The green tea gallocatechins, (-)-epigallocatechin-3-O-gallate (EGCG), and
(-)-epigallocatechin (EGC) were found to be inhibitors of Dopa decarboxylas
e (DDC). EG;CG; and EGC inactivate the enzyme in both a time- and concentra
tion-dependent manner and exhibit saturation of the rate of inactivation at
high concentrations, with efficiency of inactivation values (k(inact)/K-i)
of 868 and 1511 M-1 min(-1), respectively. In contrast, gallic acid behave
s as a weak inhibitor of DDC. Protection against inactivation by EGCG; and
EG;C was observed in the presence of the active site-directed inhibitor D-D
opa. Either EGCG or EGC induce changes in the absorbance and CD bands of th
e visible spectrum of enzyme-bound PLP. Taken together, these findings indi
cate the active site nature of the interaction of DDC with both polyphenols
. On the basis of the properties of the EGCG-inactivated enzyme, it can be
suggested that inactivation could be ascribed to a covalent modification of
not yet identified residue(s) of the active site of DDC. (C) 2001 Academic
Press.