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Literature summary for 3.1.21.B1 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
Search for more literature for 3.1.21.B1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pyrococcus furiosus

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapour-diffusion method at 4°C Pyrococcus furiosus

Protein Variants

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

Metals/Ions

Metals/Ions Comment Organism Structure
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

Organism UniProt Comment Textmining
Pyrococcus furiosus Q8U0N5
-
-
Pyrococcus furiosus ATCC 43587 Q8U0N5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus furiosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
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

Synonyms Comment Organism
PfuEndoQ
-
 Pyrococcus furiosus

General Information

General Information Comment Organism
physiological function the enzyme may be involved in the DNA repair pathway Pyrococcus furiosus