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Literature summary for 5.6.2.1 extracted from

  • Stahley, M.R.; Stivers, J.T.
    Mechanism and specificity of DNA strand exchange catalyzed by vaccinia DNA topoisomerase type I (2010), Biochemistry, 49, 2786-2795.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.2.1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information analysis of kinetic and thermodynamic parameters for strand annealing of purified vaccinia Topo I-DNA covalent complex containing a single-strand overhang, and comparison to the same overhang duplex in the absence of vTopo, overview Vaccinia virus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Vaccinia virus type I DNA topoisomerase from vaccinia virus, vTopo, forms a reversible covalent 3'-phosphotyrosyl linkage with a single strand of duplex DNA at the preferred sequence 5'-(C/T) CCTTp-/-N-1N-2N-3-3'. Site-specific DNA cleavage and ligation chemistry. Oscillation between an open and closed state of the covalently bound enzyme is likely important for regulating the number of DNA superhelical turns that are removed during the lifetime of the covalent complex with supercoiled substrates ?
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 ?

Organism

Organism UniProt Comment Textmining
Vaccinia virus
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information type I DNA topoisomerase from vaccinia virus, vTopo, forms a reversible covalent 3'-phosphotyrosyl linkage with a single strand of duplex DNA at the preferred sequence 5'-(C/T) CCTTp-/-N-1N-2N-3-3'. Site-specific DNA cleavage and ligation chemistry. Oscillation between an open and closed state of the covalently bound enzyme is likely important for regulating the number of DNA superhelical turns that are removed during the lifetime of the covalent complex with supercoiled substrates Vaccinia virus ?
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 ?

Synonyms

Synonyms Comment Organism
DNA topoisomerase type I
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 Vaccinia virus
Topo I
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 Vaccinia virus
Type I DNA topoisomerase
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 Vaccinia virus
vTopo
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 Vaccinia virus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Vaccinia virus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Vaccinia virus

General Information

General Information Comment Organism
additional information the enzyme-DNA covalent adduct is recombinogenic in cells, because the nicked strand downstream of the cleavage site can dissociate and be replaced by another DNA strand, potentially resulting in genome rearrangements if the enzyme executes strand ligation. The enzyme plays an active role in strand exchange, either by altering the kinetics or thermodynamics of DNA strand binding, or by serving as a proofreading gate to prevent ligation of incoming DNA strands containing mismatches. Topo I-mediated strand exchange can be divided into two distinct steps: (1) a strand binding step, which involves replacement of the nicked, base paired DNA strand with a new incoming strand, and (2) a strand ligation step, which results in covalent attachment of the new DNA strand at the vTopo cleavage site. Oscillation between an open and closed state of the covalently bound enzyme is likely important for regulating the number of DNA superhelical turns that are removed during the lifetime of the covalent complex with supercoiled substrates. vTopo also resolves pre-formed Holliday junctions that contain the consensus cleavage sequence, and when recombinantly expressed in Escherichia coli, promotes illegitimate recombination Vaccinia virus