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Literature summary for 3.5.1.119 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
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Cloned(Commentary)

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

Crystallization (Commentary)

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

Organism

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

Purification (Commentary)

Purification (Comment) Organism
-
 Acidothermus cellulolyticus

Cofactor

Cofactor Comment Organism Structure
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
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