Literature summary for 3.1.3.32 extracted from

Havali-Shahriari, Z.; Weinfeld, M.; Glover, J.N.
Characterization of DNA substrate binding to the phosphatase domain of the DNA repair enzyme polynucleotide kinase/phosphatase (2017), Biochemistry, 56, 1737-1745 .

Search for more literature for 3.1.3.32

Application

Application	Comment	Organism
analysis	fluorescence polarization methods can detect specific binding of single-stranded DNAs with the phosphatase domain, but not specific interactions between the PNKP phosphatase and double-stranded substrates	Mus musculus

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli, full-length enzyme and catalytic domain, i.e. residues 141-522	Mus musculus

Protein Variants

Protein Variants	Comment	Organism
D170A	mutation of the first aspartate of the conserved phosphatase motif, catalytically inactive but structurally intact protein	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q9JLV6	bifunctional polynucleotide phosphatase/kinase, cf. EC 2.7.1.78	-

General Information

General Information	Comment	Organism
physiological function	the phosphatase domain binds 3'-phosphorylated single-stranded DNAs in a manner that is highly dependent on the presence of the 3'-phosphate. Double-stranded substrate binding is not as dependent on the 3'-phosphate. The predicted loss of energy due to base pair disruption upon binding of the phosphatase active site is likely balanced by favorable interactions between the liberated complementary strand and PNKP. The surrounding surfaces of the active site cleft are important in binding to double-stranded substrates	Mus musculus

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Release 2023.1 (January 2023)