Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.21.1 extracted from

  • Fujihara, J.; Yasuda, T.; Kunito, T.; Fujii, Y.; Takatsuka, H.; Moritani, T; Takeshita, H.
    Two N-linked glycosylation sites (Asn18 and Asn106) are both required for full enzymatic activity, thermal stability, and resistance to proteolysis in mammalian deoxyribonuclease I (2008), Biosci. Biotechnol. Biochem., 72, 3197-3205.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutants in COS-7 cells Bos taurus
expression of wild-type and mutants in COS-7 cells Homo sapiens
expression of wild-type and mutants in COS-7 cells Equus caballus

Protein Variants

Protein Variants Comment Organism
N106Q enzyme activity is lower than that of the wild-type, is unstable to heat and less resistant to trypsin Homo sapiens
N106Q enzyme activity is lower than that of the wild-type, is unstable to heat and less resistant to trypsin Equus caballus
N106Q enzyme activity is lower than that of the wild-type, is unstable to heat, trypsin resistance is similar to that of the wild-type Bos taurus
N18Q enzyme activity is lower than that of the wild-type, is unstable to heat and less resistant to trypsin Homo sapiens
N18Q enzyme activity is lower than that of the wild-type, is unstable to heat and less resistant to trypsin Equus caballus
N18Q enzyme activity is lower than that of the wild-type, is unstable to heat, trypsin resistance is similar to that of the wild-type Bos taurus
N18Q/N106Q enzyme activity is lower than those of the single mutants, is unstable to heat and is the most sensitive to trypsin Homo sapiens
N18Q/N106Q enzyme activity is lower than those of the single mutants, is unstable to heat and is the most sensitive to trypsin Equus caballus
N18Q/N106Q enzyme activity is lower than those of the single mutants, is unstable to heat, trypsin resistance decreases in a time-dependent manner Bos taurus

General Stability

General Stability Organism
N18 and N106 are both necessary for full enzymatic activity, heat-stability, and trypsin resistance Bos taurus
N18 and N106 are both necessary for full enzymatic activity, heat-stability, and trypsin resistance Homo sapiens
N18 and N106 are both necessary for full enzymatic activity, heat-stability, and trypsin resistance Equus caballus

Inhibitors

Inhibitors Comment Organism Structure
additional information is resistant to trypsin Homo sapiens
Trypsin is less resistant to trypsin than human DNase I, DNase I activity decreases gradually Bos taurus
Trypsin is less resistant to trypsin than human DNase I, DNase I activity decreases gradually Equus caballus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Equus caballus Q4AEE3
-
-
Homo sapiens P24855
-
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information pancreas-parotid Bos taurus
-
pancreas
-
Homo sapiens
-
parotid gland
-
Equus caballus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
salmon testis DNA + H2O
-
Bos taurus 5'-phosphooligonucleotides + ?
-
?
salmon testis DNA + H2O
-
Homo sapiens 5'-phosphooligonucleotides + ?
-
?
salmon testis DNA + H2O
-
Equus caballus 5'-phosphooligonucleotides + ?
-
?

Synonyms

Synonyms Comment Organism
deoxyribonuclease I
-
Bos taurus
deoxyribonuclease I
-
Homo sapiens
deoxyribonuclease I
-
Equus caballus
DNase I
-
Bos taurus
DNase I
-
Homo sapiens
DNase I
-
Equus caballus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
both N-linked glycosylation sites N18 and N106 are required for heat stability Bos taurus
additional information
-
both N-linked glycosylation sites N18 and N106 are required for heat stability Homo sapiens
additional information
-
both N-linked glycosylation sites N18 and N106 are required for heat stability Equus caballus