EC Number   |
General Information |
Reference |
|---|
   3.1.30.2 | 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 |
730587 |
| 3.1.30.2 | malfunction |
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 |
718176 |
| 3.1.30.2 | more |
specific site(s) for the nucleotide(s) binding in Sma nuc endonuclease |
730959 |
| 3.1.30.2 | more |
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 |
730764 |
| 3.1.30.2 | 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 |
730959 |
| 3.1.30.2 | physiological function |
enzyme is able to ablate cells in culture |
701699 |
| 3.1.30.2 | physiological function |
FEN1, a key participant in DNA replication and repair, is the major human flap endonuclease that recognizes and cleaves flap DNA structures |
718176 |
| 3.1.30.2 | physiological function |
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 |
717042 |
| 3.1.30.2 | physiological function |
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 |
717824 |
| 3.1.30.2 | physiological function |
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 |
717471 |
