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Literature summary for 3.1.21.4 extracted from

  • Cymerman, I.A.; Obarska, A.; Skowronek, K.J.; Lubys, A.; Bujnicki, J.M.
    Identification of a new subfamily of HNH nucleases and experimental characterization of a representative member, HphI restriction endonuclease (2006), Proteins, 65, 867-876.
    View publication on PubMed
Search for more literature for 3.1.21.4

Crystallization (Commentary)

Crystallization (Comment) Organism
three-dimensional model of the enzyme's catalytic domain Haemophilus parahaemolyticus

Protein Variants

Protein Variants Comment Organism
D317A 84% of DNA binding compared to wild-type Haemophilus parahaemolyticus
D321A 119% of DNA binding compared to wild-type Haemophilus parahaemolyticus
D328A 76% of DNA binding compared to wild-type Haemophilus parahaemolyticus
D329A 123% of DNA binding compared to wild-type Haemophilus parahaemolyticus
H291A 96% of DNA binding compared to wild-type Haemophilus parahaemolyticus
H368A 129% of DNA binding compared to wild-type Haemophilus parahaemolyticus
N308A 104% of DNA binding compared to wild-type Haemophilus parahaemolyticus

Organism

Organism UniProt Comment Textmining
Haemophilus parahaemolyticus
-
 isoform HphI
-

Reaction

Reaction Comment Organism Reaction ID
endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates residue H291 is the direct catalytic residue, N308 is important for the structural integrity of the betabetaalpha motif, while D317 and D321 are involved in metal ion binding Haemophilus parahaemolyticus
a