3.1.30.2: Serratia marcescens nuclease
This is an abbreviated version!
For detailed information about Serratia marcescens nuclease, go to the full flat file.
Word Map on EC 3.1.30.2
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3.1.30.2
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strand
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single-stranded
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nick
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chromatin
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exonuclease
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phage
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nucleases
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rnase
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bacteriophage
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endonucleolytic
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mismatch
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palindromic
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structure-specific
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internucleosomal
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homing
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glycosylase
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methylase
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phosphodiester
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fork
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restriction-modification
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interspaced
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supercoiled
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crispr
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heteroduplexes
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abasic
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deoxyribonuclease
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retrotransposons
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xeroderma
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aif
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caspase-independent
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dsdna
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pigmentosum
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ape1
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endoribonuclease
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holliday
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end-joining
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nucleolytic
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colicins
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ecorv
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retrotransposition
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interstrand
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okazaki
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mre11
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superhelical
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pvuii
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haeiii
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overhang
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cap-dependent
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sgrnas
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resolvase
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molecular biology
- 3.1.30.2
- strand
-
single-stranded
- nick
- chromatin
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exonuclease
- phage
- nucleases
- rnase
- bacteriophage
-
endonucleolytic
- mismatch
-
palindromic
-
structure-specific
-
internucleosomal
-
homing
- glycosylase
-
methylase
-
phosphodiester
- fork
-
restriction-modification
-
interspaced
-
supercoiled
-
crispr
- heteroduplexes
-
abasic
- deoxyribonuclease
-
retrotransposons
- xeroderma
- aif
-
caspase-independent
- dsdna
- pigmentosum
- ape1
-
endoribonuclease
-
holliday
-
end-joining
-
nucleolytic
- colicins
- ecorv
-
retrotransposition
-
interstrand
-
okazaki
- mre11
-
superhelical
- pvuii
- haeiii
-
overhang
-
cap-dependent
-
sgrnas
- resolvase
- molecular biology
Reaction
endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products =
Synonyms
barley nuclease, BFN1, BMN, CAD, caspase-activated DNase, DFF, DFF40/CAD endonuclease, DNA fragmentation factor, EC 3.1.4.9, ENDO1, ENDO2, ENDO4, ENDO5, endonuclease, endonuclease (Serratia marcescens), endonuclease 1, endonuclease 2, endonuclease 4, endonuclease 5, Kamchatka crab duplex-specific nuclease, More, mung bean nuclease, NUC49, nucA, NucANLS, nuclease A, nuclease I, nuclease, nucleate endo-, nucleate endonuclease, Par_DSN, plant nuclease I, plant S1-like nuclease, plant type I nuclease, rNUC49, S1-like nuclease, Serratia marcescens endonuclease, Serratia marcescens nuclease, Sm2, Sma, Sma nuc, Sma nuc endonuclease, SMnase
ECTree
3.1.30.2 Serratia marcescens nucleaseAdvanced search results
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results (Metals Ions
Metals Ions on EC 3.1.30.2 - Serratia marcescens nuclease
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
Mg2+
Mn2+
NaCl
the enzyme is capable to hydrolyze DNA in the presence of 0.9% NaCl containing 0.002 M calcium cations
Zn2+
[Co(NH3)6]3+
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binding to the DNA substrate induces changes in the secondary structure of the enzyme, followed by a decrease of the enzyme activity
additional information
Ca2+
activates at pH 8.0, preferred divalent cation
Ca2+
in the presence of Mg2+ the DNase activity of Serratia marcescens nuclease is higher than in the presence of Ca2+
Mg2+
Azotobacter agilis
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increases hydrolysis rate of EDTA-dialyzed RNA, no effect on hydrolysis of undialyzed RNA, inhibition at high concentrations
Mg2+
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coordinates 5 water molecules that participate in the enzyme-controlled reaction
Mg2+
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molecular dynamic simulations, interaction with enzyme monomer-DNA complex via 6 ligands, which are changing during the reaction simulation, e.g. Asn119 loses its coordination while Glu127 becomes a ligand, overview
Mg2+
in the presence of 0.58 mM Mg2+, the digestive activity of the enzyme is approximately fourfold increased as compared with the activity in the absence of Mg2+ taken as 100%. Further fivefold increase in Mg2+ concentration causes near 1.5fold enhancement in the enzyme activity. Subsequent two- and fourfold increases in Mg2+ concentration have only a minor impact on the enzyme activity within the experimental error range. 6.0-11.6 mM of Mg2+ corresponding to 20-40 Mg2+ per 1 phosphate in RNA is optimal for the hydrolysis of RNA. Optimal Mg2+ amount is linked with the changing secondary structure of RNA substrates within A-helix. Addition of Mg2+ affects both the rates of products dissociations from the enzyme-substrate complexes and the enzyme associations with the substrates, that is supported by strong increase in the Kcat values and change in the Km values
Mg2+
in the presence of Mg2+ the DNase activity of Serratia marcescens nuclease is higher than in the presence of Ca2+
Mn2+
activates, highly activating divalent cation
Zn2+
dependent on, Zn2+-dependent activity of the enzyme can be strongly enhanced by the Ca2+
Zn2+
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the enzyme is a zinc metalloprotein, three zinc ions interact with the DNA substrate and have different roles in catalysis, e.g. stabilization of the transition state and as reaction nucleophile, binding structures and kinetics, overview
additional information
although ENDO1 nuclease digests ssDNA in the presence of both Ca2+ and Mn2+ ions, its ability to digest dsDNA can be stimulated only by Mn2+ ions. The enzyme activity is not affected by Mg2+ or Fe2+
additional information
although ENDO1 nuclease digests ssDNA in the presence of both Ca2+ and Mn2+ ions, its ability to digest dsDNA can be stimulated only by Mn2+ ions. The enzyme activity is not affected by Mg2+ or Fe2+
additional information
although ENDO1 nuclease digests ssDNA in the presence of both Ca2+ and Mn2+ ions, its ability to digest dsDNA can be stimulated only by Mn2+ ions. The enzyme activity is not affected by Mg2+ or Fe2+
additional information
although ENDO1 nuclease digests ssDNA in the presence of both Ca2+ and Mn2+ ions, its ability to digest dsDNA can be stimulated only by Mn2+ ions. The enzyme activity is not affected by Mg2+ or Fe2+
additional information
metal ion effect is dependent on pH. The enzyme activity is not affected by Mg2+ or Fe2+
additional information
metal ion effect is dependent on pH. The enzyme activity is not affected by Mg2+ or Fe2+
additional information
metal ion effect is dependent on pH. The enzyme activity is not affected by Mg2+ or Fe2+
additional information
metal ion effect is dependent on pH. The enzyme activity is not affected by Mg2+ or Fe2+
additional information
the enzyme activity is not affected by Mg2+ or Fe2+
additional information
the enzyme activity is not affected by Mg2+ or Fe2+
additional information
the enzyme activity is not affected by Mg2+ or Fe2+
additional information
the enzyme activity is not affected by Mg2+ or Fe2+
