Species: Rubus idaeus
Subunit composition of benzalacetone synthase = [BAS subunit]2
The enzyme catalyzing the decarboxylative condensation of p-coumaroyl-CoA and malonyl-CoA to form p-hydroxybenzalacetone has been partially purified from berries of raspberry (Rubus idaeus). Assessing the substrate specificity and effects of inhibitors it was concluded that benzalacetone synthase (BST) represents a unique enzyme and differs from the closely related enzymes chalcone synthase (CHS) and stilbene synthase (STS) that also operate in this plant [BorejszaWysocki96].
note of curator:
This enzyme may or may not be identical with 4-hydroxybenzalacetone synthase. Although very similar to 4-hydroxybenzalacetone synthase with regard to catalytic properties this enzyme remains to be characterized on a molecular level to confirm identity with 4-hydroxybenzalacetone synthase (personal communication: G. Hrazdina, November 2012)
Molecular Weight of Polypeptide: 41.5 kD (experimental) [BorejszaWysocki96 ]
Molecular Weight of Multimer: 83 kD (experimental) [BorejszaWysocki96]
pI: 5.3 [BorejszaWysocki96]
Enzymatic reaction of: benzalacetone synthase
EC Number: 18.104.22.168
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is favored in the direction shown.
In Pathways: raspberry ketone biosynthesis
pH(opt): 8.0 [BorejszaWysocki96]
BorejszaWysocki96: Borejsza-Wysocki W, Hrazdina G (1996). "Aromatic Polyketide Synthases (Purification, Characterization, and Antibody Development to Benzalacetone Synthase from Raspberry Fruits)." Plant Physiol 110(3);791-799. PMID: 12226219
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493