Information on EC 3.1.31.1 - micrococcal nuclease

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.1.31.1
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RECOMMENDED NAME
GeneOntology No.
micrococcal nuclease
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
CAS REGISTRY NUMBER
COMMENTARY hide
9013-53-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
pFOG
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
human adenovirus
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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UniProt
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
protozoa
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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1094684 A+, 1183442 A+, 134451 A+, 1370296 A+, 1528975 A+, 1528991 A+, 1534001 A+, 1534992 A+, 1536169 A+, 1540864 A+, 1576123 A+, 1577505 A+, 1577571 A+, 1577591 A+, 1577593 A+, 1577598 A+, 1577626 A+, 1577683 A+, 1577685 A+, 1577688 A+, 1577693 A+, 1577767 A+, 1577853 A+, 2197875 A+, 2647009 A+, 2647286 A+, 2648489 A+, 2670422 A+, 2670431 A+, 2670440 A+, 2670447 A+, 2670449 A+, 2670473 A+, 2670508 A+, 2670515 A+, 2670535 A+, 2670570 A+, 2670583 A+, 2670593 A+, 2670600 A+, 2670620 A+, 1159055 A++, 1173702 A++, 1241455 A++, 1254500 A++, 1361770 A++, 1361808 A++, 1407943 A++, 1533958 A++, 1533984 A++, 1535552 A++, 1535737 A++, 1535801 A++, 1535847 A++, 1536868 A++, 1542049 A++, 1546041 A++, 1574293 A++, 1577458 A++, 1577483 A++, 1577490 A++, 1577494 A++, 1577616 A++, 1577645 A++, 1577744 A++, 1577817 A++, 2189476 A++, 2197864 A++, 2197866 A++, 2197930 A++, 2419786 A++, 2644178 A++, 2646110 A++, 2646243 A++, 2647189 A++, 2670408 A++, 2670474 A++, 2670481 A++, 2670500 A++, 2670511 A++, 2670518 A++, 2670533 A++, 2670542 A++, 2670554 A++, 2670559 A++, 2670572 A++, 2670574 A++, 2670719 A++, 896146 A++, 911216 A++, 1461619 A++, 1533952 A++, 1535613 A++, 1535740 A++, 1535995 A++, 1536094 A++, 1575785 A++, 1577467 A++, 1577539 A++, 1577572 A++, 1577660 A++, 1577665 A++, 1577692 A++, 1577696 A++, 1577699 A++, 1577759 A++, 2189481 A++, 2189909 A++, 2197878 A++, 2197901 A++, 2197906 A++, 2197910 A++, 2197922 A++, 2197942 A++, 2472822 A++, 2646103 A++, 2646311 A++, 2669468 A++, 2669544 A++, 2670423 A++, 2670424 A++, 2670427 A++, 2670429 A++, 2670446 A++, 2670456 A++, 2670504 A++, 2670514 A++, 2670524 A++, 2670596 A++, 912120 A++, 912129 A++, 912134 A++, 895286 A++++, 895442 A++++, 912090 A++++, 912092 A++++, 912130 A++++, 912132 A++++, 912133 A++++
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
salmon
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
209P
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Manually annotated by BRENDA team
Staphylococcus aureus CCTCC AB91093
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Manually annotated by BRENDA team
strain KCCM 11335, Korean Culture Center of Microorganisms, Korea
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Manually annotated by BRENDA team
gene nuc1
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Manually annotated by BRENDA team
a community-acquired CA-MRSA strain, gene nuc
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Manually annotated by BRENDA team
strain V8
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Manually annotated by BRENDA team
gene nucM
A0A076JSR1
UniProt
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3'-O-acetylnitrophenyl-pdT + H2O
?
show the reaction diagram
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?
5'-chloromethyl-pdTp-nitrophenyl + H2O
?
show the reaction diagram
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?
5'-O-acetyl-dTp-nitrophenyl + H2O
?
show the reaction diagram
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?
5'-sulfate-dTp-nitrophenyl + H2O
?
show the reaction diagram
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?
DNA
?
show the reaction diagram
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?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
show the reaction diagram
dTp-nitrophenyl + H2O
?
show the reaction diagram
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?
GFP-ssDNA + H2O
?
show the reaction diagram
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partial degradation
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?
GFP-ssRNA + H2O
?
show the reaction diagram
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complete degradation
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?
M13mp18 DNA + H2O
?
show the reaction diagram
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circular single stranded DNA
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?
methyl-pdTp-nitrophenyl + H2O
?
show the reaction diagram
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?
nitrophenyl-pdT + H2O
?
show the reaction diagram
nitrophenyl-pdTp + H2O
?
show the reaction diagram
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?
nitrophenyl-pdTpdTp-nitrophenyl + H2O
?
show the reaction diagram
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?
