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Information on EC 3.1.99.B1 - flap endonuclease-1 and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58839

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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Methanocaldococcus jannaschii
UNIPROT: Q58839
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
monovalent salt effect is broad, with equal activities observed in 50 and 100 mM KCl
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
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7 - 9.5
pH 7.7: 77% of maximal activity, pH 9.5: 91% of maximal activity
6 - 8
pH 6.0-7.0: optimum, pH 8.0: about 55% of maximal activiy
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
enzyme begins to show activity at temperatures above 35 °C
50 - 80
about 50% of maximal activity, 80°C: about 65% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are grown at 7°C by hanging drop vapor diffusion method, crystal structure of FEN-1 from Methanococcus jannaschii, determined at 2.0 A resolution, reveals an active site with two metal ions residing on top of a deep cleft where several conserved acidic residues are clustered. Near the active site, a long flexible loop comprised of many basic and aromatic residues forms a hole large enough to accommodate the DNA substrate
the crystal belongs to the space group of P2(1) with unit cell dimensions of a = 58.93 A, b = 42.53 A, c = 62.62 A and beta = 92.250, 2.0 A resolution, frozen crystal
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95
enzyme retains activity for 15 min
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rao, H.G.; Rosenfeld, A.; Wetmur, J.G.
Methanococcus jannaschii flap endonuclease: expression, purification, and substrate requirements
J. Bacteriol.
180
5406-5412
1998
Methanocaldococcus jannaschii (Q58839), Methanocaldococcus jannaschii
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
Bae, K.W.; Baek, K.W.; Cho, C.S.; Hwang, K.Y.; Kim, H.-R.; Sung, H.-C.; Cho, Y.
Expression, purification, characterization and crystallization of flap endonuclease-1 from Methanococcus jannaschii
Mol. Cells
9
45-48
1999
Methanocaldococcus jannaschii (Q58839), Methanocaldococcus jannaschii
Manually annotated by BRENDA team
Hwang, K.Y.; Baek, K.; Kim, H.-Y.; Cho, Y.
The crystal structure of flap endonuclease-1 from Methanococcus jannaschii
Nat. Struct. Biol.
5
707-713
1998
Methanocaldococcus jannaschii (Q58839), Methanocaldococcus jannaschii
Manually annotated by BRENDA team