title: Catalytic properties of alcohol acyltransferase in different strawberry species and cultivars.
abstract: 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.
authors.affiliation: Departamento Physiology and Technology of Plant Products, Instituto de la Grasa, CSIC, Padre García Tejero 4, 41012 Sevilla, Spain.
authors.forename: Raquel
authors.initials: R
authors.lastname: Olías
authors.forename: Ana G
authors.initials: AG
authors.lastname: Pérez
authors.forename: Carlos
authors.initials: C
authors.lastname: Sanz
mesh_terms: 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
chemical_list: D010940:Plant Proteins; D000217:Acyltransferases; C411082:alcohol acyltransferase, Fragaria ananassa