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Information on EC 3.1.99.B1 - flap endonuclease-1 and Organism(s) Pyrococcus horikoshii and UniProt Accession O50123
for references in articles please use BRENDA:EC3.1.99.B1preliminary BRENDA-supplied EC number
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EC Tree
3.1.99.B1 flap endonuclease-1Specify your search results
Word Map
- 3.1.99.B1
- strand
-
okazaki
-
structure-specific
- pcna
-
exonuclease
- nick
-
single-stranded
-
fork
- nucleases
- duplex
-
5'-flaps
-
long-patch
- endonucleases
-
abasic
- rpa
- ape1
- trinucleotide
-
lp-ber
-
exonucleolytic
-
strand-displacement
-
lagging-strand
-
unannealed
-
pcna-dependent
-
rad9-rad1-hus1
-
pcna-binding
-
5'-tails
-
werner
-
3\'-flap
-
incise
-
holliday
- glycosylases
- drug development
The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The expected taxonomic range for this enzyme is: Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Archaea, Eukaryota
Reaction Schemes
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DNA + H2O
?
the aromatic residues Tyr33 and Phe79, and the aromatic cluster Phe278-Phe279 mainly contribute to the recognition of the substrates without the 3' projection of the upstream strand (the nick, 5'-recess-end, single-flap, and pseudo-Y substrates) for the both exo- and endo-activities, but play minor roles in recognizing the substrates with the 3' projection (the double flap substrate and the nick substrate with the 3' projection)
-
-
?
additional information
?
-
the aromatic residues Tyr33 and Phe79, and the aromatic cluster Phe278-Phe279 mainly contribute to the recognition of the substrates without the 3' projection of the upstream strand (the nick, 5'-recess-end, single-flap, and pseudo-Y substrates) for the both exo- and endo-activities, but play minor roles in recognizing the substrates with the 3' projection (the double flap substrate and the nick substrate with the 3' projection)
-
-
?
additional information
?
-
-
the aromatic residues Tyr33 and Phe79, and the aromatic cluster Phe278-Phe279 mainly contribute to the recognition of the substrates without the 3' projection of the upstream strand (the nick, 5'-recess-end, single-flap, and pseudo-Y substrates) for the both exo- and endo-activities, but play minor roles in recognizing the substrates with the 3' projection (the double flap substrate and the nick substrate with the 3' projection)
-
-
?
additional information
?
-
the enzyme cleaves replication fork-like substrates and 5' double-strand flap structures using both flap endonuclease and 5'->3'-exonuclease activities
-
-
?
additional information
?
-
-
the enzyme cleaves replication fork-like substrates and 5' double-strand flap structures using both flap endonuclease and 5'->3'-exonuclease activities
-
-
?
additional information
?
-
FEN-1 has both 5'-flap endonuclease and 5'-3' exonuclease activities, FEN-1 activity is elevated by the presence of a 1 nucleotide expansion at the 3' end in the upstream primer of substrates called: structures with a 1 nt 3'-flap, which appear to be the most preferable substrates for FEN-1. Serial intermediates with a 1 nt 3'-flap and 5' variable-length flaps are formed by cooperative functioning of Pyrococcus horikoshii FEN-1 with either B or D DNA polymerases
-
-
?
additional information
?
-
-
FEN-1 has both 5'-flap endonuclease and 5'-3' exonuclease activities, FEN-1 activity is elevated by the presence of a 1 nucleotide expansion at the 3' end in the upstream primer of substrates called: structures with a 1 nt 3'-flap, which appear to be the most preferable substrates for FEN-1. Serial intermediates with a 1 nt 3'-flap and 5' variable-length flaps are formed by cooperative functioning of Pyrococcus horikoshii FEN-1 with either B or D DNA polymerases
-
-
?
additional information
?
-
the enzyme possesses 5'-flap endonuclease and 5'->3' exonuclease activity
-
-
?
additional information
?
