Catalytic properties of alcohol acyltransferase in different strawberry species and cultivars.
The substrate specificity of alcohol acyltransferase (AAT) enzymes from different strawberry varieties was studied. Proteins with AAT activity from fruits of Fragaria x ananassa Duch. cv. Oso Grande were purified to apparent homogeneity and used for kinetic studies with different straight-chain alcohols and acyl-CoAs. K(m) values obtained for Oso Grande enzyme with six different alcohols, using acetyl-CoA as cosubstrate, decreased with increasing length of the alcohol chain. In similar experiments the increase in the acyl-CoA carbon chain was also found to be correlated with a higher substrate specificity. Heptanol (K(m) = 0.73 mM) and hexanoyl-CoA (K(m) = 0.41 mM) were the best substrates for Oso Grande AAT. Comparative catalytic studies were carried out with AAT partially purified extracts from the wild type Fragaria vesca and five commercial strawberry varieties: Tudnew, Carisma, Camarosa, Sweet Charlie, and Eris. The specificities of these enzymes toward five selected alcohols and acyl-CoAs reflected interesting cultivar differences.
Olías
Raquel
R
Departamento Physiology and Technology of Plant Products, Instituto de la Grasa, CSIC, Padre García Tejero 4, 41012 Sevilla, Spain.
Pérez
Ana G
AG
Sanz
Carlos
C
D000217:Acyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D002384:Catalysis; D005638:Fruit / Q000201:enzymology*; D007700:Kinetics; D010940:Plant Proteins; D027824:Rosaceae / Q000201:enzymology*; D013045:Species Specificity; D013379:Substrate Specificity
D010940:Plant Proteins; D000217:Acyltransferases; C411082:alcohol acyltransferase, Fragaria ananassa