3.1.22.1: deoxyribonuclease II
This is an abbreviated version!
For detailed information about deoxyribonuclease II, go to the full flat file.
Word Map on EC 3.1.22.1
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3.1.22.1
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chromatin
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endonuclease
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nuclei
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spleen
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nucleases
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nucleosome
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cathepsins
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micrococcal
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engulf
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caspase-independent
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spiralis
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medicine
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trichinella
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caspase-activated
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dnaase
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ii-like
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internucleosomal
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undigested
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endonucleolytic
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nonhistone
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corpses
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cation-independent
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analysis
- 3.1.22.1
- chromatin
- endonuclease
- nuclei
- spleen
- nucleases
- nucleosome
- cathepsins
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micrococcal
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engulf
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caspase-independent
- spiralis
- medicine
- trichinella
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caspase-activated
- dnaase
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ii-like
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internucleosomal
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undigested
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endonucleolytic
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nonhistone
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corpses
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cation-independent
- analysis
Reaction
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products =
Synonyms
acid deoxyribonuclease, acid DNase, crn-7, deoxyribonuclease II, deoxyribonuclease IIalpha, deoxyribonuclease IIbeta, deoxyribonucleate 3'-nucleotidohydrolase, DNase 2, DNase 2a, DNase II, DNase II homolog, DNase II-1, DNase II-7, DNase IIalpha, DNase IIb, DNase IIbeta, EC 3.1.4.6, L-DNase II, LEI, LEI-derived DNase II, LEI/L-DNase II, leukocyte elastase inhibitor-derived DNase II, leukocyte elastase inhibitor/LEI-derived DNase II, lysosomal DNase II, Nuc-1, NUC-1 apoptotic nuclease, pancreatic DNase II, plancitoxin 1, R31240_2, Sjda, TsDNase II-1, TsDNase II-7
ECTree
3.1.22.1 deoxyribonuclease IIAdvanced search results
results (
results (Activating Compound
Activating Compound on EC 3.1.22.1 - deoxyribonuclease II
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
AP-24
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apoptotic protease of 24 kDa, is activated during apoptosis and is able to activate L-DNase II
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bromobenzene
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the changes of enzyme activity in vivo are likely to be caused by adaption and compensation processes in the organisms of the molluscs exposed to toxicants
chlorobenzene
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the changes of enzyme activity in vivo are likely to be caused by adaption and compensation processes in the organisms of the molluscs exposed to toxicants
gasoline
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increases enzyme activity in the digestive gland and in hemocytes
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intracellular elastase
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a neutral protease, can transform LEI into L-DNase II
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iodobenzene
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the changes of enzyme activity in vivo are likely to be caused by adaption and compensation processes in the organisms of the molluscs exposed to toxicants
phenol
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the changes of enzyme activity in vivo are likely to be caused by adaption and compensation processes in the organisms of the molluscs exposed to toxicants
additional information
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activation is favoured at pH 4 but is increased by a tissue extract
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additional information
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catalytic center of the human DNase II involves His113 and His295, as well as Lys115 and Lys295. The histidine at position 295 of the human sequence is critical for DNase II activity. The human DNase II is active as a contiguous polypeptide chain and has four potential glycosylated sites
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additional information
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His115, His132, and His297 play crucial roles in the function of porcine DNase II. His115 and His297 residues in porcine DNase II act as a general acid-base pair during catalysis, whereas residue His132 appears to be involved in proper protein folding. The porcine DNase II is processed into two non-covalently linked peptides of 35 and 10 kDa and has six potential glycosylated sites
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additional information
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proteolytic processing of recombinant DNase II occurs in the lysosome, which is not involved in the activation of DNase II. The processed enzyme is relatively stable after it is formed
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