-
-
the enzyme possesses 5'-flap endonuclease and 5'->3' exonuclease activity
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
60 mM, the activity increases 1.3-fold, 100 mM KCl result in significant inhibition of activity
Mg2+
addition of 1 mM MgCl2 increases the activity 1.4-fold. 10 mM MgCl2 results in greater than 90% inhibition
Mn2+
addition of 0.1 mM MgCl2 increases the activity 1.5-fold. 10 mM MnCl2 results in greater than 90% inhibition
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KCl
60 mM, the activity increases 1.3-fold, 100 mM KCl result in significant inhibition of activity
Mg2+
addition of 1 mM MgCl2 increases the activity 1.4-fold. 10 mM MgCl2 results in greater than 90% inhibition
Mn2+
addition of 0.1 mM MgCl2 increases the activity 1.5-fold. 10 mM MnCl2 results in greater than 90% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
comparison of the Km, kcat, and kcat/Km values between WT and the mutants
-
additional information
additional information
-
comparison of the Km, kcat, and kcat/Km values between WT and the mutants
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
comparison of the Km, kcat, and kcat/Km values between WT and the mutants
-
additional information
additional information
-
comparison of the Km, kcat, and kcat/Km values between WT and the mutants
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
comparison of the Km, kcat, and kcat/Km values between WT and the mutants
-
additional information
additional information
-
comparison of the Km, kcat, and kcat/Km values between WT and the mutants
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
the activity of phFEN decreases immediately at pH values below 6.0 and over 7.0. The activity can not be detected at pH 5.0 and decreased to 24% at pH 9.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
additional information
additional information
the optimal temperature could not be determined since the activity peak could not be detected
additional information
-
the optimal temperature could not be determined since the activity peak could not be detected
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the pI value of the phFEN is greater than 9.3
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
the enzyme has important roles in DNA replication, repair, and recombination
metabolism
plays important roles with DNA polymerases in DNA replication, repair and recombination
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion, the crystal structure of flap endonuclease-1 from Pyrococcus horikoshii (phFEN-1) is determined to a resolution of 3.1 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F278A
the substitution of the aromatic residues with alanine leads to a large reduction in kcat value, although the mutants retains Km-value similar to that of the wild-type enzyme
F278A/F279A
F278H/F279H
F278L/F279L
F278W/F279W
F278Y/F279Y
F279A
the substitution of the aromatic residues with alanine leads to a large reduction in kcat value, although the mutants retains Km-value similar to that of the wild-type enzyme
F35A
F35L
F35Y
F79A
F79H
F79L
F79W
F79Y
K193A
KM-value is 4fold of the wild-type value, kcat is almost the same as for wild-type enzyme
K193A/R194A/K195A
K193E/R194E/K195E
the negatively charged triple mutant shows similar but more magnified effects on both parameters compared with the alanine triple mutant K193A/R194A/K195A
K195A
KM-value is 8fold of the wild-type value, kcat is almost the same as for wild-type enzyme
K199A
km and kcat values of the mutant enzyme differ little from the wild-type values
K243A
Km and kcat/Km values of the mutant enzyme do not change markedly compared with the wild-type values
K243E
Km and kcat/Km values of the mutant enzyme do not change markedly compared with the wild-type values
K248A
Km and kcat/Km values of the mutant enzyme do not change markedly compared with the wild-type values
K249A
Km and kcat/Km values of the mutant enzyme do not change markedly compared with the wild-type values
K263A
Km and kcat/Km values of the mutant enzyme do not change markedly compared with the wild-type values
K263E
Km and kcat/Km values of the mutant enzyme do not change markedly compared with the wild-type values
K51E/R53E
the double mutant retains 30% of the wild-type kcat/Km value
K87A
the kcat value of the mutant decreased 400fold, whereas the Km value is almost the same as that of wild-type enzyme
K87A/R88A/K89A
the Km-value is 5fold higher, the kcat is 184fold lower than that of the wild-type enzyme
K93A/R94A/R95A
Km-value and kcat-value is increased 17fold and decreased 96fold, respectively, compared with the wild-type values
R118A/K119A
R194A
KM-value is 5fold of the wild-type value, kcat is almost the same as for wild-type enzyme
R40E/R42E
