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Literature summary for 3.1.99.B1 extracted from

  • Gloor, J.W.; Balakrishnan, L.; Bambara, R.A.
    Flap endonuclease 1 mechanism analysis indicates flap base binding prior to threading (2010), J. Biol. Chem., 285, 34922-34931.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.99.B1

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of His-tagged FEN1 in Escherichia coli strain BL21 (DE3)/pLysS Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged FEN1 from Escherichia coli strain BL21 (DE3)/pLysS Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information FEN1 binding to a flap substrate show that the nuclease binds with similar high affinity to the base of a long flap even when the 5'-end is blocked with biotin/streptavidin. However, FEN1 bound to a blocked flap is more sensitive to sequestration by a competing substrate. FEN1 first binds the flap base and then threads the flap through an opening in the protein from the 5'-end to the base for cleavage, substrate interaction mechanism, overview. Short flaps, below two to four nucleotides long, are cleaved without a threading requirement. Direct flap interactions improve FEN1 binding affinity, dissociation rate is slow when FEN1 is bound to a long, unblocked flap Homo sapiens ?
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 ?

Synonyms

Synonyms Comment Organism
FEN1
-
 Homo sapiens
flap endonuclease 1
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Homo sapiens