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

Schenk, Gerhard and Gahan, Lawrence R. and Carrington, Lyle E. and Mitic, Natasa and Valizadeh, Mohsen and Hamilton, Susan E. and de Jersey, John and Guddat, Luke W. (2005) Phosphate forms an unusual tripodal complex with the Fe–Mn center of sweet potato purple acid phosphatase. Proceedings of the National Academy of Sciences , 102 (2). pp. 273-278. ISSN 1091-6490

[img] Download (408kB)

Share your research

Twitter Facebook LinkedIn GooglePlus Email more...

Add this article to your Mendeley library


Purple acid phosphatases (PAPs) are a family of binuclear metalloenzymes that catalyze the hydrolysis of phosphoric acid esters and anhydrides. A PAP in sweet potato has a unique, strongly antiferromagnetically coupled Fe(III)–Mn(II) center and is distinguished from other PAPs by its increased catalytic efficiency for a range of activated and unactivated phosphate esters, its strict requirement for Mn(II), and the presence of a -oxo bridge at pH 4.90. This enzyme displays maximum catalytic efficiency (kcatKm) at pH 4.5, whereas its catalytic rate constant (kcat) is maximal at near-neutral pH, and, in contrast to other PAPs, its catalytic parameters are not dependent on the pKa of the leaving group. The crystal structure of the phosphate-bound Fe(III)–Mn(II) PAP has been determined to 2.5-Å resolution (final Rfree value of 0.256). Structural comparisons of the active site of sweet potato, red kidney bean, and mammalian PAPs show several amino acid substitutions in the sweet potato enzyme that can account for its increased catalytic efficiency. The phosphate molecule binds in an unusual tripodal mode to the two metal ions, with two of the phosphate oxygen atoms binding to Fe(III) and Mn(II), a third oxygen atom bridging the two metal ions, and the fourth oxygen pointing toward the substrate binding pocket. This binding mode is unique among the known structures in this family but is reminiscent of phosphate binding to urease and of sulfate binding to protein phosphatase. The structure and kinetics support the hypothesis that the bridging oxygen atom initiates hydrolysis.

Item Type: Article
Additional Information: Postprint version of original published article. The original article is available at . DOI: 10.1073/pnas.0407239102
Keywords: binuclear metal center; phosphate coordination; tripodal complex; acid phosphatase;
Academic Unit: Faculty of Science and Engineering > Chemistry
Item ID: 3668
Depositing User: Gary Schenk
Date Deposited: 16 May 2012 15:42
Journal or Publication Title: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Refereed: Yes

Repository Staff Only(login required)

View Item Item control page

Document Downloads

More statistics for this item...