A comprehensive survey of the extensive literature relevant to the evolutio
n, physiology, biochemistry, regulation, and genetic engineering applicatio
ns of plant aromatic L-amino acid decarboxylases (AADCs) is presented. AADC
s catalyze the pyridoxal-5'-phosphate (PLP)-dependent decarboxylation of se
lect aromatic L-amino acids in plants, mammals, and insects. Two plant AADC
s, L-tryptophan decarboxylase (TDC) and L-tyrosine decarboxylase (TYDC), ha
ve attracted considerable attention because of their role in the biosynthes
is of pharmaceutically important monoterpenoid indole alkaloids and benzyli
soquinoline alkaloids, respectively. Although plant and animal AADCs share
extensive amino acid homology, the enzymes display striking differences in
their substrate specificities. AADCs from mammals and insects accept a broa
d range of aromatic L-amino acids, whereas TDC and TYDC from plants exhibit
exclusive substrate specificity for L-amino acids with either indole or ph
enol side chains, but not both. Recent biochemical and kinetic studies on a
nimal AADCs support basic features of the classic AADC reaction mechanism.
The catalytic mechanism involves the formation of a Schiff base between PLP
and an invariable lysine residue, followed by a transaldimination reaction
with an aromatic L-amino acid substrate. Both TDC and TYDC are primarily r
egulated at the transcriptional level by developmental and environmental fa
ctors. However, the putative post-translational regulation of TDC via the u
biquitin pathway, by an ATP-dependent proteolytic process, has also been su
ggested. Isolated TDC and TYDC genes have been used to genetically alter th
e regulation of secondary metabolic pathways derived from aromatic amino ac
ids in several plant species. The metabolic modifications include increased
serotonin levers, reduced indole glucosinolate levels, redirected shikimat
e metabolism, increased indole alkaloid levels, and increased cell wall-bou
nd tyramine levels. (C) 2000 Elsevier Science Ltd. All rights reserved.