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Literature summary extracted from

  • Bolten, M.; Vahlensieck, C.; Lipp, C.; Leibundgut, M.; Ban, N.; Weber-Ban, E.
    Depupylase Dop requires inorganic phosphate in the active site for catalysis (2017), J. Biol. Chem., 292, 4044-4053 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.119 expressed from isopropyl beta-D-1-thiogalactopyranoside-inducible pET21 vector in Escherichia coli Rosetta Acidothermus cellulolyticus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.119 sitting drop vapor diffusion method Acidothermus cellulolyticus

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.119 Acidothermus cellulolyticus A0LU48
-
-
3.5.1.119 Acidothermus cellulolyticus 11B A0LU48
-
-
3.5.1.119 Acidothermus cellulolyticus ATCC 43068 A0LU48
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.119
-
 Acidothermus cellulolyticus

Cofactor

EC Number Cofactor Comment Organism Structure
3.5.1.119 ADP although the enzyme does not turn over ATP stoichiometrically with substrate, the active site nucleotide species in the enzyme is ADP and inorganic phosphate rather than ATP. Non-hydrolyzable analogs of ATP cannot support the enzymatic reaction Acidothermus cellulolyticus
3.5.1.119 ATP although the enzyme does not turn over ATP stoichiometrically with substrate, the active site nucleotide species in the enzyme is ADP and inorganic phosphate rather than ATP. Non-hydrolyzable analogs of ATP cannot support the enzymatic reaction Acidothermus cellulolyticus