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.

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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

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Release 2023.1 (January 2023)