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Literature summary for 5.6.2.1 extracted from

  • Lu, J.; Wang, W.; Tan, G.; Landry, A.P.; Yi, P.; Si, F.; Ren, Y.; Ding, H.
    Escherichia coli topoisomerase I is an iron and zinc binding protein (2011), Biometals, 24, 729-736.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.2.1

Inhibitors

Inhibitors Comment Organism Structure
Fe2+ competes with Zn2+. TopA is an iron and zinc binding protein. Whereas the zinc-bound TopA is fully active to relax the negatively supercoiled DNA, the iron-bound TopA has little or no enzyme activity. The C-terminal zinc-binding region, but not the N-terminal fragment, of TopA, is involved in the iron binding Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli
Zn2+ TopA is an iron and zinc binding protein, it contains a C-terminal zinc-binding region that is required for relaxation of the negatively supercoiled DNA. Whereas the zinc-bound TopA is fully active to relax the negatively supercoiled DNA, the iron-bound TopA has little or no enzyme activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 gene topA
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information topoisomerase I cleaves and rejoins one strand of double-stranded DNA to relax the negatively supercoiled DNA Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
More TopA contains an N-terminal catalytic fragment and a C-terminal zinc-binding region that is required for relaxation of the negatively supercoiled DNA Escherichia coli

Synonyms

Synonyms Comment Organism
TopA
-
 Escherichia coli
Topoisomerase I
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Escherichia coli

General Information

General Information Comment Organism
additional information TopA contains an N-terminal catalytic fragment and a C-terminal zinc-binding region that is required for relaxation of the negatively supercoiled DNA Escherichia coli