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Literature summary extracted from
- Pancreatic DNase (1981), The Enzymes, 3rd Ed. (Boyer, P. D. , ed. ), 14, 281-296.
No PubMed abstract available
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.1.21.1 | analysis | study of chromatin structure, visualizing cellular microfilaments by DNase I-actin interaction | Bos taurus |
| 3.1.21.1 | medicine | inhibition of viral synthesis by DNase I in cell cultures | Bos taurus |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 3.1.21.1 | extremely sensitive to inactivation by proteases in the absence of Ca2+ | Bos taurus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.21.1 | 2-Nitro-5-thiocyanobenzoic acid | inactivation by cleavage of peptide chain at positions 14, 40, 72 and 135 | Bos taurus |  |
| 3.1.21.1 | Ca2+ | inhibitory above 1 mM | Bos taurus | |
| 3.1.21.1 | carbodiimide | presence of divalent cations slows the rate of inactivation | Bos taurus | |
| 3.1.21.1 | EGTA | inhibition at 0.01 mM in the presence of 2.5 mM Mg2+ | Bos taurus | |
| 3.1.21.1 | G-actin | DNase I causes depolymerization of F-actin to form a stable complex of 1 mol DNase I with 1 mol G-actin, this complex inhibits DNase I activity | Bos taurus | |
| 3.1.21.1 | iodoacetate | inhibition in the presence of Mn2+ or Ca2+ at pH 7.2 | Bos taurus | |
| 3.1.21.1 | methanesulfonylchloride | inactivation at pH 5.0 | Bos taurus | |
| 3.1.21.1 | N-bromosuccinimide | inactivation by modification at Trp155 | Bos taurus | |
| 3.1.21.1 | NaCl | Na-DNA is inhibitory | Bos taurus | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.21.1 | Ba2+ | can substitute for Ca2+, but less effective | Bos taurus | |
| 3.1.21.1 | Ca2+ | resistance to proteolysis conveyed by Ca2+ | Bos taurus | |
| 3.1.21.1 | Ca2+ | activation synergistic with Mg2+ | Bos taurus | |
| 3.1.21.1 | Co2+ | can substitute for Mg2+, but only 10% efficiency | Bos taurus | |
| 3.1.21.1 | Mg2+ | enzyme about 99.5% inactive if Ca2+ contamination is reduced to a minimum, must bind to the substrate, whereas Ca2+ must bind to the enzyme | Bos taurus | |
| 3.1.21.1 | Mn2+ | can substitute for Mg2+ | Bos taurus | |
| 3.1.21.1 | Sr2+ | can substitute for Ca2+, but less effective | Bos taurus | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.1.21.1 | 30070 | - |
calculated from amino acid and carbohydrate composition for DNase A | Bos taurus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.21.1 | double-stranded DNA + H2O | Bos taurus | double-strand scission obtained if affinity for the substrate is at a maximum in the presence of both Ca2+ and Mg2+, single-strand scission and changes in specificity are associated with suboptimal concentrations of Ca2+ | 5'-phosphooligonucleotides + ? | in the presence of divalent cations that give less maximum activity consistent yields of long oligonucleotides lacking dA at the 3'-end | ? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.21.1 | Bos taurus | - |
4 active compounds: A, B, C, D | - |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.1.21.1 | glycoprotein | DNase D contains sialic acid in the carbohydrate portion | Bos taurus |
| 3.1.21.1 | glycoprotein | carbohydrate-chain at Asn 18 | Bos taurus |
| 3.1.21.1 | glycoprotein | DNase A with a neutral carbohydrate side-chain, DNase B with a sialic acid carbohydrate side-chain | Bos taurus |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.21.1 | conconavalin A-agarose as an effective step for DNases with neutral carbohydrate side-chains, preparing a protease free DNase I | Bos taurus |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 3.1.21.1 | 37°C, protease free preparation, absence of Ca2+, pH 8.0, more than 10 days | Bos taurus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.21.1 | crab d(A-T) polymer + H2O | unique polymer of alterating A and T contains about 3% G and C residues integrated into its structure | Bos taurus | 5'-hexanucleotides + ? | enriched in C and G, sugar specificity may be limited to the nucleotide following the point of cleavage | ? | |
| 3.1.21.1 | double-stranded DNA + H2O | double-strand scission obtained if affinity for the substrate is at a maximum in the presence of both Ca2+ and Mg2+, single-strand scission and changes in specificity are associated with suboptimal concentrations of Ca2+ | Bos taurus | 5'-phosphooligonucleotides + ? | in the presence of divalent cations that give less maximum activity consistent yields of long oligonucleotides lacking dA at the 3'-end | ? | |
| 3.1.21.1 | NO2-Ph-pdTp-NO2Ph + H2O | rapidly hydrolyzed at a single bond | Bos taurus | p-nitrophenol + NO2-Ph-pdT-3'-phosphate | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.21.1 | DNase A | - |
Bos taurus |
| 3.1.21.1 | DNase B | - |
Bos taurus |
| 3.1.21.1 | DNase C | - |
Bos taurus |
| 3.1.21.1 | DNase D | - |
Bos taurus |
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Release 2023.1 (January 2023)
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