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Literature summary for 4.4.1.26 extracted from

  • Yang, X.; Matsui, T.; Kodama, T.; Mori, T.; Zhou, X.; Taura, F.; Noguchi, H.; Abe, I.; Morita, H.
    Structural basis for olivetolic acid formation by a polyketide cyclase from Cannabis sativa (2016), FEBS J., 283, 1088-1106 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Cannabis sativa

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of free enzyme and in complex with olivetolic acid, to 1.32 and 1.70 A resolutions. The active-site cavity contains the pentyl-binding hydrophobic pocket and the polyketide binding site. Residues Tyr72 and His78 function as acid/base catalysts at the catalytic center. The enzyme may lack thioesterase and aromatase activities Cannabis sativa

Protein Variants

Protein Variants Comment Organism
F24L 49% of wild-type activity Cannabis sativa
H5L 36% of wild-type activity Cannabis sativa
H5Q 22% of wild-type activity Cannabis sativa
H5S 47% of wild-type activity Cannabis sativa
H78N 0% of wild-type activity Cannabis sativa
H78Q 0% of wild-type activity Cannabis sativa
H78S 0% of wild-type activity Cannabis sativa
I7F 64% of wild-type activity Cannabis sativa
I7L 85% of wild-type activity Cannabis sativa
V59M 65% of wild-type activity Cannabis sativa
Y27F 162% of wild-type activity Cannabis sativa
Y27L 48% of wild-type activity Cannabis sativa
Y27M 30% of wild-type activity Cannabis sativa
Y27W 37% of wild-type activity Cannabis sativa
Y72F 0% of wild-type activity Cannabis sativa

Organism

Organism UniProt Comment Textmining
Cannabis sativa I6WU39
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