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Literature summary extracted from

  • Chen, W.J.; Huang, P.T.; Cheng, Y.C.; Liao, T.H.
    Putative secondary active site of bovine pancreatic deoxyribonuclease I (2008), Protein Pept. Lett., 15, 640-646.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.21.1 additional information His44 may play a critical role in substrate DNA binding in the putative secondary active site, and introduction of sulfhydryl groups at Thr14 and Ser43 may facilitate Mn2+-coordination and further contribute to the catalytic activity of DNase I Bos taurus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.21.1 into vector pET15b and expressed in Escherichia coli strain BL21(DE3)pLysE Bos taurus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.21.1 H44A DNase I activity is similar to that of the wild-type Bos taurus
3.1.21.1 H44D inactive, can only cleave the Mn2+-DNA substrate in a single nicking mode Bos taurus
3.1.21.1 S43A in the presence of Mn2+, as the wild-type, is able to hydrolyze the Mn2+-substrate forming-linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission Bos taurus
3.1.21.1 S43A/H44D inactive, can only cleave the Mn2+-DNA substrate in a single nicking mode Bos taurus
3.1.21.1 S43C in the presence of Mn2+, as the wild-type, is able to hydrolyze the Mn2+-substrate forming-linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission Bos taurus
3.1.21.1 T14A in the presence of Mn2+, as the wild-type, is able to hydrolyze the Mn2+-substrate forming-linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission Bos taurus
3.1.21.1 T14A/H44D inactive, can only cleave the Mn2+-DNA substrate in a single nicking mode Bos taurus
3.1.21.1 T14A/S43A in the presence of Mn2+, though being less active than the wild-type, can still cleave the plasmid DNA in the double scission mode Bos taurus
3.1.21.1 T14A/S43A/H44D inactive Bos taurus
3.1.21.1 T14A/S43C DNase I activity is similar to that of the wild-type Bos taurus
3.1.21.1 T14C in the presence of Mn2+, as the wild-type, is able to hydrolyze the Mn2+-substrate forming-linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission Bos taurus
3.1.21.1 T14C/H44D significant increase in DNase I activity Bos taurus
3.1.21.1 T14C/S43A DNase I activity is similar to that of the wild-type Bos taurus
3.1.21.1 T14C/S43A/H44D significant increase in DNase I activity Bos taurus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.21.1 Ca2+
-
Bos taurus
3.1.21.1 Mg2+ in the presence of Mg2+ only, the wild-type cleaves the Mg2+-DNA substrate in a single nicking mode with the formation of only the relaxed open-circular DNA Bos taurus
3.1.21.1 Mn2+ in the presence of Mn2+, the wild-type is able to hydrolyze the Mn2+-substrate forming-linear duplex DNA in addition to the relaxed open-circular DNA, indicating double scission Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
3.1.21.1 Bos taurus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.21.1 to homogeneity Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.21.1 pancreas
-
Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.21.1 calf thymus DNA + H2O
-
Bos taurus 5'-phosphooligonucleotides + ?
-
?
3.1.21.1 plasmid DNA + H2O
-
Bos taurus ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.1.21.1 DNase I
-
Bos taurus