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.
Reaction
endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products
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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
General Information
General Information on EC 3.1.30.2 - Serratia marcescens nuclease
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evolution
the enzyme belongs to the plant S1-like nucleases class of enzymes. Different members of this family are characterized by a surprisingly large variety of catalytic properties, nucleolytic activities of all Arabidopsis thaliana S1-like paralogues, overview. In addition to Zn2+-dependent enzymes, this family also comprises nucleases activated by Ca2+ and Mn2+, which implies that the apparently well-known S1 nuclease active site in plant nucleases is able to cooperate with different activatory ions. Particular members of this class differ in their optimum pH value and substrate specificity. Plant representatives of this family evolve toward an increase in catalytic diversity. Phylogenetic analysis, overview
malfunction
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Deficiencies in FEN1 function or deletion of the fen1 gene have profound biological effects, including the suppression of repair of DNA damage incurred from the action of various genotoxic agents
physiological function
enzyme is able to ablate cells in culture
physiological function
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FEN1, a key participant in DNA replication and repair, is the major human flap endonuclease that recognizes and cleaves flap DNA structures
physiological function
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flap endonuclease 1 is a key enzyme in DNA repair and DNA replication. It is a structure-specific nuclease that removes 5'-overhanging flaps and the RNA/DNA primer during maturation of the Okazaki fragment
physiological function
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Flap endonuclease 1 plays critical roles in both DNA replication and repair. Human FEN1 endonuclease, an enzyme involved in excising single-stranded DNA flaps that arise during Okazaki fragment processing and base excision repair, cleaves model flap substrates assembled into nucleosomes. Orienting the flap substrate toward the histone octamer does not significantly alter the rotational orientation of two different nucleosome positioning sequences on the surface of the histone octamer but does cause minor perturbation of nucleosome structure. In contrast, neither flaps oriented toward nor away from the nucleosome surface are cleaved by the enzyme in nucleosomes containing the high-affinity 601 nucleosome positioning sequence. Sequence-dependent motility of DNA on the nucleosome is a major determinant of FEN1 activity
physiological function
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Flap endonuclease, FEN1, is essential for DNA replication and repair, and removes RNA and DNA 5' flaps. Structural and functional analyses of human FEN1:DNA complexes show structure-specific, sequence-independent recognition for nicked dsDNA bent 100° with unpaired 3' and 5' flaps. dsDNA binding and bending, the ssDNA gateway, and double-base unpairing flanking the scissile phosphate control precise flap incision by the two-metal-ion active site
physiological function
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role of FEN1 in replication, recombination, DNA repair and maintenance of telomeres. FEN1 exhibits distinct activity on G4 DNA substrates representative of intermediates in immunoglobulin class switch recombination. hFEN1 but not hEXO1 cleaves substrates bearing telomeric G4 DNA 5'-flaps, consistent with the requirement for FEN1 in telomeric lagging strand replication. FEN1 can create ssDNA at uncapped telomere ends thereby contributing to recombination
physiological function
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the Dna2 enzyme is at the center of both DNA replication and DNA damage repair, acting in conjunction with flap endonuclease 1 and replication protein A in DNA lagging strand replication and with BLM/Sgs1 and MRN/X in double strand break repair. Dna2 shows helicase and flap endo/exonuclease activities requiring an unblocked 5' single-stranded DNA end to unwind or cleave DNA, but Dna2 in fact can create 5' single-stranded DNA ends. Both endonuclease and flap endo/exonuclease are abolished by the Dna2-K677R mutation, implicating the same active site in catalysis. ATP-dependent flap endo/exonuclease activity is observed only in the presence of Mn2+. The endonuclease is blocked by ATP and is thus experimentally distinguishable from the flap endo/exonuclease function. Mechanism of action of Dna2 in multiprotein complexes, overview
physiological function
any mononucleotide produced by Sma nuc during hydrolysis of DNA or RNA may regulate the enzyme activity affecting the RNase activity without pronounced influence on the activity towards DNA. The type of carbohydrate residue in mononucleotides does not affect the regulation. In contrast, the effects depend on the type of bases in nucleotides
physiological function
involvement of isozyme ENDO1 in endosperm senescence. Plant S1-like nucleases are the main class of enzymes involved in nucleic acid degradation during plant programmed cell death
physiological function
plant S1-like nucleases are the main class of enzymes involved in nucleic acid degradation during plant programmed cell death
additional information
specific site(s) for the nucleotide(s) binding in Sma nuc endonuclease
additional information
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specific site(s) for the nucleotide(s) binding in Sma nuc endonuclease
additional information
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treatment of enriched DNA with the mung bean nuclease, an endonuclease specific to single-stranded DNA or RNA, can dramatically reduce genomic DNA carry over of single-stranded template genomic DNA from microdroplet-PCR and increase on-target efficiency of the resultant library. Nuclease treatment of enrichment products shall be incorporated in the workflow of targeted sequencing using microdroplet-PCR for enrichment