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
results (
results (Inhibitors
Inhibitors on EC 3.1.30.2 - Serratia marcescens nuclease
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
dAMP
competitive inhibitor of partial type, dAMP forming a complex with Sma nuc does not completely prevent the RNA binding and reduces the enzyme affinity to RNA substrate in competition with RNA for the binding site
AMP
competitive inhibitor of partial type, AMP forming a complex with Sma nuc does not completely prevent the RNA binding and reduces the enzyme affinity to RNA substrate in competition with RNA for the binding site
EDTA
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90% inhibition at 2.5 mM, inhibition fully reversible by addition of Mg2+
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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binding of Co(NH3)6 3+ to highly polymerized DNA caused correspondingly about 7fold decrease in Km and more than 600fold decrease in Kcat compared with that of Mg-DNA complex of B-form; binding of Mg2+ to highly polymerized DNA causes correspondingly about 80fold decrease in Km and more than 1600fold decrease in Kcat compared with that of Mg-DNA complex of B-form
Mn2+
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inhibits hydrolysis of RNA, denatured DNA and 3'-AMP, not: native DNA
Zn2+
complete inhibition; complete inhibition
additional information
Azotobacter agilis
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secondary interaction in long RNA chains inhibit the enzyme
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additional information
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DNA transition from the right handed B-form to the hybrid B-Z-form causes a decrease in Vmax, Km and Kcat of DNA cleavage with the nuclease
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