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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.
    View publication on PubMed
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