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Literature summary for 2.7.7.31 extracted from

  • Marsin, S.; Forterre, P.
    A rolling circle replication initiator protein with a nucleotidyl-transferase activity encoded by the plasmid pGT5 from the hyperthermophilic archaeon Pyrococcus abyssi (1998), Mol. Microbiol., 27, 1183-1192.
    View publication on PubMed
Search for more literature for 2.7.7.31

Cloned(Commentary)

Cloned (Comment) Organism
-
 Pyrococcus abyssi

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ nucleotidyl-transferase activity of Rep75 is Mn2+ dependent, no nucleotidyl-transferase activity with Mg2+ Pyrococcus abyssi

Organism

Organism UniProt Comment Textmining
Pyrococcus abyssi O54003
-
-
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543 O54003
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus abyssi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dATP + DNAn terminal transferase activity at the 3'-OH extremity of the nicking site Pyrococcus abyssi diphosphate + DNAn+1
-
 ?
dATP + DNAn terminal transferase activity at the 3'-OH extremity of the nicking site Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543 diphosphate + DNAn+1
-
 ?

Synonyms

Synonyms Comment Organism
Rep75
-
 Pyrococcus abyssi

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
75
-
 the nucleotidyl-transferase activity of Rep75 is less thermophilic than its nicking activity (105°C) Pyrococcus abyssi

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
100
-
 1 h, no loss of activity after 1 h Pyrococcus abyssi