Literature summary for 3.1.30.2 extracted from

Chen, C.; Beck, B.W.; Krause, K.; Pettitt, B.M.
Solvent participation in Serratia marcescens endonuclease complexes (2006), Proteins, 62, 982-995.

Search for more literature for 3.1.30.2

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	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	Serratia marcescens

Organism

Organism	UniProt	Comment	Textmining
Serratia marcescens	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products	catalytic mechanism, enzyme monomer-DNA binding complex, hydration sites and influence of solvent on structure and reaction, active site structure	Serratia marcescens	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the subunits of the dimer function independently as monomers, molecular dynamic simulations involving Mg2+, modelling of complex building with DNA	Serratia marcescens	?	-	?

Subunits

Subunits	Comment	Organism
dimer	monomer and dimer of the enzyme are catalytically active	Serratia marcescens
monomer	monomer and dimer of the enzyme are catalytically active	Serratia marcescens
More	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	Serratia marcescens

Synonyms

Synonyms	Comment	Organism
Serratia marcescens endonuclease	-	Serratia marcescens
SMnase	-	Serratia marcescens

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Release 2023.1 (January 2023)