Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/5198
Title: Biochemical characterization of the class B acid phosphatase (AphA) of Escherichia coli MG1655
Authors: C., Passariello
C., Forleo
V., Micheli
S., Schippa
R., Leone
Mangani, Stefano 
M. C., Thaller
Rossolini, GIAN MARIA
Keywords: phosphatase; magnesium; kinetics; mechanism
Issue Date: 2006
Project: None 
Journal: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Abstract: 
The AphA enzyme of Escherichia coli, a molecular class B periplasmic phosphatase that belongs to the DDDD superfamily of phosphohydrolases, was purified and subjected to biochemical characterization. Kinetic analysis with several substrates revealed that the enzyme essentially behaves as a broad-spectrum nucleotidase highly active on 3'- and 5'-mononucleotides and monodeoxynucleotides, but not active on cyclic nucleotides, or nucleotides di- and triphosphate. Mononucleotides are degraded to nucleosides, and AphA apparently does not exhibit any nucleotide phosphomutase activity. However, it can transphosphorylate nucleosides in the presence of phosphate donors. Kinetic properties of AphA are consistent with structural data, and suggest a role for the hydrophobic pocket present in the active site crevice, made by residues Phe 56, Leu71, Trp77 and Tyr193, in conferring preferential substrate specificity by accommodating compounds with aromatic rings. AphA was inhibited by several chelating agents, including EDTA, EGTA, 1,10-phenanthroline and dipicolinic acid, with EDTA being apparently the most powerful inhibitor. (c) 2005 Elsevier B.V. All rights reserved.
Description: 
47931
URI: http://hdl.handle.net/20.500.12779/5198
ISSN: 1570-9639
DOI: 10.1016/j.bbapap.2005.08.028
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