scholarly journals Metal-Ion Mutagenesis: Conversion of a Purple Acid Phosphatase from Sweet Potato to a Neutral Phosphatase with the Formation of an Unprecedented Catalytically Competent MnIIMnIIActive Site

2009 ◽  
Vol 131 (23) ◽  
pp. 8173-8179 ◽  
Author(s):  
Nataša Mitić ◽  
Christopher J. Noble ◽  
Lawrence R. Gahan ◽  
Graeme R. Hanson ◽  
Gerhard Schenk
Keyword(s):  
Acid Phosphatase ◽  
Sweet Potato ◽  
Metal Ion ◽  
Purple Acid Phosphatase

scholarly journals A Purple Acid Phosphatase from Sweet Potato Contains an Antiferromagnetically Coupled Binuclear Fe-Mn Center

2001 ◽  
Vol 276 (22) ◽  
pp. 19084-19088 ◽  
Author(s):  
Gerhard Schenk ◽  
Clare L. Boutchard ◽  
Lyle E. Carrington ◽  
Christopher J. Noble ◽  
Boujemaa Moubaraki ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Sweet Potato ◽  
Purple Acid Phosphatase

Crystal structure and mechanism of a purple acid phosphatase from sweet potato: an enzyme with a novel FeMn binuclear metal centre

2003 ◽  
Vol 96 (1) ◽  
pp. 225
Author(s):  
Gerhard Schenk ◽  
Lyle E. Carrington ◽  
Mohsen Valizadeh ◽  
John de Jersey ◽  
Susan E. Hamilton ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Acid Phosphatase ◽  
Sweet Potato ◽  
Purple Acid Phosphatase ◽  
Metal Centre ◽  
Binuclear Metal

scholarly journals Recombinant purple acid phosphatase isoform 3 from sweet potato is an enzyme with a diiron metal center

FEBS Journal ◽  
2006 ◽  
Vol 273 (8) ◽  
pp. 1649-1659 ◽  
Author(s):  
Teerawit Waratrujiwong ◽  
Bernt Krebs ◽  
Friedrich Spener ◽  
Pornsawan Visoottiviseth
Keyword(s):  
Acid Phosphatase ◽  
Sweet Potato ◽  
Metal Center ◽  
Purple Acid Phosphatase

scholarly journals Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet potato purple acid phosphatase

2004 ◽  
Vol 102 (2) ◽  
pp. 273-278 ◽  
Author(s):  
G. Schenk ◽  
L. R. Gahan ◽  
L. E. Carrington ◽  
N. Mitic ◽  
M. Valizadeh ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Sweet Potato ◽  
Purple Acid Phosphatase

scholarly journals Crystallization and preliminary X-ray diffraction data for a purple acid phosphatase from sweet potato

1999 ◽  
Vol 55 (12) ◽  
pp. 2051-2052 ◽  
Author(s):  
Gerhard Schenk ◽  
Lyle E. Carrington ◽  
Susan E. Hamilton ◽  
John de Jersey ◽  
Luke W. Guddat
Keyword(s):  
Acid Phosphatase ◽  
Sweet Potato ◽  
Diffraction Data ◽  
Three Dimensional ◽  
Purple Acid Phosphatase ◽  
Dimensional Structure ◽  
X Ray Diffraction ◽  
X Ray ◽  
Cell Parameters ◽  
The Subject

Purple acid phosphatase from sweet potato is a homodimer of 110 kDa. Two forms of the enzyme have been characterized. One contains an Fe–Zn centre similar to that previously reported for red kidney bean purple acid phosphatase. Another isoform, the subject of this work, is the first confirmed example of an Fe–Mn-containing enzyme. Crystals of this protein have been grown from PEG 6000. They have unit-cell parameters a = b = 118.4, c = 287.4 Å and have the symmetry of space group P6522, with one dimer per asymmetric unit. Diffraction data collected using a conventional X-ray source from a cryocooled crystal extend to 2.90 Å resolution. The three-dimensional structure of the enzyme will provide insight into the coordination of this novel binuclear metal centre.

scholarly journals Acylated Anthocyanins from Red Cabbage and Purple Sweet Potato Can Bind Metal Ions and Produce Stable Blue Colors

2021 ◽  
Vol 22 (9) ◽  
pp. 4551
Author(s):  
Julie-Anne Fenger ◽  
Gregory T. Sigurdson ◽  
Rebecca J. Robbins ◽  
Thomas M. Collins ◽  
M. Mónica Giusti ◽  
...  
Keyword(s):  
Metal Ions ◽  
Sweet Potato ◽  
Metal Binding ◽  
Metal Ion ◽  
High Resolution Mass Spectrometry ◽  
Large Set ◽  
Water Addition ◽  
Red Cabbage ◽  
Aluminum Ions ◽  
Purple Sweet Potato

Red cabbage (RC) and purple sweet potato (PSP) are naturally rich in acylated cyanidin glycosides that can bind metal ions and develop intramolecular π-stacking interactions between the cyanidin chromophore and the phenolic acyl residues. In this work, a large set of RC and PSP anthocyanins was investigated for its coloring properties in the presence of iron and aluminum ions. Although relatively modest, the structural differences between RC and PSP anthocyanins, i.e., the acylation site at the external glucose of the sophorosyl moiety (C2-OH for RC vs. C6-OH for PSP) and the presence of coordinating acyl groups (caffeoyl) in PSP anthocyanins only, made a large difference in the color expressed by their metal complexes. For instance, the Al3+-induced bathochromic shifts for RC anthocyanins reached ca. 50 nm at pH 6 and pH 7, vs. at best ca. 20 nm for PSP anthocyanins. With Fe2+ (quickly oxidized to Fe3+ in the complexes), the bathochromic shifts for RC anthocyanins were higher, i.e., up to ca. 90 nm at pH 7 and 110 nm at pH 5.7. A kinetic analysis at different metal/ligand molar ratios combined with an investigation by high-resolution mass spectrometry suggested the formation of metal–anthocyanin complexes of 1:1, 1:2, and 1:3 stoichiometries. Contrary to predictions based on steric hindrance, acylation by noncoordinating acyl residues favored metal binding and resulted in complexes having much higher molar absorption coefficients. Moreover, the competition between metal binding and water addition to the free ligands (leading to colorless forms) was less severe, although very dependent on the acylation site(s). Overall, anthocyanins from purple sweet potato, and even more from red cabbage, have a strong potential for development as food colorants expressing red to blue hues depending on pH and metal ion.

Synthesis, Structural, Magnetic, and Redox Properties of Asymmetric Diiron Complexes with a Single Terminally Bound Phenolate Ligand. Relevance to the Purple Acid Phosphatase Enzymes

1997 ◽  
Vol 119 (40) ◽  
pp. 9424-9437 ◽  
Author(s):  
Elisabeth Lambert ◽  
Barbara Chabut ◽  
Sylvie Chardon-Noblat ◽  
Alain Deronzier ◽  
Geneviève Chottard ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Redox Properties ◽  
Purple Acid Phosphatase
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