Literature summary for 3.1.22.1 extracted from

MacLea, K.S.; Krieser, R.J.; Eastman, A.
Revised structure of the active form of human deoxyribonuclease IIalpha (2002), Biochem. Biophys. Res. Commun., 292, 415-421.

Search for more literature for 3.1.22.1

Cloned(Commentary)

Cloned (Comment)	Organism
the wild-type and mutant enzyme cDNA plasmid are transiently transfected in HCT116 cells	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
H295A	the mutant is inactive	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
tunicamycin	inhibits the N-linked glycosylation and virtually abolishes the enzyme activity	Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
45000	-	Western blot analysis, the incubation with tunicamycin results in a 37000 Da enzyme	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q8WZ79	enzyme activity is reported in all of the human cell lines examined	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	glycosylation is apparently required for maximal enzyme activity	Homo sapiens

Reaction

Reaction	Comment	Organism	Reaction ID
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products	The protein is a single, contiguous polypeptide chain, featuring N-linked sugar moieties and at least one disulfide bridge	Homo sapiens	a

Synonyms

Synonyms	Comment	Organism
deoxyribonuclease IIalpha	-	Homo sapiens
DNase IIalpha	-	Homo sapiens

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Release 2023.1 (January 2023)