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2003 | 50 | 4 | 1245-1256
Article title

Plant purple acid phosphatases - genes, structures and biological function.

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EN
Abstracts
EN
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. Among plant PAPs two groups can be distinguished: small PAPs, monomeric proteins with molecular mass around 35 kDa, structurally close to mammalian PAPs, and large PAPs, homodimeric proteins with a single polypeptide of about 55 kDa. Large plant PAPs exhibit two types of structural organization. One type comprises enzymes with subunits bound by a disulfide bridge formed by cysteines located in the C-terminal region around position 350. In the second type no cysteines are located in this position and no disulfide bridges are formed between subunits. Differences in structural organisation are reflected in substrate preferences. Recent data reveal in plants the occurrence of metallophosphoesterases structurally different from small or large PAPs but with metal-ligating sequences characteristic for PAPs and expressing pronounced specificity towards phytate or diphosphate nucleosides and inorganic pyrophosphate.
Publisher

Year
Volume
50
Issue
4
Pages
1245-1256
Physical description
Dates
published
2003
received
2003-08-28
revised
2003-11-17
accepted
2003-11-27
Contributors
  • Institute of Biochemistry and Molecular Biology, Wrocław University, Wrocław, Poland
  • Institute of Biochemistry and Molecular Biology, Wrocław University, Wrocław, Poland
  • Institute of Biochemistry and Molecular Biology, Wrocław University, Wrocław, Poland
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv50i4p1245kz
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