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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

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 Hydrolases
         3.1 Acting on ester bonds
             3.1.30 Endoribonucleases that are active with either ribo- or deoxyribonucleic acids and produce 5'-phosphomonoesters
                3.1.30.2 Serratia marcescens nuclease

Subunits

Subunits on EC 3.1.30.2 - Serratia marcescens nuclease

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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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x * 43000, SDS-PAGE
dimer
homodimer
each monomer consists of 245 amino acids, they function independently of each other, monomer and dimer can function with same specific activity. Dimer form has an electrostatic advantage over the monomer to associate with DNA, inner-sphere binding in the monomer, outer-sphere in the dimer, interface of the protein and DNA is full of charged side chains, such as Arg57, Arg87, Arg125, Arg196, and Mg2+. Interfacial region is highly hydrated with an average of 27 hydration sites in the monomer (water acts more to screen the electrostatic region between the monomer and DNA) and 31 sites in the dimer (water acts more as a glue to provide structural adaptability with the protein and DNA). Dynamics of H-bonds of water in this active centre only little difference is found (water in the working region in the dimer complex has larger fluctuations than in monomer). Dimerization leads to different contacts between DNA and protein residues, especially to Mg2+
monomer
additional information
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the subunits of the dimer function independently as monomers, molecular dynamic simulations, modelling of complex building with DNA, hydration sites of the enzyme depending on solvent density, overview