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Information on EC 3.1.99.B1 - flap endonuclease-1 and Organism(s) Archaeoglobus fulgidus and UniProt Accession O29975

for references in articles please use BRENDA:EC3.1.99.B1
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
            
                3.1.99.B1 flap endonuclease-1
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Archaeoglobus fulgidus
UNIPROT: O29975
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The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The expected taxonomic range for this enzyme is: Archaea, Eukaryota
Reaction Schemes
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endonucleases that remove 5' DNA sequences from a DNA structure called a DNA flap. The DNA flap structure occurs in double-stranded DNA containing a single-stranded break where the 5' portion of the downstream strand is too long and overlaps the 3' end of the upstream strand. Flap endonucleases cleave the downstream strand of the overlap flap structure precisely after the first base-paired nucleotide, creating a ligatable nick.
endonucleases that remove 5' DNA sequences from a DNA structure called a DNA flap. The DNA flap structure occurs in double-stranded DNA containing a single-stranded break where the 5' portion of the downstream strand is too long and overlaps the 3' end of the upstream strand. Flap endonucleases cleave the downstream strand of the overlap flap structure precisely after the first base-paired nucleotide, creating a ligatable nick
Synonyms
flap endonuclease 1, flap endonuclease, flap endonuclease-1, hfen1, t5fen, fen1 endonuclease, t5 flap endonuclease, affen, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
flap endonuclease
-
FENs catalyse both the 5'-exonucleolytic and structure-specific endonucleolytic reactions of DNA substrates
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
DNA + H2O
?
show the reaction diagram
flap DNA + H2O
?
show the reaction diagram
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-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
DNA + H2O
?
show the reaction diagram
catalyzes the exonucleolytic hydrolysis of blunt ended duplex DNA substrates and the endonucleolytic cleavage of 5’-bifurcated nucleic acids at the junction formed between single and doublestranded DNA
products possessing a 5’-phosphate and a 3’-hydroxyl group
-
?
flap DNA + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
the structure-specific nuclease is involved in DNA replication and repair. In DNA replication the enzyme removes the RNA primer of the lagging strand synthesis. In DNA repair, FEN-1 eliminates the damaged DNA and maintains genome integrity by preventing repeat sequence expansion. It recognizes branched structures containing single unpaired ssDNA (flap). Both the 3'-flap and 5'-flap are recognized by the enzyme and the 5'-flap region is excised. The product is a nicked duplex, which is subsequently sealed by DNA ligase
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
endonucleolytic cleavage of flap substrate is only supported by Mg2+ and Mn2+, the cleavage site preferences for each enzyme is altered in the presence of Mn2+
Mn2+
endonucleolytic cleavage of flap substrate is only supported by Mg2+ and Mn2+, the cleavage site preferences for each enzyme is altered in the presence of Mn2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9.5
pH 5.0: 65% of maximal activity, pH 9.5: 21% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
enzyme begins to show activity at temperatures above 35 °C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the structure-specific nuclease is involved in DNA replication and repair. In DNA replication the enzyme removes the RNA primer of the lagging strand synthesis. In DNA repair, FEN-1 eliminates the damaged DNA and maintains genome integrity by preventing repeat sequence expansion. It recognizes branched structures containing single unpaired ssDNA (flap). Both the 3'-flap and 5'-flap are recognized by the enzyme and the 5'-flap region is excised. The product is a nicked duplex, which is subsequently sealed by DNA ligase
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme bound to dsDNA
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichi coli
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Williams, R.; Sengerova, B.; Osborne, S.; Syson, K.; Ault, S.; Kilgour, A.; Chapados, B.R.; Tainer, J.A.; Sayers, J.R.; Grasby, J.A.
Comparison of the catalytic parameters and reaction specificities of a phage and an archaeal flap endonuclease
J. Mol. Biol.
371
34-48
2007
Archaeoglobus fulgidus, Archaeoglobus fulgidus (O29975), Tequintavirus T5
Manually annotated by BRENDA team
Chapados, B.R.; Hosfield, D.J.; Han, S.; Qiu, J.; Yelent, B.; Shen, B.; Tainer, J.A.
Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair
Cell
116
39-50
2004
Archaeoglobus fulgidus (O29975)
Manually annotated by BRENDA team
Hosfield, D.J.; Frank, G.; Weng, Y.; Tainer, J.A.; Shen, B.
Newly discovered archaebacterial flap endonucleases show a structure-specific mechanism for DNA substrate binding and catalysis resembling human flap endonuclease-1
J. Biol. Chem.
273
27154-27161
1998
Archaeoglobus fulgidus (O29975), Methanocaldococcus jannaschii (Q58839), Methanocaldococcus jannaschii, Pyrococcus furiosus (O93634), Pyrococcus furiosus
Manually annotated by BRENDA team
Dor, A.S.; Kilkenny, M.L.; Jones, S.A.; Oliver, A.W.; Roe, S.M.; Bell, S.D.; Pearl, L.H.
Structure of an archaeal PCNA1-PCNA2-FEN1 complex: elucidating PCNA subunit and client enzyme specificity
Nucleic Acids Res.
34
4515-4526
2006
Archaeoglobus fulgidus (O29975)
Manually annotated by BRENDA team