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Literature summary extracted from

  • Miyazono, K.I.; Ishino, S.; Makita, N.; Ito, T.; Ishino, Y.; Tanokura, M.
    Crystal structure of the novel lesion-specific endonuclease PfuEndoQ from Pyrococcus furiosus (2018), Nucleic Acids Res., 46, 4807-4818 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.21.B1 expression in Escherichia coli Pyrococcus furiosus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.21.B1 sitting-drop vapour-diffusion method at 4°C Pyrococcus furiosus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.21.B1 D193N endonuclease activity is almost abolished Pyrococcus furiosus
3.1.21.B1 E76Q endonuclease activity is almost abolished Pyrococcus furiosus
3.1.21.B1 H10A mutant enzyme retaines approximately half of the wild-type endonuclease activity Pyrococcus furiosus
3.1.21.B1 H139A endonuclease activity is almost abolished Pyrococcus furiosus
3.1.21.B1 H84A endonuclease activity is almost abolished Pyrococcus furiosus
3.1.21.B1 H8A mutant enzyme retaines approximately half of the wild-type endonuclease activity Pyrococcus furiosus
3.1.21.B1 K320A decreased dsDNA-binding ability Pyrococcus furiosus
3.1.21.B1 W144A mutant enzyme with decreased activity Pyrococcus furiosus
3.1.21.B1 Y244A mutant shows reduced DNA cleavage activity for the hypoxanthine-containing DNA Pyrococcus furiosus
3.1.21.B1 Y244F mutant enzyme cleaves the same DNA more effectively than the wild-type enzyme Pyrococcus furiosus
3.1.21.B1 Y377A mutant enzyme cleaves the same DNA more effectively than the wild-type enzyme Pyrococcus furiosus
3.1.21.B1 Y377F mutant enzyme cleaves the same DNA more effectively than the wild-type enzyme Pyrococcus furiosus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.21.B1 Zn2+ PfuEndoQ recognizes a deaminated base using a highly conserved pocket adjacent to a Zn2+-binding site and hydrolyses a phosphodiester bond using two Zn2+ ions. The PfuEndoQ-DNA complex is stabilized by a Zn-binding domain and a C-terminal helical domain, and the complex may recruit downstream proteins in the DNA repair pathway Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
3.1.21.B1 Pyrococcus furiosus Q8U0N5
-
-
3.1.21.B1 Pyrococcus furiosus ATCC 43587 Q8U0N5
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.21.B1
-
 Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.21.B1 double-stranded DNA + H2O the enzyme recognizes a deaminated base in double-stranded DNA and cleaves the phosphodiester bond 5' of the lesion site Pyrococcus furiosus ?
-
 ?
3.1.21.B1 double-stranded DNA + H2O the enzyme recognizes a deaminated base in double-stranded DNA and cleaves the phosphodiester bond 5' of the lesion site Pyrococcus furiosus ATCC 43587 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.21.B1 PfuEndoQ
-
 Pyrococcus furiosus

General Information

EC Number General Information Comment Organism
3.1.21.B1 physiological function the enzyme may be involved in the DNA repair pathway Pyrococcus furiosus