-acid residues involved in metal ligation. Animal PAPs contain a binuclear metallic center composed of two irons, whereas in plant PAPs one iron ion is joined by zinc or manganese ion. Amo...
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Mammalian and plant purple acid phosphatases have similar active site structures despite low sequence identity (<20%). Although no bacterial enzyme has been purified, a sequence database search revealed that genes that could encode potential purple acid phosphatases may be restricted to a small number of organisms (i.e. myco- and cyanobacteria). Analysis of their deduced amino acid sequences an...
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Purple acid phosphatases (PAPs) are dinuclear monoesterases1,2 that are structurally diverse but with a conserved set of ligands to the Fe3+-M2+ metal centers (M2+ ) Fe, Zn, or Mn).3 The identity of the nucleophile and the substrate binding mode have been matters of controversy (Figure 1).1,3-5 In one proposal, substrate binds to the divalent metal and is attacked by a terminal Fe3+-bound hydro...
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Purple acid phosphatases are metal-containing hydrolases. While their precise biological role(s) is unknown, the mammalian enzyme has been linked in a variety of biological circumstances (e.g., osteoporosis) with increased bone resorption. Inhibition of the human enzyme is a possible strategy for the treatment of bone-resorptive diseases such as osteoporosis. Previously, we determined the cryst...
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ژورنال
عنوان ژورنال: Acta Biochimica Polonica
سال: 2003
ISSN: 1734-154X,0001-527X
DOI: 10.18388/abp.2003_3648