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

BRENDA support

Literature summary for 3.6.1.13 extracted from

  • Yoshiba, S.; Nakagawa, N.; Masui, R.; Shibata, T.; Inoue, Y.; Yokoyama, S.; Kuramitsu, S.
    Overproduction, crystallization and preliminary diffraction data of ADP-ribose pyrophosphatase from Thermus thermophilus HB8 (2003), Acta Crystallogr. Sect. D, 59, 1840-1842.
    View publication on PubMed
Search for more literature for 3.6.1.13

Cloned(Commentary)

Cloned (Comment) Organism
overproduction in Escherichia coli Thermus thermophilus

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallized in absence or presence of ADP-ribose by hanging-drop vapour-diffusion method. 1.5 A resolution from the apo form using synchrotron radiation and 2.0 A resolution from the complexed form. Both crystals belong to space group P3(1)21 or P3(2)21 and contain one molecule in the asymmetric unit Thermus thermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on Mg2+ or Zn2+ Thermus thermophilus
Zn2+ dependent on Mg2+ or Zn2+ Thermus thermophilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
 gel filtration Thermus thermophilus

Organism

Organism UniProt Comment Textmining
Thermus thermophilus Q84CU3
-
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 Q84CU3
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Thermus thermophilus

Subunits

Subunits Comment Organism
dimer
-
 Thermus thermophilus