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

BRENDA support

Literature summary for 4.2.3.117 extracted from

  • Hyat, D.C.; Croteau, R.
    Mutational analysis of a monoterpene synthase reaction: altered catalysis through directed mutagenesis of (-)-pinene synthase from Abies grandis (2005), Arch. Biochem. Biophys., 439, 222-233.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
modeling of amino acid sequence onto the crystal structures of tobacco 5-epi-aristolochene synthase and bornyl diphosphate synthase and comparison with (-)-pinene synthase Abies grandis

Protein Variants

Protein Variants Comment Organism
additional information replacement of selected amino acid residues in (-)-pinene synthase with the corresponding residues from (-)-camphene synthase in an effort to identify the amino acids responsible for the catalytic differences. The approach produces an enzyme in which more than half of the product is channeled through an alternative pathway. Several (-)-pinene synthase to (-)-camphene synthase amino acid substitutions are necessary before catalysis is significantly altered Abies grandis

Organism

Organism UniProt Comment Textmining
Abies grandis Q948Z0
-
-

Synonyms

Synonyms Comment Organism
(-)-pinene synthase
-
Abies grandis