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Literature summary for 3.1.21.1 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

Activating Compound Comment Organism Structure
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)

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

Protein Variants

Protein Variants Comment Organism
H44A DNase I activity is similar to that of the wild-type Bos taurus
H44D inactive, can only cleave the Mn2+-DNA substrate in a single nicking mode Bos taurus
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
S43A/H44D inactive, can only cleave the Mn2+-DNA substrate in a single nicking mode Bos taurus
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
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
T14A/H44D inactive, can only cleave the Mn2+-DNA substrate in a single nicking mode Bos taurus
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
T14A/S43A/H44D inactive Bos taurus
T14A/S43C DNase I activity is similar to that of the wild-type Bos taurus
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
T14C/H44D significant increase in DNase I activity Bos taurus
T14C/S43A DNase I activity is similar to that of the wild-type Bos taurus
T14C/S43A/H44D significant increase in DNase I activity Bos taurus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+
-
Bos taurus
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
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

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
to homogeneity Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
Bos taurus
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
DNase I
-
Bos taurus