Abstract Title:

Purification and properties of a stilbene synthase from induced cell suspension cultures of peanut.

Abstract Source:

J Biol Chem. 1984 Jun 10;259(11):6806-11. PMID: 6427224

Abstract Author(s):

A Schöppner, H Kindl


Stilbene synthase ( resveratrol -forming) converts one molecule of rho- coumaroyl -CoA and three molecules of malonyl-CoA into 3,4',5- trihydroxystilbene . Following selective induction of stilbene synthesis in cell suspension cultures of peanut (Arachis hypogaea), the enzyme was extracted and purified to apparent homogeneity by chromatography on DEAE-cellulose and hydroxylapatite. The enzyme was found to be a dimer of estimated Mr = 90,000 exhibiting under denaturing conditions a subunit Mr of approximately 45,000. The isoelectric point was determined with pI = 4.8. The enzyme's high selectivity towards rho- coumaroyl -CoA (Km = 2 microM) as substrate qualified it as resveratrol -forming stilbene synthase. Structurally related CoA esters, e.g. dihydro-rho- coumaroyl -CoA and cinnamoyl-CoA, were converted less than 1/10 as efficiently as rho- coumaroyl -CoA. Malonyl-CoA (Km = 10 microM) could not be substituted by acetyl-CoA. The purified enzyme was free of chalcone synthase activity. Antibodies raised against stilbene synthase were shown to be monospecific and not to cross-react with chalcone synthase.

Study Type : In Vitro Study

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