Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.6.2.2 extracted from

  • Hartmann, S.; Gubaev, A.; Klostermeier, D.
    Binding and hydrolysis of a single ATP is sufficient for N-gate closure and DNA supercoiling by gyrase (2017), J. Mol. Biol., 429, 3717-3729 .
    View publication on PubMed
Search for more literature for 5.6.2.2

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
D75N nucleotide-binding-deficient mutant of subunit GyrB Bacillus subtilis
E44Q ATP-hydrolysis-deficient mutant of subunit GyrB Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.85
-
 ATP mutant enzyme E44Q, at pH 7.5 and 37°C Bacillus subtilis
1.5
-
 ATP wild type enzyme, at pH 7.5 and 37°C Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, 10 mM used in assay conditions Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + relaxed pUC18 DNA enzyme that binds and hydrolyzes only one ATP undergoes nucleotide-induced N-gate closure and supercoils DNA Bacillus subtilis ADP + phosphate + supercoiled pUC18 DNA
-
 ?
ATP + supercoiled pUC18 DNA
-
 Bacillus subtilis ADP + phosphate + relaxed pUC18 DNA
-
 ?

Synonyms

Synonyms Comment Organism
GyrA subunit Bacillus subtilis
gyrase
-
 Bacillus subtilis
GyrB subunit Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.16
-
 ATP mutant enzyme E44Q, at pH 7.5 and 37°C Bacillus subtilis
3.4
-
 ATP wild type enzyme, at pH 7.5 and 37°C Bacillus subtilis