Cloned (Comment) | Organism |
---|---|
MEF-/- cells null for enzyme expression and activity are transiently transfected with plasmid-expression constructs encoding wild-type human DNase IIalpha, pD2, or mutant forms | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
C11A | the mutation decreases the activity | Homo sapiens |
C159A | complete loss of activity | Homo sapiens |
C19A | complete loss of activity | Homo sapiens |
C267A | complete loss of activity | Homo sapiens |
C299A | the mutation increases the activity | Homo sapiens |
C308A | complete loss of activity | Homo sapiens |
C327A | complete loss of activity | Homo sapiens |
C347A | complete loss of activity | Homo sapiens |
D107N | although the mutant is capable of even greater glycosylation, this mutant results in some loss of activity | Homo sapiens |
H295A | mutant can effectively bind DNA, but has a direct role in the catalysis | Homo sapiens |
N212Q | mutation decreases activity, tunicamycin treatment results in complete loss of activity | Homo sapiens |
N266Q | mutation decreases activity, tunicamycin treatment results in complete loss of activity | Homo sapiens |
N290Q | mutation decreases activity, tunicamycin treatment results in complete loss of activity | Homo sapiens |
N69Q | mutation decreases activity, tunicamycin treatment results in complete loss of activity | Homo sapiens |
N86Q | mutation decreases activity, tunicamycin treatment results in complete loss of activity | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
tunicamycin | the N-glycosylation inhibitor diminishes the activity | Homo sapiens |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
37000 | - |
unglycosylated form of wild-type enzyme and N69Q mutant upon tunicamycin treatment | Homo sapiens |
43000 | - |
mutants N86Q, N212Q, N266Q, N290Q. It appears that the four sites each contribute to glycosylation and no additional glycosylation sites are responsible for the observed size | Homo sapiens |
45000 | - |
glycosylated form of wild-type enzyme and N69Q mutant | Homo sapiens |
47000 | - |
D107N mutant, addition of glycosylation site | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | Both enzymes alpha and beta contain four predicted N-glycosylation sites, including one site that is found in both proteins and one site found in enzyme beta for which the corresponding site in enzyme alpha does not fit the consensus. The N-glycosylation inhibitor tunicamycin diminishes the activity, but the deglycosylation with peptide N-glycosidase has no effect on protein activity | Homo sapiens |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products | the signal-peptide leader sequence is required for correct glycosylation and the N-glycosylation is important for formation of the active enzyme | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
DNA + H2O | double-strand DNA | Homo sapiens | 3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DNase II | two subfamilies: DNase IIalpha and DNase IIbeta | Homo sapiens |