Literature summary for 3.1.21.4 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.

Search for more literature for 3.1.21.4

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Protein Variants	Comment	Organism
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

Organism	UniProt	Comment	Textmining
Haemophilus influenzae	P17743	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
HincII	-	Haemophilus influenzae

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Release 2023.1 (January 2023)