Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Joshi, H.K.; Etzkorn, C.; Chatwell, L.; Bitinaite, J.; Horton, N.C.
    Alteration of sequence specificity of the type II restriction endonuclease HincII through an indirect readout mechanism (2006), J. Biol. Chem., 281, 23852-23869.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.21.4 crystal structures of mutant enzyme Q138F bound to GTTAAC, GTCGAC both with and without Ca2+, as well as the structure of the wild-type HincII bound to GTTAAC Haemophilus influenzae

Protein Variants

EC Number Protein Variants Comment Organism
3.1.21.4 Q138F mutation results in a change in the sequence specificity at the center two base pairs of the cognate recognition site. Alteration in preference of HicII for cutting, but not binding, the three cognate sites differening in the center two base pairs.The Q138F HincII/DNA crystal structures show conformational changes in the protein, bound DNA, and at the protein-DNA interface Haemophilus influenzae

Organism

EC Number Organism UniProt Comment Textmining
3.1.21.4 Haemophilus influenzae P17743
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.21.4 wild-type and mutant enzymes Haemophilus influenzae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.21.4 DNA + H2O
-
 Haemophilus influenzae double-stranded DNA fragments with terminal 5'-phosphates
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.21.4 HincII
-
 Haemophilus influenzae