A Mixed-Valent, Unsymmetrical FeIIFeIII Complex with a Terminal Phenolato Ligand as a Model for the Active Site of Purple Acid Phosphatases

1994 ◽  
Vol 33 (8) ◽  
pp. 887-889 ◽  
Author(s):  
Elisabeth Bernard ◽  
William Moneta ◽  
Jean Laugier ◽  
Sylvie Chardon-Noblat ◽  
Alain Deronzier ◽  
...  
Keyword(s):  
Active Site ◽  
Acid Phosphatases ◽  
Purple Acid Phosphatases

Mutational Analysis of the Interaction between Active Site Residues and the Loop Region in Mammalian Purple Acid Phosphatases†

Biochemistry ◽  
2001 ◽  
Vol 40 (38) ◽  
pp. 11614-11622 ◽  
Author(s):  
Enrico G. Funhoff ◽  
Jenny Ljusberg ◽  
Yunling Wang ◽  
Goran Andersson ◽  
Bruce A. Averill
Keyword(s):  
Active Site ◽  
Mutational Analysis ◽  
Acid Phosphatases ◽  
Active Site Residues ◽  
Loop Region ◽  
Purple Acid Phosphatases

scholarly journals MODELS FOR THE ACTIVE SITE STRUCTURE OF PURPLE ACID PHOSPHATASES

1996 ◽  
Vol 4 (4) ◽  
pp. 19-26
Author(s):  
Marcos Aires de Brito
Keyword(s):  
Active Site ◽  
Bioinorganic Chemistry ◽  
Review Article ◽  
Acid Phosphatases ◽  
Site Structure ◽  
Purple Acid Phosphatases ◽  
Active Site Structure

This review article examines the current and most relevant models proposed for purple acid phosphatases (PAPs). It also presents a new possibility for the active site structure of mammalian PAPs based on the work that we and other researchers have done in bioinorganic chemistry.

FeIIIFeIIIand FeIIFeIIIComplexes as Synthetic Analogues for the Oxidized and Reduced Forms of Purple Acid Phosphatases

1996 ◽  
Vol 35 (8) ◽  
pp. 2360-2368 ◽  
Author(s):  
Ademir Neves ◽  
Marcos A. de Brito ◽  
Ivo Vencato ◽  
Valderes Drago ◽  
Klaus Griesar ◽  
...  
Keyword(s):  
Acid Phosphatases ◽  
Synthetic Analogues ◽  
Purple Acid Phosphatases ◽  
Reduced Forms

scholarly journals Systematic synthesis of functional unsymmetric FeZn model complexes for plant purple acid phosphatases

2010 ◽  
Vol 13 (3) ◽  
pp. 334-337 ◽  
Author(s):  
Martin Jarenmark ◽  
Håkan Carlsson ◽  
Vladimir M. Trukhan ◽  
Matti Haukka ◽  
Sophie E. Canton ◽  
...  
Keyword(s):  
Acid Phosphatases ◽  
Model Complexes ◽  
Purple Acid Phosphatases ◽  
Systematic Synthesis

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

2003 ◽  
Vol 50 (4) ◽  
pp. 1245-1256 ◽  
Author(s):  
Mariusz Olczak ◽  
Bronisława Morawiecka ◽  
Wiesław Watorek
Keyword(s):  
Disulfide Bridge ◽  
Acid Phosphatases ◽  
Amino Acid Residues ◽  
Disulfide Bridges ◽  
Inorganic Pyrophosphate ◽  
Manganese Ion ◽  
Substrate Preferences ◽  
Purple Acid Phosphatases ◽  
Single Polypeptide ◽  
Monomeric Proteins

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.

Studies on Model Compound of Purple Acid Phosphatases Hydrolysis of ATP

1997 ◽  
Vol 13 (07) ◽  
pp. 643-646
Author(s):  
Wang Tian-Zhi ◽  
◽  
Wu Ding-Quan ◽  
Huang Zai-Yin ◽  
Qu Song-Sheng ◽  
...  
Keyword(s):  
Model Compound ◽  
Acid Phosphatases ◽  
Purple Acid Phosphatases ◽  
Hydrolysis Of

scholarly journals Electronic Structure and Spectro-Structural Correlations of FeIIIZnIIBiomimetics for Purple Acid Phosphatases: Relevance to DNA Cleavage and Cytotoxic Activity

2010 ◽  
Vol 49 (24) ◽  
pp. 11421-11438 ◽  
Author(s):  
Rosely A. Peralta ◽  
Adailton J. Bortoluzzi ◽  
Bernardo de Souza ◽  
Rafael Jovito ◽  
Fernando R. Xavier ◽  
...  
Keyword(s):  
Electronic Structure ◽  
Cytotoxic Activity ◽  
Dna Cleavage ◽  
Acid Phosphatases ◽  
Purple Acid Phosphatases

scholarly journals A new heterobinuclear FeIIICuII complex with a single terminal FeIII–O(phenolate) bond. Relevance to purple acid phosphatases and nucleases

2005 ◽  
Vol 10 (4) ◽  
pp. 319-332 ◽  
Author(s):  
Mauricio Lanznaster ◽  
Ademir Neves ◽  
Adailton J. Bortoluzzi ◽  
Veronika V. E. Aires ◽  
Bruno Szpoganicz ◽  
...  
Keyword(s):  
Acid Phosphatases ◽  
Purple Acid Phosphatases

Vanadate-Containing Haloperoxidases and Acid Phosphatases: The Conserved Active Site

1998 ◽  
pp. 216-227 ◽  
Author(s):  
Wieger Hemrika ◽  
Rokus Renirie ◽  
Henk Dekker ◽  
Ron Wever
Keyword(s):  
Active Site ◽  
Acid Phosphatases
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