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Literature summary extracted from

  • Manjunath, K.; Jeyakanthan, J.; Sekar, K.
    Catalytic pathway, substrate binding and stability in SAICAR synthetase: A structure and molecular dynamics study (2015), J. Struct. Biol., 191, 22-31.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.2.6 overexpression in Escherichia coli Pyrococcus horikoshii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.2.6 co-crystallization of SAICAR synthetase from Pyrococcus horikoshii with substrates and other nucleotides produces eight ligand bound structures, five in C2221 and three in H3 space groups. These ligand bound complexes have minor structural deviations compared to their corresponding apo structures. In most of the structures the hydrolyzed product of the nucleotide triphosphates are bound to the enzyme Pyrococcus horikoshii

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.6 Pyrococcus horikoshii O57978
-
-
6.3.2.6 Pyrococcus horikoshii OT-3 O57978
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.2.6
-
 Pyrococcus horikoshii

Synonyms

EC Number Synonyms Comment Organism
6.3.2.6 PH0239 locus name Pyrococcus horikoshii
6.3.2.6 SAICAR synthetase
-
 Pyrococcus horikoshii