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Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.21.4
-
 Haemophilus influenzae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.21.4 hanging-drop method Haemophilus influenzae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.21.4 28000
-
 gel filtration Haemophilus influenzae

Organism

EC Number Organism UniProt Comment Textmining
3.1.21.4 Haemophilus influenzae
-
 recombinant
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.21.4
-
 Haemophilus influenzae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.21.4 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

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

Synonyms

EC Number Synonyms Comment Organism
3.1.21.4 HinP1I
-
 Haemophilus influenzae