the Km of the mutynt is increased 105fold compared with wild-type. The kcat and kcat/Km values areo decreased 4- and 680fold, respectively
R40G
Km of the mutant increases 7fold, compared with that of the wild-type enzyme
R40G/R42G
R42E
Km and kcat/Km values of the mutant are 19fold higher and 25fold lower than the values of wild-type enzyme, respectively
R42G
Km of the mutant increases 7fold, compared with that of the wild-type enzyme
R42Q
KM-value is almost the same as the value for wild-type enzyme
R88A
Km and kcat values of the mutant enzyme do not change markedly, compared with the wild-type values
R89A
Km and kcat values of the mutant enzyme do not change markedly, compared with the wild-type values
R94A
Y237A
Km and kcat/Km values of the mutant enzyme do not change markedly compared with the wild-type values
Y33A
Y33F
Y33H
Y33L
Y33W
additional information
F278A/F279A
the kcat values of the mutant enzyme are decreased about 1020% with the 5'-recess-end substrate and the nick substrate
F278A/F279A
the kcat value of the mutant enzyme with the 5'-recess-end substrate and the the nick substrate is 10-20% of that of wild-type enzyme
F278H/F279H
kcat value decreases 83fold for the 5'-recess-end substrate and 150fold for the nick substrate compared with the wild-type values. 454fold decrease in kcat/Km for the 5'-recess-end substrate, 80fold decrease in kcat/Km for the nick substrate. The Km-value for the endo activity with the double flap substrate is increased 4fold, the kcat/Km-value is decreased 14fold, compared with the wild-type value
F278H/F279H
the Km value for the 5'-recess-end substrate is elevated 5 times compared with the wild-type value whereas for the nick substrate the Km value of F278H/F279H is 60% the wild-type value
F278H/F279H
the Km value for the 5'-recess-end substrate is elevated 5times compared with that of wild-type enzyme, for the nick substrate the Km value is 60% that of wild-type enzyme
F278L/F279L
the kcat values of the mutant enzyme are decreased about 1020% with the 5'-recess-end substrate and the nick substrate
F278L/F279L
the kcat value of the mutant enzyme with the 5'-recess-end substrate and the the nick substrate is 10-20% of that of wild-type enzyme
F278L/F279L
the Km value for the 5'-recess-end substrate and the the nick substrate is lower than that of the wild-type enzyme
F278W/F279W
the kcat values of the mutant enzyme are decreased about 1020% with the 5'-recess-end substrate and the nick substrate
F278W/F279W
the kcat value of the mutant enzyme with the 5'-recess-end substrate and the the nick substrate is 10-20% of that of wild-type enzyme
F278W/F279W
the Km value for the 5'-recess-end substrate and the the nick substrate is lower than that of the wild-type enzyme
F278Y/F279Y
the kcat value of F278Y/F279Y is restored to around 70% of that of wil-type enzyme with the 5'-recess-end substrate and the nick substrate
F278Y/F279Y
the kcat value of the mutant enzyme with the 5'-recess-end substrate and the the nick substrate is around 70% of that of wild-type enzyme
F278Y/F279Y
the Km value for the 5'-recess-end substrate and the the nick substrate is lower than that of the wild-type enzyme
F35A
kcat and Km of F35A and F35L show no significant decrease compared with the wild-type values
F35A
the kcat and Km show no significant decrease compared with that of wild-type. For the nick substrate, the kcat value decreases 25fold compared with that of wild-type enzyme
F35L
kcat and Km of F35A and F35L show no significant decrease compared with the wild-type values
F35L
the kcat and Km show no significant decrease compared with that of wild-type
F35Y
the Km values of the mutant enzyme are about 4- and 3fold higher than the values of wild-type enzyme with the nick and 5'-recess-end substrates, respectively
F35Y
mutation causes an 17fold decrease and an 24fold decrease in kcat with the nick and 5'-recess-end substrates, respectively
F79A
for the 5'-recess-end substrate, the kcat value of the mutant enzyme decreases 71fold compared with that of wild-type.For the nick substrate, the kcat value decreases 25fold compared with that of wild-type. 58fold decrease in kcat/Km for the 5'-recess-end substrate, 75fold decrease in kcat/Km for the nick substrate. The Km-value for the endo activity with the double flap substrate is increased 7fold, the kcat/Km-value is decreased 6fold, compared with the wild-type value.For the single flap and pseudo-Y substrates, the kcat of F79A decreases 31- and 37fold, respectively, compared with that of wild-type
F79A
for the 5'-recess-end substrate, the kcat value decreases 71fold compared with that of wild-type enzyme. For the nick substrate, the kcat-value decreases 25fold compared with that of wild-type enzyme
F79H
