| Description | This entry represents the DNase I conserved site that is involved in disulphide bond formation. It has the consensus pattern G-D-F-N-A-x-C-[SAK].Deoxyribonuclease I (DNase I) ( ) [ ] is a vertebrate enzyme which catalyzes the endonucleolytic cleavage of double-stranded DNA to 5'- phosphodinucleotide and 5'-phosphooligonucleotide end-products. DNase I is an enzyme involved in DNA degradation; it is normally secreted outside of the cell but seems to be able to gain access to the nucleus where it is involved in cell death by apoptosis [].As shown in the following schematic representation, DNase I is a glycoprotein of about 260 residues with two conserved disulphide bonds.+-+ +--------+ | | | |xxxxxxxxxxxxxxxxx#xxxxxxCxCxxxxx#xxxxxxxxxCxxxxxxxxCxxxxxxxxxxxxx 'C': conserved cysteine involved in a disulphide bond. '#': active site residue.DNase I has a pH-optimum around 7.5 and requires calcium and magnesium for full activity. It causes single strand nicks in duplex DNA. A proton acceptor-donor chain composed of a histidine and a glutamic acid produce a nucleophilic hydroxyl ion from water, which cleaves the 3'-P-O bond [ ]. DNase I forms a 1:1 complex with G-actin, resulting in the inhibition of DNase activity and loss of the ability of G-actin to polymerise into fibres []. DNase I has been used in the treatment of lung problems in patients with cystic fibrosis: here it acts by degrading DNA found in purulent lung secretions, reducing their viscosity and making it easier for the patient to breathe [].The sequence of DNase I is evolutionary related to that of human muscle-specific DNase-like protein and human proteins DHP1 and DHP2. However, the first disulphide bond of DNase I is not conserved in these proteins. | Name | Deoxyribonuclease I, conservied site |
| Short Name | DNASE_I_2 | Type | Conserved_site |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
