According to the literature [2], this enzyme can hydrolyze nucleoside triphosphate (C00201) and nucleoside diphosphate (C00454) in addition to 5'-ribonucleotides (activity of EC 3.1.3.5) and UDP-sugars (activity of EC 3.6.1.45).
Purple Acid Phosphatase; chain A, domain 2
nucleosidediphosphate-sugar pyrophosphatase
nucleosidediphosphate-sugar diphosphatase
mutant S228C, disulfide bridge(C228-C513)
mutant P513C, disulfide bridge C228-C513
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
E. coli 5'-nucleotidase undergoes a hinge-bending domain rotation resembling a ball-and-socket motion.
Cobalt activation of Escherichia coli 5'-nucleotidase is due to zinc ion displacement at only one of two metal-ion-binding sites.
Identification of histidyl and cysteinyl residues essential for catalysis by 5'-nucleotidase.
Kinetic characteristics of nucleoside mono-, di- and triphosphatase activities of the periplasmic 5'-nucleotidase of Escherichia coli.
X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 26-550
X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site.
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; PRODUCT AND INHIBITOR.
Mechanism of hydrolysis of phosphate esters by the dimetal center of 5'-nucleotidase based on crystal structures.
Trapping a 96 degrees domain rotation in two distinct conformations by engineered disulfide bridges.
A large hinge bending domain rotation is necessary for the catalytic function of Escherichia coli 5'-nucleotidase.
The catalytic mechanisms of binuclear metallohydrolases.