te kcat value of the mutant for the 5'-recess-end substrate is decreased to about 50% of the wild-type value, and the kcat value of F79H for the nick substrate is seven times lower than that of wild-type enzyme. The Km value of F79H for the 5'-recess-end substrate is 13fold higher than that of wild-type, whereas the Km value of F79H for the nick substrate is about 2 times higher than that of wild-type
F79H
the kcat value of the mutant enzyme for the nick substrate is seven times lower than that of the wild-type enzyme. The Km value of the mutant enzyme for the 5'-recess-end substrate is 13fold higher than that of wild-type enzyme. The Km value of the mutant enzyme for the nick substrate is about 2 times higher than that of the wild-type enzyme
F79L
for the 5'-recess-end substrate, the kcat value of the mutant enzyme is restored to 20% of the wild-type value.For the nick substrate, the kcat value of the mutant enzyme is restored to 20% of that of the wild-type enzyme. The kcat-values for of the single flap and pseudo-Y substrates decrease to 17 and 7% of the wild-type values, respectively. The Km for the single flap and pseudo-Y substrates is varied moderately, but not significantly, compared with that of wild-type enzyme
F79L
for the 5'-recess-end substrate and for the the nick substrate, the kcat value is 20% of the wild-type value value
F79W
the kcat values of the mutant enzyme for the 5'-recess-end substrate and the nick substrate are restored to almost the same level as the wild-type values
F79W
the kcat value for the 5'-recess-end substrate and for the the nick substrate are almost the same as the wild-type values
F79Y
the kcat values of the mutant enzyme for the 5'-recess-end substrate and the nick substrate are restored to almost the same level as the wild-type values. The kcat-value for the single flap and pseudo-Y substrates are restored to almost the same level as the wild-type substrates
F79Y
the kcat value for the 5'-recess-end substrate and for the the nick substrate are almost the same as the wild-type values
K193A/R194A/K195A
kcat/Km-value is decreased 76fold, compared with the value of wild-type enzyme
K193A/R194A/K195A
the Km value of the mutant enzyme increases markedly and the kcat value decreases moderately
R118A/K119A
kcat-value is decreased 111fold, compared with the wild-type value
R118A/K119A
kcat/Km-value is decreased 1851fold, compared with the value of wild-type enzyme
R40G/R42G
kcat/Km-value is decreased 222fold, compared with the value of wild-type enzyme
R40G/R42G
Km-value of the mutant enzyme is elevated 26fold compared with that of the wild type
R94A
kcat-value is decreased 200fold compared with the wild-type value
R94A
mutant enzyme shows a 12fold increase in the Km value and a 15fold decrease in the kcat-value compared with the wild-type values
Y33A
kcat decreases 333fold, compared with that of the wild-type enzyme, for exo-activity against the 5'-recess-end substrate. For the exo-activity against the nick substrate, the kcat values decreases 53fold.The kcat of Y33A for the single flap substrate decreases 30fold. The kcat of Y33A for the pseudo-Y substrate decreases 485fold
Y33A
the substitution of the aromatic residues with alanine leads to a large reduction in kcat value (333fold decrease in exo-activity against the 5'-recess-end substrate), although the mutants retains Km-value similar to that of the wild-type enzyme. The exo-activity against the nick substrate, the kcat values decreases 53fold compared with that of wild-type enzyme
Y33F
kcat for exo-activity against the 5'-recess-end substrate is 20-30% of the wild-type value. The kcat values of Y33F for the single flap and pseudo-Y substrates are restored to 38 and 20% of the value of wild-type, respectively
Y33F
the kcat value for exo-activity against the 5'-recess-end substrate is about 25% compared to tht kcat value of wild-type enzyme, the Km value changes slightly compared with that of wild-type enzyme
Y33H
kcat for exo-activity against the 5'-recess-end substrate is 20-30% of the wild-type value
Y33H
the kcat value for exo-activity against the 5'-recess-end substrate is about 25% compared to tht kcat value of wild-type enzyme, the Km value changes slightly compared with that of wild-type enzyme
Y33L
kcat decreases 1180fold, compared with that of the wild-type enzyme, for exo-activity against the 5'-recess-end substrate. For the exo-activity against the nick substrate, the kcat values decreases 134fold. 2353fold decrease in kcat/Km for the 5'-recess-end substrate, 270fold decrease in kcat/Km for the nick substrate. The Km-value for the endo activity with the double flap substrate is increased 4fold, the kcat/Km-value is decreased 5fold, compared with the wild-type value. The kcat of Y33A for the single flap substrate decreases 433fold. The kcat of Y33A for the pseudo-Y substrate decreases 3233fold