RNA + H2O
nucleoside 3'-phosphates + dinucleotides
show the reaction diagram
ss-DNA + H2O
?
show the reaction diagram
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single strand salmon sperm DNA, obtained by boiling for 30 min and rapid cooling on ice
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?
ssDNA + H2O
?
show the reaction diagram
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single stranded salmon sperm DNA
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?
T2 DNA + H2O
?
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
DNA + H2O
3'-deoxymononucleotides + dinucleotides
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
Q7A5U0, Q7A6P2
activates slightly at 5 mM
Cu2+
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minimal activation if Ca2+ is replaced by Cu2+
Fe2+
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minimal activation if Ca2+ is replaced by Fe2+
Ni2+
Q7A5U0, Q7A6P2
activates slightly at 0.05 mM
Sr2+
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DNase but no RNase activity if Ca2+ is replaced Sr2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-deoxythymidine 3',5'-diphosphate
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at 100 microM concentration of pdTp, parasites show block in development, most of the parasites appear dead or shrunken within six hours after inhibitor treatment
3',5'-deoxythymidine diphosphate
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addition to the cell culture medium blocks further growth
adenosine 3',5'-diphosphate
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able to induce folding of mutant proteins into the native state
Ca2+
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competitive
caspase-3
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Tudor staphylococcal nuclease, a multifunctional regulator of gene expression, is cleaved by caspase-3 during apoptosis, this cleavage impairs the ability of Tudor staphylococcal nuclease to activate mRNA splicing, inhibits its ribonuclease activity and is important for the execution of apoptosis, cleavage of enzyme lowers its nuclease activity by almost 50%
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Co2+
Q7A5U0, Q7A6P2
isozyme Nuc1 shows 79% activity at 5 mM concentration
Cu2+
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competitive
deoxythymidine 3',5'-bisphosphate
deoxythymidine 3',5'-diphosphate
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in the presence of pdTp, unfolding forces increase drastically
Hg2+
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competitive
metacaspase mcII-Pa
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Mn2+
Q7A5U0, Q7A6P2
isozyme Nuc1 activity drops sharply at 5 mM concentration; isozyme Nuc2 activity decreases with an increase in Mn2+ concentration
Mononucleotides
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with 5'-phosphate end group
oligonucleotides
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with 5'-phosphate end group
thymidine 3',5'-bisphosphate
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competitive
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mecaptoethanol
Q7A5U0, Q7A6P2
;
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dithiothreitol
Q7A5U0, Q7A6P2
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DTT
Q7A5U0, Q7A6P2
163.4% of initial isozyme Nuc1 activity at 1 mM
NaCl
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maximum activity of SNR140 and SNR141 SNAse R N-terminal fragments which extends from residues 6 to 140 and 6 to 141 respectively, 0.3 M, studies performed to explore the mechanism of nascent peptide folding
Triton X-100
Q7A5U0, Q7A6P2
; 210.5% of initial isozyme Nuc1 activity at 1%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00409 - 0.00431
DNA
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Staphylococcus aureus
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
3',5'-deoxythymidine diphosphate
Plasmodium falciparum
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after 48 h
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
732
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pH 7.4, 25C
1270
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purified recombinant mutant SNase137, pH 7.4, 25C
1319
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purified recombinant mutant SNase139, pH 7.4, 25C
2000
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purified recombinant enzyme, pH and temperature not specified in the publication
2018
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purified recombinant mutant SNase140, pH 7.4, 25C
2298
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purified recombinant mutant SNase141, pH 7.4, 25C
2553
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purified recombinant wild-type SNase, pH 7.4, 25C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5
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10 mM Ca2+, insolubilized enzyme; 1 mM Ca2+, soluble enzyme
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 8
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the overall secondary and tertiary structure of SNase remains unchanged between pH 2.5 and 8.0
3 - 10
Q7A5U0, Q7A6P2
effects of pH on thermonuclease activity of isozymes Nuc1 and Nuc2, profile overview; effects of pH on thermonuclease activity of isozymes Nuc1 and Nuc2, profile overview
9 - 10
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depends on Ca2+ concentration
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
Q7A5U0, Q7A6P2
assay at; assay at
50
Q7A5U0, Q7A6P2
recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 80
Q7A5U0, Q7A6P2
effects of temperature on thermonuclease activity of isozymes Nuc1 and Nuc2, profile overview; effects of temperature on thermonuclease activity of isozymes Nuc1 and Nuc2, profile overview
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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high SND1 enzyme expression level
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
additional information
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expression of the enzyme and of angiotensin II type 1 receptor are positively correlated
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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human Tudor staphylococcal nuclease interacts with the Ras-GAP SH3 domain-binding protein and is recruited into stress granules, the main type of discrete RNA-containing cytoplasmic foci structure that is formed under stress conditions
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Manually annotated by BRENDA team