Literature summary for 3.1.21.4 extracted from

Yang, Z.; Horton, J.R.; Maunus, R.; Wilson, G.G.; Roberts, R.J.; Cheng, X.
Structure of HinP1I endonuclease reveals a striking similarity to the monomeric restriction enzyme MspI (2005), Nucleic Acids Res., 33, 1892-1901.

Search for more literature for 3.1.21.4

Cloned(Commentary)

Cloned (Comment)	Organism
-	Haemophilus influenzae

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging-drop method	Haemophilus influenzae

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
28000	-	gel filtration	Haemophilus influenzae

Organism

Organism	UniProt	Comment	Textmining
Haemophilus influenzae	-	recombinant	-

Purification (Commentary)

Purification (Comment)	Organism
-	Haemophilus influenzae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
DNA + H2O	HinP1I recognizes and cleaves a palindromic tetranucleotide sequence (G-/-CGC) in double-stranded DNA, producing 2 nt 5' overhanging ends	Haemophilus influenzae	double-stranded DNA fragments with terminal 5'-phosphates	-	?

Subunits

Subunits	Comment	Organism
monomer	1 * 28000, the enzyme can form a dimer or a higher order molecule weight complex at high protein concentrations	Haemophilus influenzae

Synonyms

Synonyms	Comment	Organism
HinP1I	-	Haemophilus influenzae

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Release 2023.1 (January 2023)