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Literature summary extracted from

  • Jeon, S.J.; Ishikawa, K.
    A novel ADP-dependent DNA ligase from Aeropyrum pernix K1 (2003), FEBS Lett., 550, 69-73.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.5.1.1 expression in Escherichia coli Aeropyrum pernix

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.5.1.1 KCl 100 mM, approximately 70% inhibition Aeropyrum pernix
6.5.1.1 NaCl 100 mM, approximately 70% inhibition Aeropyrum pernix
6.5.1.1 NH4Cl 100 mM, approximately 70% inhibition Aeropyrum pernix

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.5.1.1 Ca2+ the enzyme requires Mg2+ or Mn2+ for activity, Ca2+ or Co2+ are less effective Aeropyrum pernix
6.5.1.1 Co2+ the enzyme requires Mg2+ or Mn2+ for activity, Ca2+ or Co2+ are less effective Aeropyrum pernix
6.5.1.1 KCl optimum concentration: 5 mM Aeropyrum pernix
6.5.1.1 Mg2+ optimal concentration: 15 mM, the enzyme requires Mg2+ or Mn2+ for activity, Ca2+ or Co2+ are less effective Aeropyrum pernix
6.5.1.1 Mn2+ optimal concentration: 7.5 mM, the enzyme requires Mg2+ or Mn2+ for activity, Ca2+ or Co2+ are less effective Aeropyrum pernix

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.5.1.1 69000
-
1 * 69000, SDS-PAGE Aeropyrum pernix
6.5.1.1 69196
-
1 * 69196, the authors refer to the protein of 619 amino acids that is later reannotated as a protein of 602 amino acids (67747.6 Da), calculated from sequence Aeropyrum pernix
6.5.1.1 70000
-
gel filtration Aeropyrum pernix

Organism

EC Number Organism UniProt Comment Textmining
6.5.1.1 Aeropyrum pernix Q9YD18 the ApeLig gene is originally annotated as a protein of 619 amino acids, with a calculated mass of 69196.2 Da. Later it was reannotated as a protein of 602 amino acids (67747.6 Da), in which 17 amino acids are truncated from the N-terminus of the originally annotated protein. The UniProt-number refers to the 602 amino acid protein
-
6.5.1.1 Aeropyrum pernix DSM 11879 Q9YD18 the ApeLig gene is originally annotated as a protein of 619 amino acids, with a calculated mass of 69196.2 Da. Later it was reannotated as a protein of 602 amino acids (67747.6 Da), in which 17 amino acids are truncated from the N-terminus of the originally annotated protein. The UniProt-number refers to the 602 amino acid protein
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.5.1.1
-
Aeropyrum pernix

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.5.1.1 ADP + (deoxyribonucleotide)n + (deoxyribonucleotide)m activity with ADP is slightly lower than with ATP Aeropyrum pernix AMP + phosphate + (deoxyribonucleotide)n+m
-
?
6.5.1.1 ADP + (deoxyribonucleotide)n + (deoxyribonucleotide)m activity with ADP is slightly lower than with ATP Aeropyrum pernix DSM 11879 AMP + phosphate + (deoxyribonucleotide)n+m
-
?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m the enzyme is inactive when ATP was substituted by AMP or NAD+ Aeropyrum pernix AMP + diphosphate + (deoxyribonucleotide)n+m
-
?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m the enzyme is inactive when ATP was substituted by AMP or NAD+ Aeropyrum pernix DSM 11879 AMP + diphosphate + (deoxyribonucleotide)n+m
-
?

Subunits

EC Number Subunits Comment Organism
6.5.1.1 monomer 1 * 69000, SDS-PAGE Aeropyrum pernix
6.5.1.1 monomer 1 * 69196, the authors refer to the protein of 619 amino acids that is later reannotated as a protein of 602 amino acids (67747.6 Da), calculated from sequence Aeropyrum pernix

Synonyms

EC Number Synonyms Comment Organism
6.5.1.1 APE1094
-
Aeropyrum pernix

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.5.1.1 70
-
optimum for nick-closing activity is above 70°C Aeropyrum pernix

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
6.5.1.1 65 80 in the nick-closing assay, the recombinant ligase shows more than 80% activity in the temperature range 65-80°C. Ligase activity declines at temperatures below 35°C. A drastic decrease in activity is observed between 80 and 90°C Aeropyrum pernix

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
6.5.1.1 100
-
stable for 60 min, half-life: 25 min Aeropyrum pernix

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5.1.1 7.5
-
optimum for nick-closing activity Aeropyrum pernix

pH Range

EC Number pH Minimum pH Maximum Comment Organism
6.5.1.1 7 8.2 80% of maximal activity is observed between pH 7.0 and 8.2 Aeropyrum pernix