Y33L
the muation leads to a large reduction in kcat value (1180fold decrease in exo-activity against the 5'-recess-end substrate) compared to tht kcat value of wild-type enzyme. The exo-activity against the nick substrate, the kcat values decreases 1343fold compared with that of wild-type enzyme
Y33W
kcat for exo-activity against the 5'-recess-end substrate is 20-30% of the wild-type value
Y33W
the kcat value for exo-activity against the 5'-recess-end substrate is about 25% compared to tht kcat value of wild-type enzyme, the Km value changes slightly compared with that of wild-type enzyme
additional information
the aromatic residues Tyr33 and Phe79, and the aromatic cluster Phe278-Phe279 mainly contribute to the recognition of the substrates without the 3' projection of the upstream strand (the nick, 5'-recess-end, single-flap, and pseudo-Y substrates) for the both exo- and endo-activities, but play minor roles in recognizing the substrates with the 3' projection (the double flap substrate and the nick substrate with the 3' projection). The replacement of Tyr33, Phe79, and Phe278-Phe279, with non-charged aromatic residues, but not with aliphatic hydrophobic residues, recovers the kcat values almost fully for the substrates without the 3' projection of the upstream strand, suggesting that the aromatic groups of Tyr33, Phe79, and Phe278-Phe279 might be involved in the catalytic reaction, probably via multiple stacking interactions with nucleotide bases
additional information
-
the aromatic residues Tyr33 and Phe79, and the aromatic cluster Phe278-Phe279 mainly contribute to the recognition of the substrates without the 3' projection of the upstream strand (the nick, 5'-recess-end, single-flap, and pseudo-Y substrates) for the both exo- and endo-activities, but play minor roles in recognizing the substrates with the 3' projection (the double flap substrate and the nick substrate with the 3' projection). The replacement of Tyr33, Phe79, and Phe278-Phe279, with non-charged aromatic residues, but not with aliphatic hydrophobic residues, recovers the kcat values almost fully for the substrates without the 3' projection of the upstream strand, suggesting that the aromatic groups of Tyr33, Phe79, and Phe278-Phe279 might be involved in the catalytic reaction, probably via multiple stacking interactions with nucleotide bases
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
102
Tm-value is 102°C in 0.0085 and 0.0014 mM protein with 1 M NaCl concentrations. Values of Tm are not dependent on the protein concentration
95
at a final concentration of 0.3 mg/ml, the half-life is 2 h in the presence of 1 M NaCl and 20 min in 50 mM NaCl
additional information
additional information
thermostability is dependent on the concentration of NaCl. Addition of 1 M NaCl increases the thermostability
additional information
-
thermostability is dependent on the concentration of NaCl. Addition of 1 M NaCl increases the thermostability
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Matsui, E.; Kawasaki, S.; Ishida, H.; Ishikawa, K.; Kosugi, Y.; Kikuchi, H.; Kawarabayashi, Y.; Matsui, I.
Thermostable flap endonuclease from the archaeon, Pyrococcus horikoshii, cleaves the replication fork-like structure endo/exonucleolytically
J. Biol. Chem.
274
18297-18309
1999
Pyrococcus horikoshii (O50123), Pyrococcus horikoshii
Matsui, E.; Musti, K.V.; Abe, J.; Yamasaki, K.; Matsui, I.; Harata, K.
Molecular structure and novel DNA binding sites located in loops of flap endonuclease-1 from Pyrococcus horikoshii
J. Biol. Chem.
277
37840-37847
2002
Pyrococcus horikoshii (O50123), Pyrococcus horikoshii
Matsui, E.; Abe, J.; Yokoyama, H.; Matsui, I.
Aromatic residues located close to the active center are essential for the catalytic reaction of flap endonuclease-1 from hyperthermophilic archaeon Pyrococcus horikoshii
J. Biol. Chem.
279
16687-16696
2004
Pyrococcus horikoshii (O50123), Pyrococcus horikoshii
Matsui, E.; Urushibata, Y.; Abe, J.; Matsui, I.
Serial intermediates with a 1 nt 3'-flap and 5' variable-length flaps are formed by cooperative functioning of Pyrococcus horikoshii FEN-1 with either B or D DNA polymerases
Extremophiles
18
415-427
2014
Pyrococcus horikoshii (O50123), Pyrococcus horikoshii, Pyrococcus horikoshii OT-3 (O50123)
Matsui, E.; Abe, J.; Yokoyama, H.; Matsui, I.
Aromatic residues located close to the active center are essential for the catalytic reaction of flap endonuclease-1 from hyperthermophilic archaeon Pyrococcus horikoshii
J. Biol. Chem.
279
16687-16696
2004
Pyrococcus horikoshii (O50123), Pyrococcus horikoshii, Pyrococcus horikoshii OT-3 (O50123)
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