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Literature summary extracted from

  • 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 (1998), J. Biol. Chem., 273, 27154-27161.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.99.B1 expression in Escherichia coli Archaeoglobus fulgidus
3.1.99.B1 expression in Escherichia coli Methanocaldococcus jannaschii
3.1.99.B1 expression in Escherichia coli Pyrococcus furiosus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.99.B1 additional information
-
additional information kinetic parameters for flap substrate cleavage Archaeoglobus fulgidus
3.1.99.B1 additional information
-
additional information kinetic parameters for flap substrate cleavage Methanocaldococcus jannaschii
3.1.99.B1 additional information
-
additional information kinetic parameters for flap substrate cleavage Pyrococcus furiosus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.99.B1 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+ Archaeoglobus fulgidus
3.1.99.B1 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+ Methanocaldococcus jannaschii
3.1.99.B1 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+ Pyrococcus furiosus
3.1.99.B1 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+ Archaeoglobus fulgidus
3.1.99.B1 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+ Methanocaldococcus jannaschii
3.1.99.B1 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+ Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
3.1.99.B1 Archaeoglobus fulgidus O29975
-
-
3.1.99.B1 Methanocaldococcus jannaschii Q58839
-
-
3.1.99.B1 Pyrococcus furiosus O93634
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.99.B1
-
Archaeoglobus fulgidus
3.1.99.B1
-
Methanocaldococcus jannaschii
3.1.99.B1
-
Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.99.B1 additional information the archaebacterial FEN-1 binds to flap, pseudo Y, 3' overhang, and nicked DNA structures. It binds weakly to 5' overhangs and shows no apparent affinity toward either single-stranded or duplex DNA Archaeoglobus fulgidus ?
-
?
3.1.99.B1 additional information the archaebacterial FEN-1 binds to flap, pseudo Y, 3' overhang, and nicked DNA structures. It binds weakly to 5' overhangs and shows no apparent affinity toward either single-stranded or duplex DNA Methanocaldococcus jannaschii ?
-
?
3.1.99.B1 additional information the archaebacterial FEN-1s bind to flap, pseudo Y, 3' overhang, and nicked DNA structures. It binds weakly to 5' overhangs and shows no apparent affinity toward either single-stranded or duplex DNA Pyrococcus furiosus ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.1.99.B1 FEN-1
-
Archaeoglobus fulgidus
3.1.99.B1 FEN-1
-
Methanocaldococcus jannaschii
3.1.99.B1 FEN-1
-
Pyrococcus furiosus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.99.B1 35
-
enzyme begins to show activity at temperatures above 35 °C Archaeoglobus fulgidus
3.1.99.B1 35
-
enzyme begins to show activity at temperatures above 35 °C Pyrococcus furiosus
3.1.99.B1 55
-
assay at Archaeoglobus fulgidus
3.1.99.B1 55
-
assay at Methanocaldococcus jannaschii
3.1.99.B1 55
-
assay at Pyrococcus furiosus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.99.B1 35
-
enzyme begins to show activity at temperatures above 35 °C Methanocaldococcus jannaschii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.99.B1 8 8.8
-
Pyrococcus furiosus
3.1.99.B1 8.8
-
-
Archaeoglobus fulgidus
3.1.99.B1 8.8
-
-
Methanocaldococcus jannaschii

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.99.B1 5 9.5 pH 5.0: 38% of maximal activity, pH 9.5: 56% of maximal activity Pyrococcus furiosus
3.1.99.B1 5 9.5 pH 5.0: 65% of maximal activity, pH 9.5: 21% of maximal activity Archaeoglobus fulgidus
3.1.99.B1 5.7 9.5 pH 7.7: 77% of maximal activity, pH 9.5: 91% of maximal activity Methanocaldococcus jannaschii