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Literature summary for 2.7.7.7 extracted from

  • Lapenna, A.; Stefan, A.; Hochkoeppler, A.
    ASFV DNA polymerase extends recessed DNAs with catalytic efficiencies outperforming those exerted on gapped DNA substrates (2020), Biochem. Biophys. Res. Commun., 534, 526-532 .
    View publication on PubMed
Search for more literature for 2.7.7.7

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 (DE3) African swine fever virus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn African swine fever virus
-
 diphosphate + DNAn+1
-
 ?
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn African swine fever virus Badajoz 1971 Vero-adapted
-
 diphosphate + DNAn+1
-
 ?

Organism

Organism UniProt Comment Textmining
African swine fever virus P42494
-
-
African swine fever virus Badajoz 1971 Vero-adapted P42494
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn
-
 African swine fever virus diphosphate + DNAn+1
-
 ?
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn the enzyme features poor filling activity of DNA gaps consisting of 15 bases, and exerts a more efficient action at the expense of DNA substrates containing a recessed end of equal length. Shortening the recessed end of DNA substrates decreases the rate of DNA elongation catalysed by ASFV Pol X. DNA binding is a step responsible for restraining the efficiency of ASFV Pol X catalytic action African swine fever virus diphosphate + DNAn+1
-
 ?
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn
-
 African swine fever virus Badajoz 1971 Vero-adapted diphosphate + DNAn+1
-
 ?
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn the enzyme features poor filling activity of DNA gaps consisting of 15 bases, and exerts a more efficient action at the expense of DNA substrates containing a recessed end of equal length. Shortening the recessed end of DNA substrates decreases the rate of DNA elongation catalysed by ASFV Pol X. DNA binding is a step responsible for restraining the efficiency of ASFV Pol X catalytic action African swine fever virus Badajoz 1971 Vero-adapted diphosphate + DNAn+1
-
 ?

Synonyms

Synonyms Comment Organism
ASFV DNA polymerase
-
 African swine fever virus
ASFV Pol X
-
 African swine fever virus