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PLANT PHYSIOLOGY , Vol 107, Issue 2 545-552, Copyright © 1995 by American Society of Plant Biologists
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BIOCHEMISTRY AND ENZYMOLOGY |
Partial Purification and Characterization of Hydroxycinnamoyl-Coenzyme A:Tyramine Hydroxycinnamoyltransferase from Cell Suspension Cultures of Solanum tuberosum
H. Hohlfeld, W. Schurmann, D. Scheel and D. Strack
Institut fur Pflanzenbiochemie, Abteilung Sekundarstoffwechsel, Weinberg 3, D-06120, Halle (Saale), Germany(H.H., W.S., D.Strack)
A pathogen elicitor-inducible soluble acyltransferase (tyramine
hydroxycinnamoyltransferase [THT], EC 2.3.1), which catalyzes the transfer
of hydroxycinnamic acids from hydroxycinnamoyl-coenzyme A (CoA) esters to
tyramine in the formation of N-hydroxycinnamoyltyramine, was partially
purified with a 380-fold enrichment and a 6% recovery from cell-suspension
cultures of potato (Solanum tuberosum L. cv Datura). The enzyme showed
specific activities of 33 mkat (kg protein)-1 (formation of
feruloyltyramine). The apparent native Mr was found to be approximately
49,000. Highest activity was at pH 6.8 in K-phosphate. The isoelectric
point of the enzyme was approximately pH5.2. The apparent energy of
activation was calculated to be 96 kJ mol-1. The enzyme activity was
stimulated more than 5-fold by 10 mM Ca2+ or Mg2+. The apparent Km values
were 36 [mu]M for feruloyl-CoA and 85 and 140 [mu]M for cinnamoyl- and
4-coumaroyl-CoA, respectively. The Km value for tyramine in the presence of
feruloyl-CoA was 22 [mu]M. In the presence of 4-coumaroyl-CoA, however, the
Km for tyramine increased to about 230 [mu]M. The mode of action was an
iso-ordered bi bi mechanism in which A, B, P, and Q equal
hydroxycinnamoyl-CoA, tyramine, N-hydroxycinnamoyltyramine, and CoA,
respectively. Thus, the reaction occurred in a ternary complex of the
enzyme and substrates. The equilibrium constant of the reaction was
determined to be 1.3 x 104. This gave a [delta]G[deg][prime] eq value of
-23.5 kJ mol-1.
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