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Literature summary for 3.1.22.1 extracted from

  • MacLea, K.S.; Krieser, R.J.; Eastman, A.
    Structural requirements of human DNase II alpha for formation of the active enzyme: the role of the signal peptide, N-glycosylation, and disulphide bridging (2003), Biochem. J., 371, 867-876.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

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

Inhibitors Comment Organism Structure
tunicamycin the N-glycosylation inhibitor diminishes the activity Homo sapiens

Molecular Weight [Da]

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

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

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

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 and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA + H2O double-strand DNA Homo sapiens 3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
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Synonyms

Synonyms Comment Organism
DNase II two subfamilies: DNase IIalpha and DNase IIbeta Homo sapiens